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Volumn 46, Issue C, 1999, Pages 151-208

Heparin in Inflammation: Potential Therapeutic Applications beyond Anticoagulation

Author keywords

[No Author keywords available]

Indexed keywords

HEPARIN; INTEGRIN; SELECTIN;

EID: 0032610504     PISSN: 10543589     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1054-3589(08)60471-8     Document Type: Chapter
Times cited : (227)

References (350)
  • 1
    • 0028226536 scopus 로고
    • Leucocyte-endothelial interactions and regulation of leucocyte migration
    • Adams D.H., and Shaw S. Leucocyte-endothelial interactions and regulation of leucocyte migration. Lancet 343 (1994) 831-836
    • (1994) Lancet , vol.343 , pp. 831-836
    • Adams, D.H.1    Shaw, S.2
  • 2
    • 0028124722 scopus 로고
    • Lymphocyte recirculation and homing: Roles of adhesion molecules and chemoattractants
    • Ager A. Lymphocyte recirculation and homing: Roles of adhesion molecules and chemoattractants. Trends Cell Biol. 4 (1994) 326-333
    • (1994) Trends Cell Biol. , vol.4 , pp. 326-333
    • Ager, A.1
  • 3
    • 0026596865 scopus 로고
    • Effects of inhaled heparin on immunologic and nonimmunologic bronchoconstrictor responses in sheep
    • Ahmed T., Abraham W.M., and D'Brot J. Effects of inhaled heparin on immunologic and nonimmunologic bronchoconstrictor responses in sheep. Am. Rev. Respir. Dis. 145 (1992) 566-570
    • (1992) Am. Rev. Respir. Dis. , vol.145 , pp. 566-570
    • Ahmed, T.1    Abraham, W.M.2    D'Brot, J.3
  • 4
    • 0030968807 scopus 로고    scopus 로고
    • Inhibition of antigen-induced acute bronchoconstriction, airway hyperresponsiveness, and mast cell degranulation by a nonanticoagulant heparin: Comparison with a low molecular weight heparin
    • Ahmed T., Campo C., Abraham M.K., Molinari J.F., Abraham W.M., Ashkin D., Syriste T., Andersson L.O., and Svahn C.M. Inhibition of antigen-induced acute bronchoconstriction, airway hyperresponsiveness, and mast cell degranulation by a nonanticoagulant heparin: Comparison with a low molecular weight heparin. Am. J. Respir. Crit. Care Med. 155 (1997) 1848-1855
    • (1997) Am. J. Respir. Crit. Care Med. , vol.155 , pp. 1848-1855
    • Ahmed, T.1    Campo, C.2    Abraham, M.K.3    Molinari, J.F.4    Abraham, W.M.5    Ashkin, D.6    Syriste, T.7    Andersson, L.O.8    Svahn, C.M.9
  • 5
    • 0027159470 scopus 로고
    • Preventing bronchoconstriction in exerciseinduced asthma with inhaled heparin
    • Ahmed T., Garrigo J., and Danta I. Preventing bronchoconstriction in exerciseinduced asthma with inhaled heparin. N. Engl. J. Med. 329 (1993) 90-95
    • (1993) N. Engl. J. Med. , vol.329 , pp. 90-95
    • Ahmed, T.1    Garrigo, J.2    Danta, I.3
  • 6
    • 0027321980 scopus 로고
    • Inhibition of antigen-induced airway and cutaneous responses by heparin: A pharmacodynamic study
    • Ahmed T., Syriste T., Lucio J., Abraham W., Robinson M., and D'Brot J. Inhibition of antigen-induced airway and cutaneous responses by heparin: A pharmacodynamic study. J. Appl. Physiol. 74 (1993) 1492-1498
    • (1993) J. Appl. Physiol. , vol.74 , pp. 1492-1498
    • Ahmed, T.1    Syriste, T.2    Lucio, J.3    Abraham, W.4    Robinson, M.5    D'Brot, J.6
  • 8
    • 0031031312 scopus 로고    scopus 로고
    • Inflammation and Alzheimer's disease: Mechanisms and therapeutic strategies
    • Aisen P.S. Inflammation and Alzheimer's disease: Mechanisms and therapeutic strategies. Gerontology 43 (1997) 143-149
    • (1997) Gerontology , vol.43 , pp. 143-149
    • Aisen, P.S.1
  • 9
    • 0028231065 scopus 로고
    • Adhesion molecules and inflammatory injury
    • Albelda S.M., Smith C.W., and Ward P.A. Adhesion molecules and inflammatory injury. FASEB J. 8 (1994) 504-512
    • (1994) FASEB J. , vol.8 , pp. 504-512
    • Albelda, S.M.1    Smith, C.W.2    Ward, P.A.3
  • 10
    • 0029826160 scopus 로고    scopus 로고
    • Interactions through Lselectin between leukocytes and adherent leukocytes nucleate rolling adhesions on selectins and VCAM-1 in shear flow
    • Alon R., Fuhlbrigge R.C., Finger E.B., and Springer T.A. Interactions through Lselectin between leukocytes and adherent leukocytes nucleate rolling adhesions on selectins and VCAM-1 in shear flow. J. Cell Biol. 135 (1996) 849-865
    • (1996) J. Cell Biol. , vol.135 , pp. 849-865
    • Alon, R.1    Fuhlbrigge, R.C.2    Finger, E.B.3    Springer, T.A.4
  • 11
    • 0025202071 scopus 로고
    • Pharmacological characterization of polycation-induced rat hind-paw oedema
    • Antunes E., Mariano M., Cirino G., Levi S., and DeNucci G. Pharmacological characterization of polycation-induced rat hind-paw oedema. Br. J. Pharmacol. 101 (1990) 986-990
    • (1990) Br. J. Pharmacol. , vol.101 , pp. 986-990
    • Antunes, E.1    Mariano, M.2    Cirino, G.3    Levi, S.4    DeNucci, G.5
  • 13
    • 0029745749 scopus 로고    scopus 로고
    • The development of articular cartilage. 2. The spatial and temporal patterns of glycosaminoglycans and small leucine-rich proteoglycans
    • Archer C.W., Morrison E.H., Bayliss M.T., and Ferguson M.W.J. The development of articular cartilage. 2. The spatial and temporal patterns of glycosaminoglycans and small leucine-rich proteoglycans. J. Anat. 189 (1996) 23-35
    • (1996) J. Anat. , vol.189 , pp. 23-35
    • Archer, C.W.1    Morrison, E.H.2    Bayliss, M.T.3    Ferguson, M.W.J.4
  • 14
    • 0027419007 scopus 로고
    • Sulfated polysaccharides in inflammation
    • Arfors K.E., and Ley K. Sulfated polysaccharides in inflammation. J. Lab. Clin. Med. 121 (1993) 201-202
    • (1993) J. Lab. Clin. Med. , vol.121 , pp. 201-202
    • Arfors, K.E.1    Ley, K.2
  • 15
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes
    • Arispe N., Pollard H.B., and Rojas E. Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes. Proc. Natl. Acad. Sci. USA 90 (1993) 10573-10577
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10573-10577
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 16
    • 0026788144 scopus 로고
    • Evidence for two classes of carbohydrate binding sites on selectins
    • Asa D., Gant T., Oda Y., and Brandley B.K. Evidence for two classes of carbohydrate binding sites on selectins. Glycobiology 2 (1992) 395-400
    • (1992) Glycobiology , vol.2 , pp. 395-400
    • Asa, D.1    Gant, T.2    Oda, Y.3    Brandley, B.K.4
  • 17
    • 0030045809 scopus 로고    scopus 로고
    • Chemokines as mediators of allergic inflammation
    • Bacon K.B., and Schall T.J. Chemokines as mediators of allergic inflammation. Int. Arch. Allergy Immunol. 109 (1996) 97-109
    • (1996) Int. Arch. Allergy Immunol. , vol.109 , pp. 97-109
    • Bacon, K.B.1    Schall, T.J.2
  • 18
    • 0031397116 scopus 로고    scopus 로고
    • A placebo-controlled study of intravesical pentosanpolysulfate for the treatment of interstitial cystitis
    • Bade J.J., Laseur M., Nieuwenburg A., van der Weele L.T., and Mensink H.J. A placebo-controlled study of intravesical pentosanpolysulfate for the treatment of interstitial cystitis. Br. J. Urol. 79 (1997) 168-171
    • (1997) Br. J. Urol. , vol.79 , pp. 168-171
    • Bade, J.J.1    Laseur, M.2    Nieuwenburg, A.3    van der Weele, L.T.4    Mensink, H.J.5
  • 19
    • 0027493879 scopus 로고
    • Inhibition of the human leukocyte endopeptidases elastase and cathepsin G and of porcine pancreatic elastase by N-oleoyl derivatives of heparin
    • Baici A., Diczházi C., Neszmélyi A., Móczár E., and Hornebeck W. Inhibition of the human leukocyte endopeptidases elastase and cathepsin G and of porcine pancreatic elastase by N-oleoyl derivatives of heparin. Biochem. Pharmacol. 46 (1993) 1545-1549
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 1545-1549
    • Baici, A.1    Diczházi, C.2    Neszmélyi, A.3    Móczár, E.4    Hornebeck, W.5
  • 20
    • 0018824895 scopus 로고
    • Inhibition of human elastase from polymorphonuclear leucocytes by a glycosaminoglycan polysulfate (Arteparon)
    • Baici A., Salgam P., Fehr K., and Böni A. Inhibition of human elastase from polymorphonuclear leucocytes by a glycosaminoglycan polysulfate (Arteparon). Biochem. Pharmacol. 29 (1980) 1723-1727
    • (1980) Biochem. Pharmacol. , vol.29 , pp. 1723-1727
    • Baici, A.1    Salgam, P.2    Fehr, K.3    Böni, A.4
  • 21
    • 0030610942 scopus 로고    scopus 로고
    • A beta (1-40) prevents heparanasecatalyzed degradation of heparan sulfate glycosaminoglycans and proteoglycans in vitro: A role for heparan sulfate proteoglycans turnover in Alzheimer's disease
    • Bame K.J., Danda J., Hassall A., and Tumova S. A beta (1-40) prevents heparanasecatalyzed degradation of heparan sulfate glycosaminoglycans and proteoglycans in vitro: A role for heparan sulfate proteoglycans turnover in Alzheimer's disease. J. Biol. Chem. 272 (1997) 17005-17011
    • (1997) J. Biol. Chem. , vol.272 , pp. 17005-17011
    • Bame, K.J.1    Danda, J.2    Hassall, A.3    Tumova, S.4
  • 22
    • 0028982172 scopus 로고
    • Distinct roles of L-selectin and integrins α4β7 and LFA-1 in lymphocyte homing to Peyer's Patch-HEV in situ: The multistep model confirmed and refined
    • Bargatze R.F., Jutila M.A., and Butcher E.C. Distinct roles of L-selectin and integrins α4β7 and LFA-1 in lymphocyte homing to Peyer's Patch-HEV in situ: The multistep model confirmed and refined. Immunity 3 (1995) 99-108
    • (1995) Immunity , vol.3 , pp. 99-108
    • Bargatze, R.F.1    Jutila, M.A.2    Butcher, E.C.3
  • 23
    • 0028143514 scopus 로고
    • Neutrophils roll on adherent neutrophils bound to cytokine-induced endothelial cells via L-selectin on the rolling cells
    • Bargatze R.F., Kurk S., Butcher E.C., and Jutila M.A. Neutrophils roll on adherent neutrophils bound to cytokine-induced endothelial cells via L-selectin on the rolling cells. J. Exp. Med. 180 (1994) 1785-1792
    • (1994) J. Exp. Med. , vol.180 , pp. 1785-1792
    • Bargatze, R.F.1    Kurk, S.2    Butcher, E.C.3    Jutila, M.A.4
  • 26
    • 0027413487 scopus 로고
    • Effect of heparin, dermatan sulfate, and related oligo-derivatives on human polymorphonuclear leukocyte functions
    • Bazzoni G., Nunez A.B., Mascellani G., Bianchini P., Dejana E., and Del Maschio A. Effect of heparin, dermatan sulfate, and related oligo-derivatives on human polymorphonuclear leukocyte functions. J. Lab. Clin. Med. 121 (1993) 268-275
    • (1993) J. Lab. Clin. Med. , vol.121 , pp. 268-275
    • Bazzoni, G.1    Nunez, A.B.2    Mascellani, G.3    Bianchini, P.4    Dejana, E.5    Del Maschio, A.6
  • 29
    • 0021913331 scopus 로고
    • Structural characterization of the oligosaccharides formed by depolymerization of heparin with nitrous acid
    • Bienkowski M.J., and Conrad H.E. Structural characterization of the oligosaccharides formed by depolymerization of heparin with nitrous acid. J. Biol. Chem. 260 (1985) 356-365
    • (1985) J. Biol. Chem. , vol.260 , pp. 356-365
    • Bienkowski, M.J.1    Conrad, H.E.2
  • 30
    • 0029071894 scopus 로고
    • Cardioprotective effects of heparin or N-acetylheparin in an in vivo model of myocardial ischaemic and reperfusion injury
    • Black S.C., Garalinski M.R., Friederichs G.S., Kilgore K.S., Driscoll E.M., and Lucchesi B.R. Cardioprotective effects of heparin or N-acetylheparin in an in vivo model of myocardial ischaemic and reperfusion injury. Cardiovascular Res. 29 (1995) 629-636
    • (1995) Cardiovascular Res. , vol.29 , pp. 629-636
    • Black, S.C.1    Garalinski, M.R.2    Friederichs, G.S.3    Kilgore, K.S.4    Driscoll, E.M.5    Lucchesi, B.R.6
  • 31
    • 0028605282 scopus 로고
    • Only simultaneous blocking of the L- and P-selectin completely inhibits neutrophil migration into mouse peritoneum
    • Bosse R., and Vestweber D. Only simultaneous blocking of the L- and P-selectin completely inhibits neutrophil migration into mouse peritoneum. Eur. J. Immunol. 24 (1994) 3019-3024
    • (1994) Eur. J. Immunol. , vol.24 , pp. 3019-3024
    • Bosse, R.1    Vestweber, D.2
  • 32
    • 0027509462 scopus 로고
    • Glycosaminoglycans and the regulation of blood coagulation
    • Bourin M.C., and Lindahl U. Glycosaminoglycans and the regulation of blood coagulation. Biochem. J. 289 2 (1993) 313-330
    • (1993) Biochem. J. , vol.289 , Issue.2 , pp. 313-330
    • Bourin, M.C.1    Lindahl, U.2
  • 33
    • 0027434514 scopus 로고
    • Heparin inhibits the immediate response to antigen in the skin and lungs of allergic subjects
    • Bowler S.D., Smith S.M., and Lavercombe P.S. Heparin inhibits the immediate response to antigen in the skin and lungs of allergic subjects. Am. Rev. Respir. Dis. 147 (1993) 160-163
    • (1993) Am. Rev. Respir. Dis. , vol.147 , pp. 160-163
    • Bowler, S.D.1    Smith, S.M.2    Lavercombe, P.S.3
  • 34
    • 0022504141 scopus 로고
    • Heparin-induced platelet aggregation: Dose-response relationships for a low molecular weight heparin derivative (PK10169) and its subfractions
    • Brace L.D., and Fareed J. Heparin-induced platelet aggregation: Dose-response relationships for a low molecular weight heparin derivative (PK10169) and its subfractions. Thromb. Res. 42 (1986) 769-782
    • (1986) Thromb. Res. , vol.42 , pp. 769-782
    • Brace, L.D.1    Fareed, J.2
  • 35
    • 0028071928 scopus 로고
    • Entry of naive CD4 T cells into peripheral lymph nodes requires L-selectin
    • Bradley L.M., Watson S.R., and Swain S.L. Entry of naive CD4 T cells into peripheral lymph nodes requires L-selectin. J. Exp. Med. 180 (1994) 2401-2406
    • (1994) J. Exp. Med. , vol.180 , pp. 2401-2406
    • Bradley, L.M.1    Watson, S.R.2    Swain, S.L.3
  • 36
    • 0023840720 scopus 로고
    • Purification of rat liver N-heparan sulfate sulfotransferase
    • Brandan E., and Hirschberg C.B. Purification of rat liver N-heparan sulfate sulfotransferase. J. Biol. Chem. 263 (1988) 2417-2422
    • (1988) J. Biol. Chem. , vol.263 , pp. 2417-2422
    • Brandan, E.1    Hirschberg, C.B.2
  • 37
    • 0022633567 scopus 로고
    • Modification of lymphocyte migration by sulfated polysaccharides
    • Brenan M., and Parish C.R. Modification of lymphocyte migration by sulfated polysaccharides. Eur. J. Immunol. 16 (1986) 423-430
    • (1986) Eur. J. Immunol. , vol.16 , pp. 423-430
    • Brenan, M.1    Parish, C.R.2
  • 40
    • 0027407521 scopus 로고
    • Binding of secreted human neuroblasoma proteoglycans to the Alzheimer's amyloid A4 peptide
    • Buee L., Ding W., Delacourte A., and Fillit H.M. Binding of secreted human neuroblasoma proteoglycans to the Alzheimer's amyloid A4 peptide. Brain Res. 601 (1993) 154-163
    • (1993) Brain Res. , vol.601 , pp. 154-163
    • Buee, L.1    Ding, W.2    Delacourte, A.3    Fillit, H.M.4
  • 41
    • 0029572426 scopus 로고
    • Coagulation and platelet activation pathways: A review of the key components and the way in which these can be manipulated
    • Buller H.R., and Ten Cate T. Coagulation and platelet activation pathways: A review of the key components and the way in which these can be manipulated. Eur. Heart J. 16 Suppl. L (1995) 8-10
    • (1995) Eur. Heart J. , vol.16 , Issue.SUPPL. L , pp. 8-10
    • Buller, H.R.1    Ten Cate, T.2
  • 42
    • 0026342111 scopus 로고
    • Leukocyte-endothelial cell recognition: Three (or more) steps to specificity and diversity
    • Butcher E.C. Leukocyte-endothelial cell recognition: Three (or more) steps to specificity and diversity. Cell 67 (1991) 1033-1036
    • (1991) Cell , vol.67 , pp. 1033-1036
    • Butcher, E.C.1
  • 43
    • 0030001675 scopus 로고    scopus 로고
    • Lymphocyte homing and homeostasis
    • Butcher E.C., and Picker L.J. Lymphocyte homing and homeostasis. Science 272 (1996) 60-66
    • (1996) Science , vol.272 , pp. 60-66
    • Butcher, E.C.1    Picker, L.J.2
  • 45
    • 0029954523 scopus 로고    scopus 로고
    • Biology of chemokine and classical chemoattractant receptors: Differential requirements for adhesion-triggering versus chemotactic responses in lymphoid cells
    • Campbell J.J., Qin S., Bacin K.B., Mackay C.R., and Butcher E.C. Biology of chemokine and classical chemoattractant receptors: Differential requirements for adhesion-triggering versus chemotactic responses in lymphoid cells. J. Cell Biol. 134 (1996) 255-266
    • (1996) J. Cell Biol. , vol.134 , pp. 255-266
    • Campbell, J.J.1    Qin, S.2    Bacin, K.B.3    Mackay, C.R.4    Butcher, E.C.5
  • 46
    • 0027940609 scopus 로고
    • Biosynthesis of heparin/heparan sulfate-Purification of the D-glucuronyl C-5 epimerase from bovine liver
    • Campbell P., Hannesson H.H., Sandback D., Roden L., Lindahl U., and Li J.P. Biosynthesis of heparin/heparan sulfate-Purification of the D-glucuronyl C-5 epimerase from bovine liver. J. Biol. Chem. 269 (1994) 26953-26958
    • (1994) J. Biol. Chem. , vol.269 , pp. 26953-26958
    • Campbell, P.1    Hannesson, H.H.2    Sandback, D.3    Roden, L.4    Lindahl, U.5    Li, J.P.6
  • 47
    • 0024584913 scopus 로고
    • Molecular modeling of proteinglycosaminoglycan interactions
    • Cardin A.D., and Weintraub H.J.R. Molecular modeling of proteinglycosaminoglycan interactions. Arteriosclerosis 9 (1989) 21-32
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.R.2
  • 48
    • 17544378558 scopus 로고    scopus 로고
    • The cytoplasmic domain of syndecan-1 is required for cytoskeleton association but not detergent insolubility-Identification of essential cytoplasmic domain residues
    • Carey D.J., Bendt K.M., and Stahl R.C. The cytoplasmic domain of syndecan-1 is required for cytoskeleton association but not detergent insolubility-Identification of essential cytoplasmic domain residues. J. Biol. Chem. 271 (1996) 15253-15260
    • (1996) J. Biol. Chem. , vol.271 , pp. 15253-15260
    • Carey, D.J.1    Bendt, K.M.2    Stahl, R.C.3
  • 49
    • 0027935309 scopus 로고
    • Leukocyte-endothelial adhesion molecules
    • Carlos T.M., and Harlan J.M. Leukocyte-endothelial adhesion molecules. Blood 84 (1994) 2068-2101
    • (1994) Blood , vol.84 , pp. 2068-2101
    • Carlos, T.M.1    Harlan, J.M.2
  • 51
    • 0019801543 scopus 로고
    • The structure of heparin oligosaccharide fragments with high anti-(Factor Xa) activity containing the minimal antithrombin-III binding sequence
    • Casu B., Oreste P., Torri G., Zoppetti G., Choay J., Lormeau J.-C., Petitou M., and Sinay P. The structure of heparin oligosaccharide fragments with high anti-(Factor Xa) activity containing the minimal antithrombin-III binding sequence. Biochem. J. 197 (1981) 599-609
    • (1981) Biochem. J. , vol.197 , pp. 599-609
    • Casu, B.1    Oreste, P.2    Torri, G.3    Zoppetti, G.4    Choay, J.5    Lormeau, J.-C.6    Petitou, M.7    Sinay, P.8
  • 52
    • 0024021040 scopus 로고
    • Conformational flexibility: A new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans
    • Casu B., Petitou M., Provasoli M., and Sinay P. Conformational flexibility: A new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans. Trends Biochem. Sci. 13 (1988) 221-225
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 221-225
    • Casu, B.1    Petitou, M.2    Provasoli, M.3    Sinay, P.4
  • 53
  • 54
    • 0028911135 scopus 로고
    • Effect of inhaled heparin on methacholine-induced bronchial hyperreactivity
    • Ceyhan B., and Celikel T. Effect of inhaled heparin on methacholine-induced bronchial hyperreactivity. Chest 107 (1995) 1009-1011
    • (1995) Chest , vol.107 , pp. 1009-1011
    • Ceyhan, B.1    Celikel, T.2
  • 55
    • 77956749391 scopus 로고
    • Low molecular weight heparin (LMWH) administration during resuscitation of hemorrhagic shock improves renal microvasculature
    • [Abstract]
    • Chaudry K.I., Singh G., Rana M.W., and Chaudry I.H. Low molecular weight heparin (LMWH) administration during resuscitation of hemorrhagic shock improves renal microvasculature. Circ. Shock 34 (1991) 25 [Abstract]
    • (1991) Circ. Shock , vol.34 , pp. 25
    • Chaudry, K.I.1    Singh, G.2    Rana, M.W.3    Chaudry, I.H.4
  • 56
    • 0344373803 scopus 로고
    • 4 ) is a chemotatic factor for eosinophils and augments Fc receptor expression on eosinophils
    • Morley J., and Colditz I. (Eds), Academic Press, London
    • 4 ) is a chemotatic factor for eosinophils and augments Fc receptor expression on eosinophils. In: Morley J., and Colditz I. (Eds). "Eosinophils and Asthma" (1989), Academic Press, London 151-156
    • (1989) "Eosinophils and Asthma" , pp. 151-156
    • Chihara, J.1    Nakajima, S.2
  • 57
    • 0021061174 scopus 로고
    • The structureactivity relationship in heparin: A synthetic pentasacharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity
    • Choay J., Petitou M., Lormeau J.-C., Sinay P., Casu B., and Gatti G. The structureactivity relationship in heparin: A synthetic pentasacharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity. Biochem. Biophys. Res. Commun. 116 (1983) 492-499
    • (1983) Biochem. Biophys. Res. Commun. , vol.116 , pp. 492-499
    • Choay, J.1    Petitou, M.2    Lormeau, J.-C.3    Sinay, P.4    Casu, B.5    Gatti, G.6
  • 58
    • 0022181969 scopus 로고
    • Heparin inhibits mesangial cell proliferation in Habu venom-induced glomerular injury
    • Coffey A.K., and Karnovsky M.J. Heparin inhibits mesangial cell proliferation in Habu venom-induced glomerular injury. Am. J. Pathol. 120 (1985) 248-255
    • (1985) Am. J. Pathol. , vol.120 , pp. 248-255
    • Coffey, A.K.1    Karnovsky, M.J.2
  • 59
    • 0018381150 scopus 로고
    • Correlation of sulfate content and degree of carboxylation of heparin and related glycosaminoglycans with anticomplement activity: Relationships to the anticoagulant and platelet-aggregating activities
    • Cofrancesco E., Radaelli F., Pogliani E., Amici N., Torri G.G., and Casu B. Correlation of sulfate content and degree of carboxylation of heparin and related glycosaminoglycans with anticomplement activity: Relationships to the anticoagulant and platelet-aggregating activities. Thromb. Res. 14 (1979) 179-187
    • (1979) Thromb. Res. , vol.14 , pp. 179-187
    • Cofrancesco, E.1    Radaelli, F.2    Pogliani, E.3    Amici, N.4    Torri, G.G.5    Casu, B.6
  • 60
    • 0014052852 scopus 로고
    • Effect of anticoagulants on delayed hypersensitivity reations
    • Cohen S., Benacerraf B., McCluskey R., and Ovary A.J. Effect of anticoagulants on delayed hypersensitivity reations. J. Immunol. 98 (1967) 351-358
    • (1967) J. Immunol. , vol.98 , pp. 351-358
    • Cohen, S.1    Benacerraf, B.2    McCluskey, R.3    Ovary, A.J.4
  • 61
    • 0029953925 scopus 로고    scopus 로고
    • Syndecans, signaling, and cell adhesion
    • Couchman J.R., and Woods A. Syndecans, signaling, and cell adhesion. J. Cell. Biochem. 61 (1996) 578-584
    • (1996) J. Cell. Biochem. , vol.61 , pp. 578-584
    • Couchman, J.R.1    Woods, A.2
  • 63
    • 0028930486 scopus 로고
    • Human eosinophilgranule major basic protein and synthetic polycations induce airway hyperresponsiveness in vivo dependent on bradykinin generation
    • Coyle A.J., Ackerman S.J., Burch R., Proud D., and Irvin C.G. Human eosinophilgranule major basic protein and synthetic polycations induce airway hyperresponsiveness in vivo dependent on bradykinin generation. J. Clin. Invest. 95 (1995) 1735-1740
    • (1995) J. Clin. Invest. , vol.95 , pp. 1735-1740
    • Coyle, A.J.1    Ackerman, S.J.2    Burch, R.3    Proud, D.4    Irvin, C.G.5
  • 65
    • 0028926451 scopus 로고
    • Activation of human neutrophils through L-selectin and Mac-1 molecules
    • Crockett-Torabi E., Sulenbarger B., Smith C.W., and Fantone J.C. Activation of human neutrophils through L-selectin and Mac-1 molecules. J. Immunol. 154 (1995) 2291-2302
    • (1995) J. Immunol. , vol.154 , pp. 2291-2302
    • Crockett-Torabi, E.1    Sulenbarger, B.2    Smith, C.W.3    Fantone, J.C.4
  • 66
    • 0001775461 scopus 로고
    • Effect of fibrinolytic activation on survival and cerebral damage following periods of circulatory arrest
    • Cromwell J., and Smith E. Effect of fibrinolytic activation on survival and cerebral damage following periods of circulatory arrest. Am. J. Physiol. 186 (1958) 283-285
    • (1958) Am. J. Physiol. , vol.186 , pp. 283-285
    • Cromwell, J.1    Smith, E.2
  • 67
    • 0000589653 scopus 로고
    • The mechanism of death after resucitation following acute circulatory failure
    • Cromwell J., Shorpe G., Lambright R., and Reed W. The mechanism of death after resucitation following acute circulatory failure. Surgery 38 (1955) 696-702
    • (1955) Surgery , vol.38 , pp. 696-702
    • Cromwell, J.1    Shorpe, G.2    Lambright, R.3    Reed, W.4
  • 68
    • 0028931052 scopus 로고
    • Protection by ITF1300, a heparin ionpair complex, against arrhythmias induced by regional ischemia and reperfusion in the isolated rat heart: Possible mechanism of action
    • Curtis M.J., Barsby R.W.J., and Forster R. Protection by ITF1300, a heparin ionpair complex, against arrhythmias induced by regional ischemia and reperfusion in the isolated rat heart: Possible mechanism of action. J. Cardiovasc. Pharmacol. 25 (1995) 643-651
    • (1995) J. Cardiovasc. Pharmacol. , vol.25 , pp. 643-651
    • Curtis, M.J.1    Barsby, R.W.J.2    Forster, R.3
  • 70
    • 0030007411 scopus 로고    scopus 로고
    • New synthetic sulfated oligosaccharides prolong survival of cardiac xenografts by inhibiting release of heparan sulfate from endothelial cells
    • Deng S., Pascual M., Lou J., Buhler L., Wessel H.P., Grau G., Schifferli J.A., and Morel P. New synthetic sulfated oligosaccharides prolong survival of cardiac xenografts by inhibiting release of heparan sulfate from endothelial cells. Transplantation 61 (1996) 1300-1305
    • (1996) Transplantation , vol.61 , pp. 1300-1305
    • Deng, S.1    Pascual, M.2    Lou, J.3    Buhler, L.4    Wessel, H.P.5    Grau, G.6    Schifferli, J.A.7    Morel, P.8
  • 72
    • 0022897091 scopus 로고
    • Nonanticoagulant protective effect of heparin in chronic aminonucleosidenephrosis
    • Diamond J.R., and Karnovsky M.J. Nonanticoagulant protective effect of heparin in chronic aminonucleosidenephrosis. Renal Physiol. 9 (1986) 366-374
    • (1986) Renal Physiol. , vol.9 , pp. 366-374
    • Diamond, J.R.1    Karnovsky, M.J.2
  • 73
    • 0029166397 scopus 로고
    • Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD18)
    • Diamond M.S., Alon R., Parkos C.A., Quinn M.T., and Springer T.A. Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD18). J. Cell Biol. 130 (1995) 1473-1482
    • (1995) J. Cell Biol. , vol.130 , pp. 1473-1482
    • Diamond, M.S.1    Alon, R.2    Parkos, C.A.3    Quinn, M.T.4    Springer, T.A.5
  • 75
    • 0028841584 scopus 로고
    • 'Sticky' neutrophils, pathergic arthritis, and response to heparin in pyodema gangrenosum complicating ulcerative colitis
    • Dwarakanath A.D., Yu L.G., Brookes C., Pryce D., and Rhodes J.M. 'Sticky' neutrophils, pathergic arthritis, and response to heparin in pyodema gangrenosum complicating ulcerative colitis. Gut 37 (1995) 585-588
    • (1995) Gut , vol.37 , pp. 585-588
    • Dwarakanath, A.D.1    Yu, L.G.2    Brookes, C.3    Pryce, D.4    Rhodes, J.M.5
  • 76
    • 0028040933 scopus 로고
    • Eosinophil transendothelial migration induced by cytokines: Effect of the chemokine RANTES
    • Ebisawa M., Yamada T., Bickel C., Klunk D., and Schleimer R.P. Eosinophil transendothelial migration induced by cytokines: Effect of the chemokine RANTES. J. Immunol. 153 (1994) 2153-2160
    • (1994) J. Immunol. , vol.153 , pp. 2153-2160
    • Ebisawa, M.1    Yamada, T.2    Bickel, C.3    Klunk, D.4    Schleimer, R.P.5
  • 77
    • 0003072554 scopus 로고
    • Heparin is not just an anticoagulant anymore: Six and one-half decades of studies on the ability of heparin to regulate complement activity
    • Edens R.E., Lindhardt R.J., and Weiler J.M. Heparin is not just an anticoagulant anymore: Six and one-half decades of studies on the ability of heparin to regulate complement activity. Complement Profiles 1 (1993) 96-120
    • (1993) Complement Profiles , vol.1 , pp. 96-120
    • Edens, R.E.1    Lindhardt, R.J.2    Weiler, J.M.3
  • 78
    • 0021878810 scopus 로고
    • Inhibition of human and guinea pig complement by heparin fractions differing in affinity for antithrombin III or in average molecular weight
    • Ekre H.-P.T. Inhibition of human and guinea pig complement by heparin fractions differing in affinity for antithrombin III or in average molecular weight. Int. J. Immunopharmacol. 7 (1985) 271-280
    • (1985) Int. J. Immunopharmacol. , vol.7 , pp. 271-280
    • Ekre, H.-P.T.1
  • 79
    • 0022620954 scopus 로고
    • Inhibition of complement dependent experimental inflammation in human skin by different heparin fractions
    • Ekre H.-P.T., Fjellner B., and Hägermark O. Inhibition of complement dependent experimental inflammation in human skin by different heparin fractions. Int. J. Immunopharmacol. 8 (1986) 277-286
    • (1986) Int. J. Immunopharmacol. , vol.8 , pp. 277-286
    • Ekre, H.-P.T.1    Fjellner, B.2    Hägermark, O.3
  • 80
    • 0029049017 scopus 로고
    • Modulated glycosylation of proteoglycans during differentiation of human B lymphocytes
    • Engelmann S., Ebeling O., and Schwartzalbiez R. Modulated glycosylation of proteoglycans during differentiation of human B lymphocytes. Biochim. Biophys. Acta Mol. Cell Res. 1267 (1995) 6-14
    • (1995) Biochim. Biophys. Acta Mol. Cell Res. , vol.1267 , pp. 6-14
    • Engelmann, S.1    Ebeling, O.2    Schwartzalbiez, R.3
  • 81
    • 0028817350 scopus 로고
    • Interleukin-8 is a potent mediator of eosinophil chemotaxis through endothelium and epithelium
    • Erger R.A., and Casale T.B. Interleukin-8 is a potent mediator of eosinophil chemotaxis through endothelium and epithelium. Am. J. Physiol. 268 (1995) L117-L122
    • (1995) Am. J. Physiol. , vol.268
    • Erger, R.A.1    Casale, T.B.2
  • 82
    • 0027401312 scopus 로고
    • 2 integrin (Mac-1) and L-selectin (LECAM-1) adherence receptors on human neutrophils by high-resolution field emission
    • 2 integrin (Mac-1) and L-selectin (LECAM-1) adherence receptors on human neutrophils by high-resolution field emission. Semin. J. Histochem. Cytochem. 41 (1993) 327-333
    • (1993) Semin. J. Histochem. Cytochem. , vol.41 , pp. 327-333
    • Erlandsen, S.L.1    Hasslen, S.R.2    Nelson, R.D.3
  • 83
    • 0030272433 scopus 로고    scopus 로고
    • Influence of core protein sequence on glycosaminoglycan assembly
    • Esko J.D., and Zhang L.J. Influence of core protein sequence on glycosaminoglycan assembly. Curr. Opin. Struct. Biol. 6 (1996) 663-670
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 663-670
    • Esko, J.D.1    Zhang, L.J.2
  • 84
  • 85
    • 0001811919 scopus 로고
    • Treatment of corticosteroid resistant ulcerative colitis with heparin-A report of 9 cases
    • [Abstract]
    • Evans R.C., and Rhodes J.M. Treatment of corticosteroid resistant ulcerative colitis with heparin-A report of 9 cases. Gut 37 Suppl 2 (1995) A49 [Abstract]
    • (1995) Gut , vol.37 , Issue.SUPPL. 2
    • Evans, R.C.1    Rhodes, J.M.2
  • 86
    • 0026657360 scopus 로고
    • Heparin-induced conformational change and activation of mucus proteinase inhibitor
    • Faller B., Mely Y., Gerard D., and Bieth J.G. Heparin-induced conformational change and activation of mucus proteinase inhibitor. Biochemistry 31 (1992) 8285-8290
    • (1992) Biochemistry , vol.31 , pp. 8285-8290
    • Faller, B.1    Mely, Y.2    Gerard, D.3    Bieth, J.G.4
  • 87
    • 0015093810 scopus 로고
    • The role of heparin in prolonging acute renal ischemia time
    • Fegen J.P., Albert D.J., and Persky L. The role of heparin in prolonging acute renal ischemia time. Invest. Urology 9 (1971) 16-20
    • (1971) Invest. Urology , vol.9 , pp. 16-20
    • Fegen, J.P.1    Albert, D.J.2    Persky, L.3
  • 89
    • 0023097239 scopus 로고
    • Antivascular antibodies in the sera of patients with senile dementia of the Alzheimer's type
    • Fillit H.M., Kemeny E., Luine V., Weksler M.E., and Zabriskie J.B. Antivascular antibodies in the sera of patients with senile dementia of the Alzheimer's type. J. Gerontol. 42 (1987) 180-184
    • (1987) J. Gerontol. , vol.42 , pp. 180-184
    • Fillit, H.M.1    Kemeny, E.2    Luine, V.3    Weksler, M.E.4    Zabriskie, J.B.5
  • 91
    • 0027279025 scopus 로고
    • Heparin suppresses mesangial cell proliferation and matrix expansion in experimental mesangioproliferative glomerulonephritis
    • Floege J., Eng E., Young B.A., Couser W.G., and Johnson R.J. Heparin suppresses mesangial cell proliferation and matrix expansion in experimental mesangioproliferative glomerulonephritis. Kidney Intl. 43 (1993) 369-380
    • (1993) Kidney Intl. , vol.43 , pp. 369-380
    • Floege, J.1    Eng, E.2    Young, B.A.3    Couser, W.G.4    Johnson, R.J.5
  • 92
    • 0001937213 scopus 로고
    • Selectin family of adhesion molecules
    • Granger D.N., and Schmid-Schönbein G.W. (Eds), Oxford University Press, New York
    • Forrest M., and Paulson J.C. Selectin family of adhesion molecules. In: Granger D.N., and Schmid-Schönbein G.W. (Eds). "Physiology and Pathophysiology of Leukocyte Adhesion" (1995), Oxford University Press, New York 43-80
    • (1995) "Physiology and Pathophysiology of Leukocyte Adhesion" , pp. 43-80
    • Forrest, M.1    Paulson, J.C.2
  • 93
    • 0000706261 scopus 로고
    • Periodate oxidation of the glucuronic acids residues in heparan sulfate and heparin
    • Fransson L.-A. Periodate oxidation of the glucuronic acids residues in heparan sulfate and heparin. Carbohydr. Res. 62 (1978) 235-244
    • (1978) Carbohydr. Res. , vol.62 , pp. 235-244
    • Fransson, L.-A.1
  • 94
    • 0010262676 scopus 로고
    • Heparan sulphate proteoglycans: structure and properties
    • Lane D.A., and Lindahl U. (Eds), CRC Press, Boca Raton, FL
    • Fransson L.-A. Heparan sulphate proteoglycans: structure and properties. In: Lane D.A., and Lindahl U. (Eds). "Heparin Chemical and Biological Properties, Clinical Applications" (1989), CRC Press, Boca Raton, FL 115-133
    • (1989) "Heparin Chemical and Biological Properties, Clinical Applications" , pp. 115-133
    • Fransson, L.-A.1
  • 95
    • 0026673537 scopus 로고
    • Effects of sulfate ions on Alzheimer-beta/A4 peptide assemblies-Implications for amyloid fibril-proteoglycan interactions
    • Fraser P.E., Nguyen J.T., Chin D.T., and Kirschner D.A. Effects of sulfate ions on Alzheimer-beta/A4 peptide assemblies-Implications for amyloid fibril-proteoglycan interactions. J. Neurochem. 59 (1992) 1531-1540
    • (1992) J. Neurochem. , vol.59 , pp. 1531-1540
    • Fraser, P.E.1    Nguyen, J.T.2    Chin, D.T.3    Kirschner, D.A.4
  • 96
    • 0027322517 scopus 로고
    • Alpha-1-antichymotrypsin binding to Alzheimer Aβ peptides is sequence specific and induces fibril disaggregation in vitro
    • Fraser P.E., Nguyen J.T., McLachlan D.R., Abraham C.R., and Kirschner D.A. Alpha-1-antichymotrypsin binding to Alzheimer Aβ peptides is sequence specific and induces fibril disaggregation in vitro. J. Neurochem. 61 (1993) 298-305
    • (1993) J. Neurochem. , vol.61 , pp. 298-305
    • Fraser, P.E.1    Nguyen, J.T.2    McLachlan, D.R.3    Abraham, C.R.4    Kirschner, D.A.5
  • 97
    • 0024521509 scopus 로고
    • Biosynthesis and deposition of a noncovalent laminin-heparan sulfate proteoglycan complex and other basal lamina components by a human malignant cell line
    • Frenette G.P., Ruddon R.W., Krzesicki R.F., Naser J.A., and Peters B.P. Biosynthesis and deposition of a noncovalent laminin-heparan sulfate proteoglycan complex and other basal lamina components by a human malignant cell line. J. Biol. Chem. 264 (1989) 3078-3088
    • (1989) J. Biol. Chem. , vol.264 , pp. 3078-3088
    • Frenette, G.P.1    Ruddon, R.W.2    Krzesicki, R.F.3    Naser, J.A.4    Peters, B.P.5
  • 98
    • 0029119149 scopus 로고
    • Platelets roll on stimulated endothelium in vivo: An interaction mediated by endothelial P-selectin
    • Frenette P.S., Johnson R.C., Hynes R.O., and Wagner D.D. Platelets roll on stimulated endothelium in vivo: An interaction mediated by endothelial P-selectin. Proc. Natl. Acad. Sci. USA 92 (1995) 7450-7454
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7450-7454
    • Frenette, P.S.1    Johnson, R.C.2    Hynes, R.O.3    Wagner, D.D.4
  • 99
    • 0028060072 scopus 로고
    • Effects of heparin and N-acetyl heparin on ischemia/reperfusion-induced alterations in myocardial function in the rabbit isolated heart
    • Friedrichs G.S., Kilgore K.S., Manley P.J., Gralinski M.R., and Lucchesi B.R. Effects of heparin and N-acetyl heparin on ischemia/reperfusion-induced alterations in myocardial function in the rabbit isolated heart. Circulation Res. 75 (1994) 701-710
    • (1994) Circulation Res. , vol.75 , pp. 701-710
    • Friedrichs, G.S.1    Kilgore, K.S.2    Manley, P.J.3    Gralinski, M.R.4    Lucchesi, B.R.5
  • 100
    • 0018834859 scopus 로고
    • Cytotoxic effects of the guinea pig eosinophil major basic protein on tracheal epithelium
    • Frigas E., Loegering D.A., and Gleich G.J. Cytotoxic effects of the guinea pig eosinophil major basic protein on tracheal epithelium. Lab. Invest. 42 (1980) 35-43
    • (1980) Lab. Invest. , vol.42 , pp. 35-43
    • Frigas, E.1    Loegering, D.A.2    Gleich, G.J.3
  • 101
    • 0028127188 scopus 로고
    • Two N-acetylglucosaminyltransferases catalyze the biosynthesis of heparan sulfate
    • Fritz T.A., Gabb M.M., Wei G., and Esko J.D. Two N-acetylglucosaminyltransferases catalyze the biosynthesis of heparan sulfate. J. Biol. Chem. 269 (1994) 28809-28814
    • (1994) J. Biol. Chem. , vol.269 , pp. 28809-28814
    • Fritz, T.A.1    Gabb, M.M.2    Wei, G.3    Esko, J.D.4
  • 103
    • 0029844407 scopus 로고    scopus 로고
    • Sialylated fucosylated ligands for L-selectin expressed on leukocytes mediate tethering and rolling adhesions in physiologic flow conditions
    • Fuhlbrigge R.C., Alon R., Puri K.D., Lowe J.B., and Springer T.A. Sialylated fucosylated ligands for L-selectin expressed on leukocytes mediate tethering and rolling adhesions in physiologic flow conditions. J. Cell Biol. 135 (1996) 837-848
    • (1996) J. Cell Biol. , vol.135 , pp. 837-848
    • Fuhlbrigge, R.C.1    Alon, R.2    Puri, K.D.3    Lowe, J.B.4    Springer, T.A.5
  • 104
  • 106
    • 0024953597 scopus 로고
    • The extended family of proteoglycans: Social residents of the pericellular zone
    • Gallagher J.T. The extended family of proteoglycans: Social residents of the pericellular zone. Curr. Opin. Cell Biol. 1 (1989) 1201-1218
    • (1989) Curr. Opin. Cell Biol. , vol.1 , pp. 1201-1218
    • Gallagher, J.T.1
  • 107
    • 0029925092 scopus 로고    scopus 로고
    • Time course of the protective effect of inhaled heparin on exercise-induced asthma
    • Garrigo J., Danta I., and Ahmed T. Time course of the protective effect of inhaled heparin on exercise-induced asthma. Am. J. Respir. Crit. Care Med. 153 (1996) 1702-1707
    • (1996) Am. J. Respir. Crit. Care Med. , vol.153 , pp. 1702-1707
    • Garrigo, J.1    Danta, I.2    Ahmed, T.3
  • 108
    • 0028829969 scopus 로고
    • Lectin and epidermal growth factor domains of P-selectin at physiologic density are the recognition unit for leukocyte binding
    • Gibson R.M., Kansas G.S., Tedder T.F., Furie B., and Furie B.C. Lectin and epidermal growth factor domains of P-selectin at physiologic density are the recognition unit for leukocyte binding. Blood 85 (1995) 151-158
    • (1995) Blood , vol.85 , pp. 151-158
    • Gibson, R.M.1    Kansas, G.S.2    Tedder, T.F.3    Furie, B.4    Furie, B.C.5
  • 109
    • 0030060311 scopus 로고    scopus 로고
    • Interplay of T cells and cytokines in the context of enzymatically modified extracellular matrix
    • Gilat D., Cahalon L., Hershkoviz R., and Lider O. Interplay of T cells and cytokines in the context of enzymatically modified extracellular matrix. Immunol. Today 17 (1996) 16-20
    • (1996) Immunol. Today , vol.17 , pp. 16-20
    • Gilat, D.1    Cahalon, L.2    Hershkoviz, R.3    Lider, O.4
  • 110
    • 0028916622 scopus 로고
    • Molecular behavior adapts to context: Heparanase functions as an extracellular matrix-degrading enzyme or as a T cell adhesion molecule, depending on the local pH
    • Gilat D., Hershkoviz R., Goldkorn I., Cahalon L., Korner G., Vlodavsky I., and Lider O. Molecular behavior adapts to context: Heparanase functions as an extracellular matrix-degrading enzyme or as a T cell adhesion molecule, depending on the local pH. J. Exp. Med. 181 (1995) 1929-1934
    • (1995) J. Exp. Med. , vol.181 , pp. 1929-1934
    • Gilat, D.1    Hershkoviz, R.2    Goldkorn, I.3    Cahalon, L.4    Korner, G.5    Vlodavsky, I.6    Lider, O.7
  • 111
    • 0028134835 scopus 로고
    • + T lymphocytes to intact or heparinase-treated subendothelial extracellular matrix by diffusible or anchored RANTES and MIP-1β
    • + T lymphocytes to intact or heparinase-treated subendothelial extracellular matrix by diffusible or anchored RANTES and MIP-1β. J. Immunol. 153 (1994) 4899-4906
    • (1994) J. Immunol. , vol.153 , pp. 4899-4906
    • Gilat, D.1    Hershkoviz, R.2    Mekori, Y.A.3    Vlodavsky, I.4    Lider, O.5
  • 112
    • 0029153736 scopus 로고
    • High endothelial venules (HEVs): Specialized endothelium for lymphocyte migration
    • Girard J.P., and Springer T.A. High endothelial venules (HEVs): Specialized endothelium for lymphocyte migration. Immunol. Today 16 (1995) 449-457
    • (1995) Immunol. Today , vol.16 , pp. 449-457
    • Girard, J.P.1    Springer, T.A.2
  • 113
    • 0031028665 scopus 로고    scopus 로고
    • Monocyte adhesion to activated aortic endothelium: Role of L-selectin and heparan sulfate proteoglycans
    • Giuffrè L., Cordey A.-S., Monai N., Tardy Y., Schapira M., and Spertini O. Monocyte adhesion to activated aortic endothelium: Role of L-selectin and heparan sulfate proteoglycans. J. Cell Biol. 136 (1997) 945-956
    • (1997) J. Cell Biol. , vol.136 , pp. 945-956
    • Giuffrè, L.1    Cordey, A.-S.2    Monai, N.3    Tardy, Y.4    Schapira, M.5    Spertini, O.6
  • 114
    • 0015633469 scopus 로고
    • Identification of a major basic protein in guinea pig eosinophil granules
    • Gleich G.J., Loegering D.A., and Maldonado J.E. Identification of a major basic protein in guinea pig eosinophil granules. J. Exp. Med. 137 (1973) 1459-1471
    • (1973) J. Exp. Med. , vol.137 , pp. 1459-1471
    • Gleich, G.J.1    Loegering, D.A.2    Maldonado, J.E.3
  • 115
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert M., Jakes R., Spillantini M.G., Hasegawa M., Smith M.J., and Crowther R.A. Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 383 (1996) 550-553
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 117
    • 0027185651 scopus 로고
    • Regulation of β-amyloid precursor protein isoform messenger RNAs by transforming growth factor-beta-1 and interleukin-1-beta in astrocytes
    • Gray C.W., and Patel A.J. Regulation of β-amyloid precursor protein isoform messenger RNAs by transforming growth factor-beta-1 and interleukin-1-beta in astrocytes. Mol. Brain Res. 19 (1993) 251-256
    • (1993) Mol. Brain Res. , vol.19 , pp. 251-256
    • Gray, C.W.1    Patel, A.J.2
  • 118
    • 0028821427 scopus 로고
    • Further studies of the binding specificity of the leukocyte adhesion molecule, L-selectin, towards sulphated oligosaccharides-Suggestion of a link between the selectin- and the integrin-mediated lymphocyte adhesion systems
    • Green P.J., Yuen C.T., Childs R.A., Chai W., Miyasaka M., Lemoine R., Lubineau A., Smith B., Ueno H., Nicolaou K.C., and Feizi T. Further studies of the binding specificity of the leukocyte adhesion molecule, L-selectin, towards sulphated oligosaccharides-Suggestion of a link between the selectin- and the integrin-mediated lymphocyte adhesion systems. Glycobiology 5 (1995) 29-38
    • (1995) Glycobiology , vol.5 , pp. 29-38
    • Green, P.J.1    Yuen, C.T.2    Childs, R.A.3    Chai, W.4    Miyasaka, M.5    Lemoine, R.6    Lubineau, A.7    Smith, B.8    Ueno, H.9    Nicolaou, K.C.10    Feizi, T.11
  • 119
    • 0027603637 scopus 로고
    • Effect of salbutamol, fenterol, and sodium cromoglycate on the release of heparin from sensitized human lung fragments challenged with Dermatophagoides pteronyssinus allergen
    • Green W.F., Konnaris K., and Woolcock A.J. Effect of salbutamol, fenterol, and sodium cromoglycate on the release of heparin from sensitized human lung fragments challenged with Dermatophagoides pteronyssinus allergen. Am. J. Respir. Cell Mol. Biol. 8 (1993) 518-521
    • (1993) Am. J. Respir. Cell Mol. Biol. , vol.8 , pp. 518-521
    • Green, W.F.1    Konnaris, K.2    Woolcock, A.J.3
  • 121
    • 0028926976 scopus 로고
    • Interleukin-1 expression in different plaque types in Alzheimer's disease: Significance in plaque evolution
    • Griffin W.S.T., Sheng J.G., Roberts G.W., and Mrak R.E. Interleukin-1 expression in different plaque types in Alzheimer's disease: Significance in plaque evolution. J. Neuropathol. Exp. Neurol. 54 (1995) 276-281
    • (1995) J. Neuropathol. Exp. Neurol. , vol.54 , pp. 276-281
    • Griffin, W.S.T.1    Sheng, J.G.2    Roberts, G.W.3    Mrak, R.E.4
  • 122
    • 0028978227 scopus 로고
    • Proteoglycan-mediated inhibition of A beta proteolysis: A potential cause of senile plaque formation
    • Gupta-Bansal R., Frederickson R.C.A., and Brunden K.R. Proteoglycan-mediated inhibition of A beta proteolysis: A potential cause of senile plaque formation. J. Biol. Chem. 170 (1995) 18666-18671
    • (1995) J. Biol. Chem. , vol.170 , pp. 18666-18671
    • Gupta-Bansal, R.1    Frederickson, R.C.A.2    Brunden, K.R.3
  • 123
    • 0029793468 scopus 로고    scopus 로고
    • P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for P-selectin in neutrophil aggregation
    • Guyer D.A., Moore K.L., Lynam E.B., Schammel C.M.G., Rogelj S., McEver R.P., and Sklar L.A. P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for P-selectin in neutrophil aggregation. Blood 88 (1996) 2415-2421
    • (1996) Blood , vol.88 , pp. 2415-2421
    • Guyer, D.A.1    Moore, K.L.2    Lynam, E.B.3    Schammel, C.M.G.4    Rogelj, S.5    McEver, R.P.6    Sklar, L.A.7
  • 124
    • 0030950546 scopus 로고    scopus 로고
    • Analysis of long-term Elmiron therapy for interstitial cystitis
    • Hanno P.M. Analysis of long-term Elmiron therapy for interstitial cystitis. Urology 49 Suppl 5A (1997) 93-99
    • (1997) Urology , vol.49 , Issue.SUPPL. 5A , pp. 93-99
    • Hanno, P.M.1
  • 125
    • 0028025212 scopus 로고
    • Competitive binding of low molecular mass heparin-tyramine fluorescein-5-isothiocyanate and unlabeled glycosaminoglycans to leukocytes
    • Harenberg J., Malsch R., Piazolo L., and Heene D.L. Competitive binding of low molecular mass heparin-tyramine fluorescein-5-isothiocyanate and unlabeled glycosaminoglycans to leukocytes. Semin. Thromb. Hemost. 20 (1994) 236-244
    • (1994) Semin. Thromb. Hemost. , vol.20 , pp. 236-244
    • Harenberg, J.1    Malsch, R.2    Piazolo, L.3    Heene, D.L.4
  • 126
    • 0029101055 scopus 로고
    • Spatial distribution of L-selectin (CD62L) on human lymphocytes and transfected murine L1-2 cells
    • Hasslen S.R., von Addrian U.H., Butcher E.C., Nelson R.D., and Erlandsen S.L. Spatial distribution of L-selectin (CD62L) on human lymphocytes and transfected murine L1-2 cells. Histochem. J. 27 (1995) 547-554
    • (1995) Histochem. J. , vol.27 , pp. 547-554
    • Hasslen, S.R.1    von Addrian, U.H.2    Butcher, E.C.3    Nelson, R.D.4    Erlandsen, S.L.5
  • 127
    • 0019513368 scopus 로고
    • Heparin aerosol-Effect on blood coagulation and pulmonary function
    • Hellgren M., Hägnevik K., and Blombäck M. Heparin aerosol-Effect on blood coagulation and pulmonary function. Thromb. Res. 21 (1981) 493-502
    • (1981) Thromb. Res. , vol.21 , pp. 493-502
    • Hellgren, M.1    Hägnevik, K.2    Blombäck, M.3
  • 129
    • 0023989699 scopus 로고
    • Heparinization reduces endothelial permeability and hydrogen ion accumulation in a canine skeletal muscle ischaemia-reperfusion model
    • Hobson II R.W., Wright J.G., Fox D., and Keer J.C. Heparinization reduces endothelial permeability and hydrogen ion accumulation in a canine skeletal muscle ischaemia-reperfusion model. J. Vasc. Surg. 7 (1988) 585-590
    • (1988) J. Vasc. Surg. , vol.7 , pp. 585-590
    • Hobson II, R.W.1    Wright, J.G.2    Fox, D.3    Keer, J.C.4
  • 130
    • 0026532797 scopus 로고
    • Dextran sulfate and heparin sulfate inhibit platelet-activating factor-induced pulmonary edema
    • Hocking D., Ferro T.J., and Johnson A. Dextran sulfate and heparin sulfate inhibit platelet-activating factor-induced pulmonary edema. J. Appl. Physiol. 72 (1992) 179-185
    • (1992) J. Appl. Physiol. , vol.72 , pp. 179-185
    • Hocking, D.1    Ferro, T.J.2    Johnson, A.3
  • 131
    • 77956744265 scopus 로고    scopus 로고
    • An alkaline O-desulfated LMW heparin derivative with reduced anticoagulant activity and retained in vivo anti-inflammatory activity
    • Abstract of the, July 21-26, Milan, Italy
    • Holme, K. R., Liang, W., Yang, Z., Kubes, P., Tuomanen, E., and Larsen, R. D. (1996a). An alkaline O-desulfated LMW heparin derivative with reduced anticoagulant activity and retained in vivo anti-inflammatory activity. Abstract of the XVII Intl. Carbohydr. Symposium, July 21-26, Milan, Italy.
    • (1996) XVII Intl. Carbohydr. Symposium
    • Holme, K.R.1    Liang, W.2    Yang, Z.3    Kubes, P.4    Tuomanen, E.5    Larsen, R.D.6
  • 133
    • 0028830210 scopus 로고
    • CXC chemokines connective tissue activating peptide-III and neutrophil activating peptide-2 are heparin/heparan sulfate-degrading enzymes
    • Hoogewerf A.J., Leone J.W., Reardon I.M., Howe W.J., Asa D., Heinrikson R.L., and Ledbetter S.R. CXC chemokines connective tissue activating peptide-III and neutrophil activating peptide-2 are heparin/heparan sulfate-degrading enzymes. J. Biol. Chem. 270 (1995) 3268-3277
    • (1995) J. Biol. Chem. , vol.270 , pp. 3268-3277
    • Hoogewerf, A.J.1    Leone, J.W.2    Reardon, I.M.3    Howe, W.J.4    Asa, D.5    Heinrikson, R.L.6    Ledbetter, S.R.7
  • 135
    • 0027753031 scopus 로고
    • Potential species dependency for the pulmonary antiallergic effects of aerosolized heparin
    • Howell R.E., and Woeppel S.L. Potential species dependency for the pulmonary antiallergic effects of aerosolized heparin. Pulm. Pharmacol. 6 (1993) 237-239
    • (1993) Pulm. Pharmacol. , vol.6 , pp. 237-239
    • Howell, R.E.1    Woeppel, S.L.2
  • 136
    • 0030873138 scopus 로고    scopus 로고
    • Efficacy of pentosan polysulfate in the treatment of interstitial cystitis: A meta-analysis
    • Hwang P., Auclair B., Beechinor D., Diment M., and Einarson T.R. Efficacy of pentosan polysulfate in the treatment of interstitial cystitis: A meta-analysis. Urology 50 (1997) 39-43
    • (1997) Urology , vol.50 , pp. 39-43
    • Hwang, P.1    Auclair, B.2    Beechinor, D.3    Diment, M.4    Einarson, T.R.5
  • 137
    • 0027167120 scopus 로고
    • Heparin inhibits histamine release from canine mast cells
    • Inase N., Schreck R.E., and Lazarus S.C. Heparin inhibits histamine release from canine mast cells. Am. J. Physiol. 264 (1993) L387-L390
    • (1993) Am. J. Physiol. , vol.264
    • Inase, N.1    Schreck, R.E.2    Lazarus, S.C.3
  • 139
    • 0023001195 scopus 로고
    • Transport of heparan sulfate into the nuclei of hepatocytes
    • Ishihara M., Fedarko N.S., and Conrad H.E. Transport of heparan sulfate into the nuclei of hepatocytes. J. Biol. Chem. 261 (1986) 13575-13580
    • (1986) J. Biol. Chem. , vol.261 , pp. 13575-13580
    • Ishihara, M.1    Fedarko, N.S.2    Conrad, H.E.3
  • 140
    • 0029929433 scopus 로고    scopus 로고
    • Phosphorylation of a membrane-intercalated proteoglycan, syndecan-2, expressed in a stroma-inducing clone from a mouse Lewis lung carcinoma
    • Itano N., Oguri K., Nagayasu Y., Kusano Y., Nakanishi H., David G., and Okayama M. Phosphorylation of a membrane-intercalated proteoglycan, syndecan-2, expressed in a stroma-inducing clone from a mouse Lewis lung carcinoma. Biochem. J. 315 (1996) 925-930
    • (1996) Biochem. J. , vol.315 , pp. 925-930
    • Itano, N.1    Oguri, K.2    Nagayasu, Y.3    Kusano, Y.4    Nakanishi, H.5    David, G.6    Okayama, M.7
  • 141
    • 0028970199 scopus 로고
    • Heparin effects on superoxide production by neutrophils
    • Itoh K., Nakao A., Kishimoto W., and Takagi H. Heparin effects on superoxide production by neutrophils. Eur. Surg. Res. 27 (1995) 184-188
    • (1995) Eur. Surg. Res. , vol.27 , pp. 184-188
    • Itoh, K.1    Nakao, A.2    Kishimoto, W.3    Takagi, H.4
  • 142
    • 0021919760 scopus 로고
    • Elastases and emphysema: Current assessment of the protease-antiproteases hypothesis
    • Janoff A. Elastases and emphysema: Current assessment of the protease-antiproteases hypothesis. Am. Rev. Respir. Dis. 132 (1985) 417-433
    • (1985) Am. Rev. Respir. Dis. , vol.132 , pp. 417-433
    • Janoff, A.1
  • 143
    • 0018477317 scopus 로고
    • Heparins-Anionic polyelectrolyte drugs
    • Jaques L.B. Heparins-Anionic polyelectrolyte drugs. Phamacol. Rev. 31 (1979) 99-166
    • (1979) Phamacol. Rev. , vol.31 , pp. 99-166
    • Jaques, L.B.1
  • 144
    • 0018605698 scopus 로고
    • Heparin: An old drug with a new paradigm
    • Jaques L.B. Heparin: An old drug with a new paradigm. Science 206 (1979) 528-533
    • (1979) Science , vol.206 , pp. 528-533
    • Jaques, L.B.1
  • 145
    • 0018099471 scopus 로고
    • Pharmacodynamics and clinical effectiveness of heparin
    • Jaques L.B., and Mahadoo J. Pharmacodynamics and clinical effectiveness of heparin. Sem. Thromb. Hemost. 4 (1978) 298-325
    • (1978) Sem. Thromb. Hemost. , vol.4 , pp. 298-325
    • Jaques, L.B.1    Mahadoo, J.2
  • 146
    • 0017120034 scopus 로고
    • Intrapulmonary heparin: A new procedure for anticoagulant therapy
    • Jaques L.B., Mahadoo J., and Kavanagh L.W. Intrapulmonary heparin: A new procedure for anticoagulant therapy. Lancet 2 (1976) 1157-1161
    • (1976) Lancet , vol.2 , pp. 1157-1161
    • Jaques, L.B.1    Mahadoo, J.2    Kavanagh, L.W.3
  • 147
    • 0030053077 scopus 로고    scopus 로고
    • Analysis of bovine γδ T cell interactions with E-, P-, and L-selectin: Characterization of lymphocyte on lymphocyte rolling and the effects of O-glycoprotease
    • Jutila M.A., and Kurk S. Analysis of bovine γδ T cell interactions with E-, P-, and L-selectin: Characterization of lymphocyte on lymphocyte rolling and the effects of O-glycoprotease. J. Immunol. 156 (1996) 289-296
    • (1996) J. Immunol. , vol.156 , pp. 289-296
    • Jutila, M.A.1    Kurk, S.2
  • 148
    • 0026766903 scopus 로고
    • Cytokine RANTES released by thrombin-stimulated platelets is a potent attractant for human eosinophils
    • Kameyoshi Y., Doorschner A., Mallet A.I., Christophers E., and Schroeder J.M. Cytokine RANTES released by thrombin-stimulated platelets is a potent attractant for human eosinophils. J. Exp. Med. 176 (1992) 582-591
    • (1992) J. Exp. Med. , vol.176 , pp. 582-591
    • Kameyoshi, Y.1    Doorschner, A.2    Mallet, A.I.3    Christophers, E.4    Schroeder, J.M.5
  • 151
    • 0028973572 scopus 로고
    • Leukotriene C4/D4 induces P-selectin and sialyl Lewis X-dependent alterations in leukocyte kinetics in vivo
    • Kanwar S., Johnston B., and Kubes P. Leukotriene C4/D4 induces P-selectin and sialyl Lewis X-dependent alterations in leukocyte kinetics in vivo. Circ. Res. 77 (1995) 879-887
    • (1995) Circ. Res. , vol.77 , pp. 879-887
    • Kanwar, S.1    Johnston, B.2    Kubes, P.3
  • 152
    • 0019411810 scopus 로고
    • Structural determinants of the capacity of heparin to inhibit the formation of the human amplification C3 convertase
    • Kazatchkine M.D., Fearon D.T., Metcalfe D.D., Rosenberg R.D., and Austen K.F. Structural determinants of the capacity of heparin to inhibit the formation of the human amplification C3 convertase. J. Clin. Invest. 67 (1981) 223-228
    • (1981) J. Clin. Invest. , vol.67 , pp. 223-228
    • Kazatchkine, M.D.1    Fearon, D.T.2    Metcalfe, D.D.3    Rosenberg, R.D.4    Austen, K.F.5
  • 153
    • 77956774348 scopus 로고
    • Use of heparin to inhibit interleukin-8
    • International Patent Application, WO94/18989
    • Kennedy, T. P. (1994). Use of heparin to inhibit interleukin-8. International Patent Application, WO94/18989.
    • (1994)
    • Kennedy, T.P.1
  • 154
    • 0028987492 scopus 로고
    • Inhibition of serum-induced proliferation of bovine tracheal smooth muscle cells in culture by heparin and related glycosaminoglycans
    • Kilfeather S.A., Tagoe S., Perez A.C., Okona-Mensa K., Matin R., and Page C.P. Inhibition of serum-induced proliferation of bovine tracheal smooth muscle cells in culture by heparin and related glycosaminoglycans. Br. J. Pharmacol. 114 (1995) 1442-1446
    • (1995) Br. J. Pharmacol. , vol.114 , pp. 1442-1446
    • Kilfeather, S.A.1    Tagoe, S.2    Perez, A.C.3    Okona-Mensa, K.4    Matin, R.5    Page, C.P.6
  • 155
    • 0028016404 scopus 로고
    • Members of the syndecan family of heparan sulfate proteoglycans are expressed in distinct cell-, tissue-, and development-specific patterns
    • Kim C.W., Goldberger O.A., Gallo R.L., and Bernfield M. Members of the syndecan family of heparan sulfate proteoglycans are expressed in distinct cell-, tissue-, and development-specific patterns. Mol. Biol. Cell. 5 (1994) 797-805
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 797-805
    • Kim, C.W.1    Goldberger, O.A.2    Gallo, R.L.3    Bernfield, M.4
  • 156
    • 0027080695 scopus 로고
    • Proteoglycans, glycosaminoglycans, amyloid-enhancing factor, and amyloid deposition
    • Kisilevsky R. Proteoglycans, glycosaminoglycans, amyloid-enhancing factor, and amyloid deposition. J. Internal Med. 232 (1992) 515-516
    • (1992) J. Internal Med. , vol.232 , pp. 515-516
    • Kisilevsky, R.1
  • 157
    • 0023767031 scopus 로고
    • The potential significance of sulphated glycosaminoglycans as a common constituent of all amyloids: Or, perhaps amyloid is not a misnomer
    • Kisilevsky R., and Snow A. The potential significance of sulphated glycosaminoglycans as a common constituent of all amyloids: Or, perhaps amyloid is not a misnomer. Med. Hypoth. 26 (1988) 231-236
    • (1988) Med. Hypoth. , vol.26 , pp. 231-236
    • Kisilevsky, R.1    Snow, A.2
  • 158
    • 0029823198 scopus 로고    scopus 로고
    • Heparin-like glycosaminoglycans inhibit leukocyte adhesion to endotoxinactivated human vascular endothelial cells under nonstatic conditions
    • Kitamura N., Yamaguchi M., Shimabukuro K., Miyasaka M., Nakano H., and Kumada K. Heparin-like glycosaminoglycans inhibit leukocyte adhesion to endotoxinactivated human vascular endothelial cells under nonstatic conditions. Eur. Surg. Res. 28 (1996) 428-435
    • (1996) Eur. Surg. Res. , vol.28 , pp. 428-435
    • Kitamura, N.1    Yamaguchi, M.2    Shimabukuro, K.3    Miyasaka, M.4    Nakano, H.5    Kumada, K.6
  • 159
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interactions
    • Kjellén L., and Lindahl U. Proteoglycans: Structures and interactions. Ann. Rev. Biochem. 60 (1991) 443-475
    • (1991) Ann. Rev. Biochem. , vol.60 , pp. 443-475
    • Kjellén, L.1    Lindahl, U.2
  • 160
    • 0005026320 scopus 로고
    • Clearing factor, a heparin-activated lipoprotein lipase. II. Substrate specificity and activation of coconut oil
    • Korn E.D. Clearing factor, a heparin-activated lipoprotein lipase. II. Substrate specificity and activation of coconut oil. J. Biol. Chem. 215 (1955) 1-14
    • (1955) J. Biol. Chem. , vol.215 , pp. 1-14
    • Korn, E.D.1
  • 161
    • 0027920418 scopus 로고
    • Occurrence of 2-O-sulphated D-glucuronic acid in rat liver heparan sulphate
    • Kovensky J., and Cirelli A.F. Occurrence of 2-O-sulphated D-glucuronic acid in rat liver heparan sulphate. Carbohydr. Res. 245 (1993) 361-365
    • (1993) Carbohydr. Res. , vol.245 , pp. 361-365
    • Kovensky, J.1    Cirelli, A.F.2
  • 163
    • 0026094880 scopus 로고
    • Prevention of leucocyte elastase-induced emphysema in mice by heparin fragments
    • Lafuma C., Frisdal E., Harf A., Robert L., and Hornebeck W. Prevention of leucocyte elastase-induced emphysema in mice by heparin fragments. Eur. Respir. J. 4 (1991) 1004-1009
    • (1991) Eur. Respir. J. , vol.4 , pp. 1004-1009
    • Lafuma, C.1    Frisdal, E.2    Harf, A.3    Robert, L.4    Hornebeck, W.5
  • 164
    • 0025010849 scopus 로고
    • Immunosuppressive action of low-dose heparin: Effect on skin allograft survival
    • Lagodzinski Z., Górski A., and Wasik M. Immunosuppressive action of low-dose heparin: Effect on skin allograft survival. Transplantation 50 (1990) 714-715
    • (1990) Transplantation , vol.50 , pp. 714-715
    • Lagodzinski, Z.1    Górski, A.2    Wasik, M.3
  • 165
    • 0000200185 scopus 로고
    • Heparin binding and neutralizing proteins
    • Lane D.A., and Lindahl U. (Eds), CRC Press, Boca Raton, FL
    • Lane D.A. Heparin binding and neutralizing proteins. In: Lane D.A., and Lindahl U. (Eds). "Heparin Chemical and Biological Properties, Clinical Applications" (1989), CRC Press, Boca Raton, FL 363-391
    • (1989) "Heparin Chemical and Biological Properties, Clinical Applications" , pp. 363-391
    • Lane, D.A.1
  • 166
    • 0027933127 scopus 로고
    • Sulfatides trigger increase of cytosolic free calcium and enhance expression of tumor necrosis factor-α and interleukin-8 mRNA in human neutrophils: Evidence for a role of L-selectin as a signaling molecule
    • Laudanna C., Constantin G., Baron P., Scarpini E., Scarlato G., Cabrini G., Dechecchi C., Rossi F., Cassatella M.A., and Berton G. Sulfatides trigger increase of cytosolic free calcium and enhance expression of tumor necrosis factor-α and interleukin-8 mRNA in human neutrophils: Evidence for a role of L-selectin as a signaling molecule. J. Biol. Chem. 269 (1994) 4021-4026
    • (1994) J. Biol. Chem. , vol.269 , pp. 4021-4026
    • Laudanna, C.1    Constantin, G.2    Baron, P.3    Scarpini, E.4    Scarlato, G.5    Cabrini, G.6    Dechecchi, C.7    Rossi, F.8    Cassatella, M.A.9    Berton, G.10
  • 168
    • 0027409602 scopus 로고
    • The effects of high molecular weight- and low molecular weight-heparins on superoxide ion production and degranulation by human polymorphonuclear leukocytes
    • Léculier C., Couprie N., Adeleine P., Leitienne P., Francina A., and Richard M. The effects of high molecular weight- and low molecular weight-heparins on superoxide ion production and degranulation by human polymorphonuclear leukocytes. Thromb. Res. 69 (1993) 519-531
    • (1993) Thromb. Res. , vol.69 , pp. 519-531
    • Léculier, C.1    Couprie, N.2    Adeleine, P.3    Leitienne, P.4    Francina, A.5    Richard, M.6
  • 169
    • 0029866431 scopus 로고    scopus 로고
    • In vivo neutralization of eosinophil-derived major basic protein inhibits antigen-induced bronchial hyperreactivity in sensitized guinea pigs
    • Lefort J., Nahori M.-A., Ruffié C., Vargaftig B.B., and Pretolani M. In vivo neutralization of eosinophil-derived major basic protein inhibits antigen-induced bronchial hyperreactivity in sensitized guinea pigs. J. Clin. Invest. 87 (1996) 1117-1121
    • (1996) J. Clin. Invest. , vol.87 , pp. 1117-1121
    • Lefort, J.1    Nahori, M.-A.2    Ruffié, C.3    Vargaftig, B.B.4    Pretolani, M.5
  • 170
    • 0021953987 scopus 로고
    • Synthetic inhibitors of human leukocyte elastase. 1. Sulphated polysaccharides
    • Lentini A., Ternai B., and Ghosh P. Synthetic inhibitors of human leukocyte elastase. 1. Sulphated polysaccharides. Biochem. Int. 10 (1985) 221-232
    • (1985) Biochem. Int. , vol.10 , pp. 221-232
    • Lentini, A.1    Ternai, B.2    Ghosh, P.3
  • 171
    • 0029075585 scopus 로고
    • Leukocyte interactions with vascular endothelium: New insights into selectin-mediated attachment and rolling
    • Ley K., and Tedder T.F. Leukocyte interactions with vascular endothelium: New insights into selectin-mediated attachment and rolling. J. Immunol. 155 (1995) 525-528
    • (1995) J. Immunol. , vol.155 , pp. 525-528
    • Ley, K.1    Tedder, T.F.2
  • 172
    • 0027485436 scopus 로고
    • Intravenous interleukin-8 inhibits granulocyte emigration from rabbit mesenteric venules without altering I.-selectin expression or leukocyte rolling
    • Ley K., Baker J.B., Cybulsky M.I., Gimbrone Jr. M.A., and Luscinskas F.W. Intravenous interleukin-8 inhibits granulocyte emigration from rabbit mesenteric venules without altering I.-selectin expression or leukocyte rolling. J. Immunol. 151 (1993) 6347-6357
    • (1993) J. Immunol. , vol.151 , pp. 6347-6357
    • Ley, K.1    Baker, J.B.2    Cybulsky, M.I.3    Gimbrone Jr., M.A.4    Luscinskas, F.W.5
  • 173
    • 0025908182 scopus 로고
    • Sulfated polysaccharides inhibit leukocyte rolling in rabbit mesentery venules
    • Ley K., Cerrito M., and Arfors K.E. Sulfated polysaccharides inhibit leukocyte rolling in rabbit mesentery venules. Am. J. Physiol. 260 (1991) H1667-H1673
    • (1991) Am. J. Physiol. , vol.260
    • Ley, K.1    Cerrito, M.2    Arfors, K.E.3
  • 174
    • 0027178702 scopus 로고
    • L-selectin can mediate leukocyte rolling in untreated mesenteric venules in vivo independent of E- or P-selectin
    • Ley K., Tedder T.F., and Kansas G.S. L-selectin can mediate leukocyte rolling in untreated mesenteric venules in vivo independent of E- or P-selectin. Blood 82 (1993) 1632-1638
    • (1993) Blood , vol.82 , pp. 1632-1638
    • Ley, K.1    Tedder, T.F.2    Kansas, G.S.3
  • 175
    • 0030041932 scopus 로고    scopus 로고
    • Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin
    • Li F., Wilkins P.P., Crawley S., Weinstein J., Cummings R.D., and McEver R.P. Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin. J. Biol. Chem. 271 (1996) 3255-3264
    • (1996) J. Biol. Chem. , vol.271 , pp. 3255-3264
    • Li, F.1    Wilkins, P.P.2    Crawley, S.3    Weinstein, J.4    Cummings, R.D.5    McEver, R.P.6
  • 176
    • 0024590281 scopus 로고
    • Suppresion of experimental autoimmune diseases and prolongation of allograft survival by treatment of animals with low doses of heparin
    • Lider O., Baharav E., Mekeri Y.A., Miller T., Naparstek Y., Vlodavsky I., and Cohen I.R. Suppresion of experimental autoimmune diseases and prolongation of allograft survival by treatment of animals with low doses of heparin. J. Clin Invest. 83 (1989) 752-756
    • (1989) J. Clin Invest. , vol.83 , pp. 752-756
    • Lider, O.1    Baharav, E.2    Mekeri, Y.A.3    Miller, T.4    Naparstek, Y.5    Vlodavsky, I.6    Cohen, I.R.7
  • 179
    • 0027427953 scopus 로고
    • Biosynthesis of heparin/heparan sulfate-Identification of a 70-kDa protein catalyzing both the D-glucuronosyltransferase and the N-acetyl-D-glucosaminyltransferase reactions
    • Lind T., Lindahl U., and Lidholt K. Biosynthesis of heparin/heparan sulfate-Identification of a 70-kDa protein catalyzing both the D-glucuronosyltransferase and the N-acetyl-D-glucosaminyltransferase reactions. J. Biol. Chem. 268 (1993) 20705-20708
    • (1993) J. Biol. Chem. , vol.268 , pp. 20705-20708
    • Lind, T.1    Lindahl, U.2    Lidholt, K.3
  • 180
    • 0003024732 scopus 로고
    • Biosynthesis of heparin and related polysaccharides
    • Lane D.A., and Lindahl U. (Eds), CRC Press, Boca Raton, FL
    • Lindahl U. Biosynthesis of heparin and related polysaccharides. In: Lane D.A., and Lindahl U. (Eds). "Heparin Chemical and Biological Properties, Clinical Applications" (1989), CRC Press, Boca Raton, FL 159-189
    • (1989) "Heparin Chemical and Biological Properties, Clinical Applications" , pp. 159-189
    • Lindahl, U.1
  • 182
    • 0023741256 scopus 로고
    • Homogenous, structurally-defined heparin-oligosaccharides with low anticoagulant activity inhibit the generation of the amplification pathway C3 convertase in vitro
    • Lindhardt R.J., Rice K.G., Kim Y.S., Engelken J.D., and Weiler J.M. Homogenous, structurally-defined heparin-oligosaccharides with low anticoagulant activity inhibit the generation of the amplification pathway C3 convertase in vitro. J. Biol. Chem. 263 (1988) 13090-13096
    • (1988) J. Biol. Chem. , vol.263 , pp. 13090-13096
    • Lindhardt, R.J.1    Rice, K.G.2    Kim, Y.S.3    Engelken, J.D.4    Weiler, J.M.5
  • 183
    • 0030026692 scopus 로고    scopus 로고
    • Chemokines regulate T cell adherence to recombinant adhesion molecules and extracellular matrix proteins
    • Lloyd A.R., Oppenheim J.J., Kelvin D.J., and Taub D.D. Chemokines regulate T cell adherence to recombinant adhesion molecules and extracellular matrix proteins. J. Immunol. 156 (1996) 932-938
    • (1996) J. Immunol. , vol.156 , pp. 932-938
    • Lloyd, A.R.1    Oppenheim, J.J.2    Kelvin, D.J.3    Taub, D.D.4
  • 185
    • 0028173205 scopus 로고
    • Amyloid-associated proteins alpha(1)-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments
    • Ma J.Y., Yee A., Brewer H.B., Das S., and Potter H. Amyloid-associated proteins alpha(1)-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments. Nature 372 (1994) 92-94
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.Y.1    Yee, A.2    Brewer, H.B.3    Das, S.4    Potter, H.5
  • 186
    • 0028875976 scopus 로고
    • Synthesis of a divalent sialyl Lewis x O-glycan, a potent inhibitor of lymphocyte-endothelium adhesion; evidence that multivalency enhances the saccharide binding to L-selectin
    • Maaheimo H., Renkonen R., Turunen J.P., Penttila L., and Renkonen O. Synthesis of a divalent sialyl Lewis x O-glycan, a potent inhibitor of lymphocyte-endothelium adhesion; evidence that multivalency enhances the saccharide binding to L-selectin. Eur. J. Biochem. 234 (1995) 616-625
    • (1995) Eur. J. Biochem. , vol.234 , pp. 616-625
    • Maaheimo, H.1    Renkonen, R.2    Turunen, J.P.3    Penttila, L.4    Renkonen, O.5
  • 187
    • 0027448951 scopus 로고
    • Minimal sequences in heparin/heparan sulate required for binding of basic fibroblast growth factor
    • Maccarana M., Casu B., and Lindahl U. Minimal sequences in heparin/heparan sulate required for binding of basic fibroblast growth factor. J. Biol. Chem. 268 (1993) 23898-23905
    • (1993) J. Biol. Chem. , vol.268 , pp. 23898-23905
    • Maccarana, M.1    Casu, B.2    Lindahl, U.3
  • 188
    • 33846575792 scopus 로고
    • Intrapulmonary heparin as a prospective anticoagulant regimen
    • Fareed J., Messmore H.L., Fenton II J.W., and Brinkhous K.M. (Eds), Pergamon Press, New York
    • Mahadoo J., and Wright C.J. Intrapulmonary heparin as a prospective anticoagulant regimen. In: Fareed J., Messmore H.L., Fenton II J.W., and Brinkhous K.M. (Eds). "Perspectives in Hemostasis" (1981), Pergamon Press, New York 233-240
    • (1981) "Perspectives in Hemostasis" , pp. 233-240
    • Mahadoo, J.1    Wright, C.J.2
  • 189
    • 0019274454 scopus 로고
    • Endothelial sequestration of heparin administered by the intrapulmonary route
    • Mahadoo J., Hiebert L.M., Jaques L.B., and Wright C.J. Endothelial sequestration of heparin administered by the intrapulmonary route. Artery 7 (1980) 438-447
    • (1980) Artery , vol.7 , pp. 438-447
    • Mahadoo, J.1    Hiebert, L.M.2    Jaques, L.B.3    Wright, C.J.4
  • 191
    • 0019421197 scopus 로고
    • Effect of intrapulmonary heparin on lipoprotein lipase activity in mice
    • Mahadoo J., Wright C.J., and Jaques L.B. Effect of intrapulmonary heparin on lipoprotein lipase activity in mice. Atherosclerosis 28 (1981) 197-202
    • (1981) Atherosclerosis , vol.28 , pp. 197-202
    • Mahadoo, J.1    Wright, C.J.2    Jaques, L.B.3
  • 192
    • 0019459129 scopus 로고
    • Effect of intrapulmonary heparin on plasma diamine oxidase (histaminase) activity in mice
    • Mahadoo J., Wright C.J., and Jaques L.B. Effect of intrapulmonary heparin on plasma diamine oxidase (histaminase) activity in mice. Agents Actions 11 (1981) 335-338
    • (1981) Agents Actions , vol.11 , pp. 335-338
    • Mahadoo, J.1    Wright, C.J.2    Jaques, L.B.3
  • 193
    • 0025059489 scopus 로고
    • Structure of a dermatan sulfate hexasaccharide that binds to heparin cofactor II with high affinity
    • Maimone M.M., and Tollefsen D.M. Structure of a dermatan sulfate hexasaccharide that binds to heparin cofactor II with high affinity. J. Biol. Chem. 265 (1990) 18263-18271
    • (1990) J. Biol. Chem. , vol.265 , pp. 18263-18271
    • Maimone, M.M.1    Tollefsen, D.M.2
  • 194
    • 0028095114 scopus 로고
    • Competitive binding of vascular cell adhesion molecule-1 and the HepII/IIICS domain of fibronectin to the integrin α4β1
    • Makarem R., Newham P., Askari J.A., Green L.J., Clements J., Edwards M., Humphries M.J., and Mould A.P. Competitive binding of vascular cell adhesion molecule-1 and the HepII/IIICS domain of fibronectin to the integrin α4β1. J. Biol. Chem. 269 (1994) 4005-4011
    • (1994) J. Biol. Chem. , vol.269 , pp. 4005-4011
    • Makarem, R.1    Newham, P.2    Askari, J.A.3    Green, L.J.4    Clements, J.5    Edwards, M.6    Humphries, M.J.7    Mould, A.P.8
  • 195
    • 0030039839 scopus 로고    scopus 로고
    • Anionic phospholipids bind to L-selection (but not E-selectin) at a site distinct from the carbohydrate-binding site
    • Malhotra R., Taylor N.R., and Bird M.I. Anionic phospholipids bind to L-selection (but not E-selectin) at a site distinct from the carbohydrate-binding site. Biochem. J. 314 (1996) 297-303
    • (1996) Biochem. J. , vol.314 , pp. 297-303
    • Malhotra, R.1    Taylor, N.R.2    Bird, M.I.3
  • 198
    • 0021175343 scopus 로고
    • The inhibitory effect of heparin and related glycosaminoglycans on neutrophil chemotaxis
    • Matzner Y., Marx G., Drexler R., and Eldor A. The inhibitory effect of heparin and related glycosaminoglycans on neutrophil chemotaxis. Thromb. Haemostas. (Stuttgart) 52 (1984) 134-137
    • (1984) Thromb. Haemostas. (Stuttgart) , vol.52 , pp. 134-137
    • Matzner, Y.1    Marx, G.2    Drexler, R.3    Eldor, A.4
  • 200
    • 0029811901 scopus 로고    scopus 로고
    • Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiological studies
    • McGeer P.L., Schulzer M., and McGeer E.G. Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiological studies. Neurol. 47 (1996) 425-432
    • (1996) Neurol. , vol.47 , pp. 425-432
    • McGeer, P.L.1    Schulzer, M.2    McGeer, E.G.3
  • 201
    • 0002530711 scopus 로고
    • The discovery of heparin
    • McLean J. The discovery of heparin. Circulation 19 (1959) 75-78
    • (1959) Circulation , vol.19 , pp. 75-78
    • McLean, J.1
  • 202
    • 0024360749 scopus 로고
    • In vitro studies of the interaction of heparin, low molecular weight heparin and heparinoids with platelets
    • Messmore Jr. H.L., Griffin B., Fareed J., Coyne E., and Seghatchian J. In vitro studies of the interaction of heparin, low molecular weight heparin and heparinoids with platelets. Annals N. Y. Acad. Sci. 556 (1989) 217-232
    • (1989) Annals N. Y. Acad. Sci. , vol.556 , pp. 217-232
    • Messmore Jr., H.L.1    Griffin, B.2    Fareed, J.3    Coyne, E.4    Seghatchian, J.5
  • 203
    • 0028957585 scopus 로고
    • Therapeutic approaches to asthma based on VLA-4 integrin and its counter receptors
    • Metzger W.J. Therapeutic approaches to asthma based on VLA-4 integrin and its counter receptors. Springer Semin. Immunopathol. 16 (1995) 467-478
    • (1995) Springer Semin. Immunopathol. , vol.16 , pp. 467-478
    • Metzger, W.J.1
  • 204
    • 0026776079 scopus 로고
    • Biology and biochemistry of the chemokines: A family of chemotactic and inflammatory cytokines
    • Miller M.D., and Krangel M.S. Biology and biochemistry of the chemokines: A family of chemotactic and inflammatory cytokines. Crit. Rev. Immunol. 12 (1992) 17-46
    • (1992) Crit. Rev. Immunol. , vol.12 , pp. 17-46
    • Miller, M.D.1    Krangel, M.S.2
  • 205
    • 0025875453 scopus 로고
    • A lipophilic heparin derivative protects elastin against degradation by leucocyte elastase
    • Moczar E., and Hornebeck W. A lipophilic heparin derivative protects elastin against degradation by leucocyte elastase. Int. J. Biol. Macromol. 13 (1991) 261-262
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 261-262
    • Moczar, E.1    Hornebeck, W.2
  • 207
    • 0027992114 scopus 로고
    • The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine
    • Moore K.L., Eaton S.F., Lyons D.E., Lichenstein H.S., Cummings R.D., and McEver R.P. The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine. J. Biol. Chem. 269 (1994) 23318-23327
    • (1994) J. Biol. Chem. , vol.269 , pp. 23318-23327
    • Moore, K.L.1    Eaton, S.F.2    Lyons, D.E.3    Lichenstein, H.S.4    Cummings, R.D.5    McEver, R.P.6
  • 209
    • 0030184579 scopus 로고    scopus 로고
    • A novel non-anticoagulant heparin prevents vascular endothelial cell dysfunction during hyperdynamic sepsis
    • Morrison A.M., Wang P., and Chaudry I.H. A novel non-anticoagulant heparin prevents vascular endothelial cell dysfunction during hyperdynamic sepsis. Shock 6 (1996) 46-51
    • (1996) Shock , vol.6 , pp. 46-51
    • Morrison, A.M.1    Wang, P.2    Chaudry, I.H.3
  • 210
    • 0024500320 scopus 로고
    • Toxicity of eosinophil cationic proteins for guinea pig tracheal epithelium in vitro
    • Motojima S., Frigas E., Loegering D.A., and Gleich G.J. Toxicity of eosinophil cationic proteins for guinea pig tracheal epithelium in vitro. Am. Rev. Respir. Dis. 139 (1989) 801-805
    • (1989) Am. Rev. Respir. Dis. , vol.139 , pp. 801-805
    • Motojima, S.1    Frigas, E.2    Loegering, D.A.3    Gleich, G.J.4
  • 211
    • 0025932687 scopus 로고
    • Identification of a novel recognition sequence for the integrin α4β1 in the COOH-terminal heparin-binding domain of fibronectin
    • Mould A.P., and Humphries M.J. Identification of a novel recognition sequence for the integrin α4β1 in the COOH-terminal heparin-binding domain of fibronectin. EMBO J. 10 (1991) 4089-4095
    • (1991) EMBO J. , vol.10 , pp. 4089-4095
    • Mould, A.P.1    Humphries, M.J.2
  • 213
    • 0026716274 scopus 로고
    • Laminin and its neurite outgrowth-promoting domain in the brain in Alzheimer's disease and Down's syndrome patients
    • Murtomaki S., Risteli J., Risteli L., Koivisto U.M., Johansson S., and Liesi P. Laminin and its neurite outgrowth-promoting domain in the brain in Alzheimer's disease and Down's syndrome patients. J. Neurosci. Res. 32 (1992) 261-273
    • (1992) J. Neurosci. Res. , vol.32 , pp. 261-273
    • Murtomaki, S.1    Risteli, J.2    Risteli, L.3    Koivisto, U.M.4    Johansson, S.5    Liesi, P.6
  • 214
    • 0001916332 scopus 로고
    • Natural occurrence and possible biological role of heparin
    • Lane D.A., and Lindahl U. (Eds), CRC Press, Boca Raton, FL
    • Nader H.B., and Dietrich C.P. Natural occurrence and possible biological role of heparin. In: Lane D.A., and Lindahl U. (Eds). "Heparin Chemical and Biological Properties, Clinical Applications" (1989), CRC Press, Boca Raton, FL 81-96
    • (1989) "Heparin Chemical and Biological Properties, Clinical Applications" , pp. 81-96
    • Nader, H.B.1    Dietrich, C.P.2
  • 217
    • 0028934953 scopus 로고
    • An interaction between basement membrane and Alzheimer amyloid precursor proteins suggests a role in the pathogenesis of Alzheimer's disease
    • Narindrasorasak S., Altman R.A., Gonzalezdewhitt P., Greenberg B.D., and Kisilevsky R. An interaction between basement membrane and Alzheimer amyloid precursor proteins suggests a role in the pathogenesis of Alzheimer's disease. Lab. Invest. 72 (1995) 272-282
    • (1995) Lab. Invest. , vol.72 , pp. 272-282
    • Narindrasorasak, S.1    Altman, R.A.2    Gonzalezdewhitt, P.3    Greenberg, B.D.4    Kisilevsky, R.5
  • 218
    • 0023781359 scopus 로고
    • Endothelial functional responses and increased vascular permeability induced by polycations
    • Needham L., Hellewell P.G., Williams T.J., and Gordon J.L. Endothelial functional responses and increased vascular permeability induced by polycations. Lab. Invest. 59 (1988) 538-548
    • (1988) Lab. Invest. , vol.59 , pp. 538-548
    • Needham, L.1    Hellewell, P.G.2    Williams, T.J.3    Gordon, J.L.4
  • 219
    • 0013802211 scopus 로고
    • The effects of anticoagulants and other drugs on cellular and cutaneous reactions to antigen in guinea-pigs with delayed-type hypersensitivity
    • Nelson D.S. The effects of anticoagulants and other drugs on cellular and cutaneous reactions to antigen in guinea-pigs with delayed-type hypersensitivity. Immunology 9 (1965) 219-234
    • (1965) Immunology , vol.9 , pp. 219-234
    • Nelson, D.S.1
  • 221
    • 0028949437 scopus 로고
    • Eosinophil granule proteins in cardiopulmonary bypass with and without heparin coating
    • Nilsson L., Peterson C., Venge P., Borowiec J.W., and Thelin S. Eosinophil granule proteins in cardiopulmonary bypass with and without heparin coating. Ann. Thorac. Surg. 59 (1995) 713-716
    • (1995) Ann. Thorac. Surg. , vol.59 , pp. 713-716
    • Nilsson, L.1    Peterson, C.2    Venge, P.3    Borowiec, J.W.4    Thelin, S.5
  • 222
    • 0027216123 scopus 로고
    • Characterization of a specific ligand for P-selectin on myeloid cells: A minor glycoprotein with sialylated O-linked oligosaccharides
    • Norgard K.E., Moore K.L., Diaz S., Stults N.L., Ushiyama S., McEver R.P., Cummings R.D., and Varki A. Characterization of a specific ligand for P-selectin on myeloid cells: A minor glycoprotein with sialylated O-linked oligosaccharides. J. Biol. Chem. 268 (1993) 12764-12774
    • (1993) J. Biol. Chem. , vol.268 , pp. 12764-12774
    • Norgard, K.E.1    Moore, K.L.2    Diaz, S.3    Stults, N.L.4    Ushiyama, S.5    McEver, R.P.6    Cummings, R.D.7    Varki, A.8
  • 223
    • 0029043456 scopus 로고
    • Endothelial heparan sulfate proteoglycans that bind to L-selectin have glycosamine residues with unsubstituted amino groups
    • Norgard-Sumnicht K., and Varki A. Endothelial heparan sulfate proteoglycans that bind to L-selectin have glycosamine residues with unsubstituted amino groups. J. Biol. Chem. 270 (1995) 12012-12024
    • (1995) J. Biol. Chem. , vol.270 , pp. 12012-12024
    • Norgard-Sumnicht, K.1    Varki, A.2
  • 224
    • 0027248439 scopus 로고
    • Calcium-dependent heparinlike ligands for L-selectin in nonlymphoid endothelial cells
    • Norgard-Sumnicht K.E., Varki N.M., and Varki A. Calcium-dependent heparinlike ligands for L-selectin in nonlymphoid endothelial cells. Science 261 (1993) 480-483
    • (1993) Science , vol.261 , pp. 480-483
    • Norgard-Sumnicht, K.E.1    Varki, N.M.2    Varki, A.3
  • 225
    • 0029443410 scopus 로고
    • Molecular and cellular interactions mediating granulocyte accumulation in vivo
    • Nourshargh S., and Williams T.J. Molecular and cellular interactions mediating granulocyte accumulation in vivo. Sem. Cell Biol. 6 (1995) 317-326
    • (1995) Sem. Cell Biol. , vol.6 , pp. 317-326
    • Nourshargh, S.1    Williams, T.J.2
  • 226
    • 0013630798 scopus 로고
    • Inhaled heparin does not protect asthmatics against antigen-induced brochconstriction
    • Part 2, [Abstract]
    • O'Donnell W.J., Rosenberg M.A., Kelleher K., Drazen J.M., and Israel E. Inhaled heparin does not protect asthmatics against antigen-induced brochconstriction. Am. Rev. Respir, Dis. 145 (1992) A422 Part 2, [Abstract]
    • (1992) Am. Rev. Respir, Dis. , vol.145
    • O'Donnell, W.J.1    Rosenberg, M.A.2    Kelleher, K.3    Drazen, J.M.4    Israel, E.5
  • 228
    • 0025374844 scopus 로고
    • Heparin, a potent releasing agent of extracellular superoxide dismutase (ecsod C), suppresses ischaemic paw oedema in mice
    • Oyanagui Y., and Sato S. Heparin, a potent releasing agent of extracellular superoxide dismutase (ecsod C), suppresses ischaemic paw oedema in mice. Free Rad. Res. Commun. 9 (1990) 87-99
    • (1990) Free Rad. Res. Commun. , vol.9 , pp. 87-99
    • Oyanagui, Y.1    Sato, S.2
  • 229
    • 0025974938 scopus 로고
    • 2 agonists
    • 2 agonists. Lancet 337 (1991) 717-720
    • (1991) Lancet , vol.337 , pp. 717-720
    • Page, C.P.1
  • 230
    • 0026535690 scopus 로고
    • Regulatory mechanisms in leukocyte adhesion: Flexible receptors for sophisticated travelers
    • Pardi R., Inverardi L., and Bender J.R. Regulatory mechanisms in leukocyte adhesion: Flexible receptors for sophisticated travelers. Immunol. Today 13 (1992) 224-230
    • (1992) Immunol. Today , vol.13 , pp. 224-230
    • Pardi, R.1    Inverardi, L.2    Bender, J.R.3
  • 231
    • 0028243327 scopus 로고
    • Treatment of interstitial cystitis with intravesical heparin
    • Parsons C.L., Housley T., Schmidt J.D., and Lebow D. Treatment of interstitial cystitis with intravesical heparin. Br. J. Urol. 73 (1994) 504-507
    • (1994) Br. J. Urol. , vol.73 , pp. 504-507
    • Parsons, C.L.1    Housley, T.2    Schmidt, J.D.3    Lebow, D.4
  • 232
    • 0031001403 scopus 로고    scopus 로고
    • Epithelial coating techniques in the treatment of interstitial cystitis
    • Parsons C.W. Epithelial coating techniques in the treatment of interstitial cystitis. Urology 49 Suppl 5A (1997) 100-104
    • (1997) Urology , vol.49 , Issue.SUPPL. 5A , pp. 100-104
    • Parsons, C.W.1
  • 233
    • 0021136255 scopus 로고
    • Heparin inhibition of polymorphonuclear leukocyte activation in vitro: A possible pharmacological approach to granulocyte-mediated vascular damage
    • Pasini F.L., Pasqui A.L., Ceccatelli L., Capecchi P.L., Orrico A., and di Perri T. Heparin inhibition of polymorphonuclear leukocyte activation in vitro: A possible pharmacological approach to granulocyte-mediated vascular damage. Thromb. Res. 35 (1984) 527-537
    • (1984) Thromb. Res. , vol.35 , pp. 527-537
    • Pasini, F.L.1    Pasqui, A.L.2    Ceccatelli, L.3    Capecchi, P.L.4    Orrico, A.5    di Perri, T.6
  • 234
    • 0030027308 scopus 로고    scopus 로고
    • The effect of inhaled heparin on bronchial reactivity to sodium metabisulphite and methacholine in patients with asthma
    • Pavord I., Mudassar T., Bennett J., Wilding P., and Knox A. The effect of inhaled heparin on bronchial reactivity to sodium metabisulphite and methacholine in patients with asthma. Eur. J. Respir. 9 (1996) 217-219
    • (1996) Eur. J. Respir. , vol.9 , pp. 217-219
    • Pavord, I.1    Mudassar, T.2    Bennett, J.3    Wilding, P.4    Knox, A.5
  • 235
    • 0028060098 scopus 로고
    • Binding of fluorescent-labeled low molecular mass heparin to latex microspheres and to rat and human leukocytes
    • Piazolo L., Harenberg J., Malsch R., and Heene D.L. Binding of fluorescent-labeled low molecular mass heparin to latex microspheres and to rat and human leukocytes. Semin. Thromb. Hemost. 20 (1994) 227-235
    • (1994) Semin. Thromb. Hemost. , vol.20 , pp. 227-235
    • Piazolo, L.1    Harenberg, J.2    Malsch, R.3    Heene, D.L.4
  • 236
    • 0028863479 scopus 로고
    • PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus
    • Pouyani T., and Seed B. PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus. Cell 83 (1995) 333-343
    • (1995) Cell , vol.83 , pp. 333-343
    • Pouyani, T.1    Seed, B.2
  • 237
    • 85064188168 scopus 로고    scopus 로고
    • Effect of heparin on antigen-induced airway responses in neonatally immunized rabbits
    • [Abstract]
    • Preuss J.M.H., and Page C.P. Effect of heparin on antigen-induced airway responses in neonatally immunized rabbits. Am. J. Hosp. Crit. Care Med. 153 (1996) A627 [Abstract]
    • (1996) Am. J. Hosp. Crit. Care Med. , vol.153
    • Preuss, J.M.H.1    Page, C.P.2
  • 238
    • 0023902288 scopus 로고
    • N-desulfated/acetylated heparin ameliorates the progression of renal disease in rats with subtotal renal ablation
    • Purkerson M.L., Tollefsen D.M., and Klahr S. N-desulfated/acetylated heparin ameliorates the progression of renal disease in rats with subtotal renal ablation. J. Clin. Invest. 81 (1988) 69-74
    • (1988) J. Clin. Invest. , vol.81 , pp. 69-74
    • Purkerson, M.L.1    Tollefsen, D.M.2    Klahr, S.3
  • 239
    • 0028903860 scopus 로고
    • Heparin: Pharmacological potentials from atherosclerosis to asthma
    • Ragazzi E., and Chinellato A. Heparin: Pharmacological potentials from atherosclerosis to asthma. Gen. Pharmacol. 26 (1995) 697-701
    • (1995) Gen. Pharmacol. , vol.26 , pp. 697-701
    • Ragazzi, E.1    Chinellato, A.2
  • 240
    • 0027327787 scopus 로고
    • Effects of glycosaminoglycans on platelet and leucocyte function: Role of N-sulfation
    • Rajtar G., Marchi E., de Gaetano G., and Cerletti C. Effects of glycosaminoglycans on platelet and leucocyte function: Role of N-sulfation. Biochem. Pharmacol. 46 (1993) 958-960
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 958-960
    • Rajtar, G.1    Marchi, E.2    de Gaetano, G.3    Cerletti, C.4
  • 241
    • 77956721649 scopus 로고
    • Heparin administration before or after hemorrhagic shock protects microvascular patency
    • Rana M.W., Singh G., Wang P., Dean R.E., and Chaudry I.H. Heparin administration before or after hemorrhagic shock protects microvascular patency. Circ. Shock 31 (1990) 59-60
    • (1990) Circ. Shock , vol.31 , pp. 59-60
    • Rana, M.W.1    Singh, G.2    Wang, P.3    Dean, R.E.4    Chaudry, I.H.5
  • 242
    • 0026695229 scopus 로고
    • Protective effects of preheparinization on the microvasculature during and after hemorrhagic shock
    • Rana M.W., Singh G., Wang P., Ayala A., Zhou M., and Chaudry I.H. Protective effects of preheparinization on the microvasculature during and after hemorrhagic shock. J. Trauma 32 (1992) 420-426
    • (1992) J. Trauma , vol.32 , pp. 420-426
    • Rana, M.W.1    Singh, G.2    Wang, P.3    Ayala, A.4    Zhou, M.5    Chaudry, I.H.6
  • 243
    • 0025289208 scopus 로고
    • Sulfated polysaccharides prevent human leukocyte elastase-induced acute lung injury and emphysema in hamsters
    • Rao N.V., Kennedy T.P., Rao G., Ky N., and Hoidal J.R. Sulfated polysaccharides prevent human leukocyte elastase-induced acute lung injury and emphysema in hamsters. Am. Rev. Respir. Dis. 142 (1990) 407-412
    • (1990) Am. Rev. Respir. Dis. , vol.142 , pp. 407-412
    • Rao, N.V.1    Kennedy, T.P.2    Rao, G.3    Ky, N.4    Hoidal, J.R.5
  • 244
    • 0029011878 scopus 로고
    • Biosynthesis of heparin/heparan sulfate
    • Razi N., and Lindahl U. Biosynthesis of heparin/heparan sulfate. J. Biol. Chem. 270 (1995) 11267-11275
    • (1995) J. Biol. Chem. , vol.270 , pp. 11267-11275
    • Razi, N.1    Lindahl, U.2
  • 247
    • 0028980134 scopus 로고
    • Inhibition of superoxide production in human neutrophils by combinations of heparin and thrombolytic agents
    • Riesenberg K., Schlaeffer F., Katz A., and Levy R. Inhibition of superoxide production in human neutrophils by combinations of heparin and thrombolytic agents. Br. Heart J. 73 (1995) 14-19
    • (1995) Br. Heart J. , vol.73 , pp. 14-19
    • Riesenberg, K.1    Schlaeffer, F.2    Katz, A.3    Levy, R.4
  • 250
    • 0028362088 scopus 로고
    • The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent
    • Romanic A.M., and Madri J.A. The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent. J. Cell Biol. 125 (1994) 1165-1178
    • (1994) J. Cell Biol. , vol.125 , pp. 1165-1178
    • Romanic, A.M.1    Madri, J.A.2
  • 252
    • 0027207854 scopus 로고
    • A causal role for amyloid in Alzheimer's disease-The end of the beginning
    • Rosenberg R.N. A causal role for amyloid in Alzheimer's disease-The end of the beginning. Neurology 43 (1993) 851-856
    • (1993) Neurology , vol.43 , pp. 851-856
    • Rosenberg, R.N.1
  • 253
    • 0007953997 scopus 로고
    • Heparin administered as an aerosol
    • Rosner S.W. Heparin administered as an aerosol. Vasc. Dis. 2 (1965) 131-134
    • (1965) Vasc. Dis. , vol.2 , pp. 131-134
    • Rosner, S.W.1
  • 254
    • 0026694563 scopus 로고
    • Endothelial cell binding of NAP-1/IL-8: Role in neutrophil emigration
    • Rot A. Endothelial cell binding of NAP-1/IL-8: Role in neutrophil emigration. Immunol. Today 13 (1992) 291-294
    • (1992) Immunol. Today , vol.13 , pp. 291-294
    • Rot, A.1
  • 255
    • 0026924154 scopus 로고
    • Binding of neutrophil attractant/activation protein-1 (interleukin 8) to resident dermal cells
    • Rot A. Binding of neutrophil attractant/activation protein-1 (interleukin 8) to resident dermal cells. Cytokine 4 (1992) 347-352
    • (1992) Cytokine , vol.4 , pp. 347-352
    • Rot, A.1
  • 256
    • 0029559628 scopus 로고
    • C-C chemokines, but not the C-X-C chemokines interleukin-8 and interferon-γ inducible protein-10, stimulate transendothelial chemotaxis of T lymphocytes
    • Roth S.J., Carr M.W., and Springer T.A. C-C chemokines, but not the C-X-C chemokines interleukin-8 and interferon-γ inducible protein-10, stimulate transendothelial chemotaxis of T lymphocytes. Eur. J. Immunol. 25 (1995) 3482-3488
    • (1995) Eur. J. Immunol. , vol.25 , pp. 3482-3488
    • Roth, S.J.1    Carr, M.W.2    Springer, T.A.3
  • 257
    • 0024402592 scopus 로고
    • Proteoglycans in cell recognition
    • Ruoslahti E. Proteoglycans in cell recognition. J. Biol. Chem. 264 (1989) 13369-13372
    • (1989) J. Biol. Chem. , vol.264 , pp. 13369-13372
    • Ruoslahti, E.1
  • 258
    • 0031057994 scopus 로고    scopus 로고
    • A monoclonal antibody against very late activation antigen-4 inhibits eosinophil accumulation and late asthmatic response in a guinea pig model of asthma
    • Sagara H., Matsuda H., Wada N., Yagita H., Fukuda T., Okumura K., Makino S., and Ra C. A monoclonal antibody against very late activation antigen-4 inhibits eosinophil accumulation and late asthmatic response in a guinea pig model of asthma. Int. Arch. Allergy Immunol. 112 (1997) 287-294
    • (1997) Int. Arch. Allergy Immunol. , vol.112 , pp. 287-294
    • Sagara, H.1    Matsuda, H.2    Wada, N.3    Yagita, H.4    Fukuda, T.5    Okumura, K.6    Makino, S.7    Ra, C.8
  • 259
    • 0028885684 scopus 로고
    • A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding
    • Sako D., Comess K.M., Barone K.M., Camphausen R.T., Cumming D.A., and Shaw G.D. A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding. Cell 83 (1995) 323-331
    • (1995) Cell , vol.83 , pp. 323-331
    • Sako, D.1    Comess, K.M.2    Barone, K.M.3    Camphausen, R.T.4    Cumming, D.A.5    Shaw, G.D.6
  • 260
    • 0017319346 scopus 로고
    • Effects of heparin in large doses on the extent of myocardial ischemia after acute coronary occlusion in the dog
    • Saliba Jr. M.J., Covell J.W., and Bloor C.M. Effects of heparin in large doses on the extent of myocardial ischemia after acute coronary occlusion in the dog. Am. J. Cardiology 37 (1976) 599-603
    • (1976) Am. J. Cardiology , vol.37 , pp. 599-603
    • Saliba Jr., M.J.1    Covell, J.W.2    Bloor, C.M.3
  • 261
    • 0028786553 scopus 로고
    • Syndecan family of cell surface proteoglycans: Developmentally regulated receptors for extracellular effector molecules
    • Salmivirta M., and Jalkanen M. Syndecan family of cell surface proteoglycans: Developmentally regulated receptors for extracellular effector molecules. Experientia 51 (1995) 863-872
    • (1995) Experientia , vol.51 , pp. 863-872
    • Salmivirta, M.1    Jalkanen, M.2
  • 262
    • 0023764067 scopus 로고
    • Cytophilic and cytotoxic properties of human eosinophil peroxidase plus major basic protein
    • Samoszuk M.K., Petersen A., Gidanian F., and Rietveld C. Cytophilic and cytotoxic properties of human eosinophil peroxidase plus major basic protein. Am. J. Pathol. 132 (1988) 455-460
    • (1988) Am. J. Pathol. , vol.132 , pp. 455-460
    • Samoszuk, M.K.1    Petersen, A.2    Gidanian, F.3    Rietveld, C.4
  • 264
    • 0027182251 scopus 로고
    • Effect of heparin and a low-molecular weight hepariniod on PAF-induced airway responses in neonatally immunized rabbits
    • Sasaki M., Herd C.M., and Page C.P. Effect of heparin and a low-molecular weight hepariniod on PAF-induced airway responses in neonatally immunized rabbits. Br. J. Pharmacol. 110 (1993) 107-112
    • (1993) Br. J. Pharmacol. , vol.110 , pp. 107-112
    • Sasaki, M.1    Herd, C.M.2    Page, C.P.3
  • 265
    • 13344295095 scopus 로고    scopus 로고
    • Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor
    • Savage B., Saldivar E., and Ruggeri Z.M. Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor. Cell 84 (1996) 289-297
    • (1996) Cell , vol.84 , pp. 289-297
    • Savage, B.1    Saldivar, E.2    Ruggeri, Z.M.3
  • 266
    • 0028825543 scopus 로고
    • Regulation of growth factor activation by proteoglycans: What is the role of the low affinity receptors?
    • Schlessinger J., Lax I., and Lemmon M. Regulation of growth factor activation by proteoglycans: What is the role of the low affinity receptors?. Cell 83 (1995) 357-360
    • (1995) Cell , vol.83 , pp. 357-360
    • Schlessinger, J.1    Lax, I.2    Lemmon, M.3
  • 267
    • 0027270904 scopus 로고
    • The effect of heparin and related proteoglycans on allergen and PAF-induced eosinophil infiltration
    • Seeds E.A.M., Hanss J., and Page C.P. The effect of heparin and related proteoglycans on allergen and PAF-induced eosinophil infiltration. J. Lipid Mediators 7 (1993) 269-278
    • (1993) J. Lipid Mediators , vol.7 , pp. 269-278
    • Seeds, E.A.M.1    Hanss, J.2    Page, C.P.3
  • 268
    • 0029564079 scopus 로고
    • The effect of inhaled heparin and related glycosaminoglycans on allergen-induced eosinophil infiltration in guinea-pigs
    • Seeds E.A.M., Horne A.P., Tyrrell D.J., and Page C.P. The effect of inhaled heparin and related glycosaminoglycans on allergen-induced eosinophil infiltration in guinea-pigs. Pulm. Pharmacol. 8 (1995) 97-105
    • (1995) Pulm. Pharmacol. , vol.8 , pp. 97-105
    • Seeds, E.A.M.1    Horne, A.P.2    Tyrrell, D.J.3    Page, C.P.4
  • 269
    • 17144437307 scopus 로고    scopus 로고
    • Polysulfated derivatives of β-cyclodextrin and myo-inositol as potent inhibitors of the interaction between L-selectin and peripheral addressin: Implying a requirement for highly clustered sulfate groups
    • Shailubhai K., Abbas S.Z., and Jacob G.S. Polysulfated derivatives of β-cyclodextrin and myo-inositol as potent inhibitors of the interaction between L-selectin and peripheral addressin: Implying a requirement for highly clustered sulfate groups. Biochem. Biophys. Res. Commun. 229 (1996) 488-493
    • (1996) Biochem. Biophys. Res. Commun. , vol.229 , pp. 488-493
    • Shailubhai, K.1    Abbas, S.Z.2    Jacob, G.S.3
  • 270
    • 0030932520 scopus 로고    scopus 로고
    • Sulfation and sialylation requirements for a glycoform of CD34, a major endothelial ligand for L-selectin in porcine peripheral lymph nodes
    • Shailubhai K., Streeter P.R., Smith C.E., and Jacob G.S. Sulfation and sialylation requirements for a glycoform of CD34, a major endothelial ligand for L-selectin in porcine peripheral lymph nodes. Glycobiology 7 (1997) 305-314
    • (1997) Glycobiology , vol.7 , pp. 305-314
    • Shailubhai, K.1    Streeter, P.R.2    Smith, C.E.3    Jacob, G.S.4
  • 272
    • 0025203323 scopus 로고
    • Mechanism of acute gastrointestinal mucosal damage in endotoxic shock and the effect of Fragmin
    • Shiba T., Ikeda M., Hara A., Yoshida H., Kaneko H., and Takeuchi S. Mechanism of acute gastrointestinal mucosal damage in endotoxic shock and the effect of Fragmin. Semin. Thromb. Hemost. 16 (1990) 55-59
    • (1990) Semin. Thromb. Hemost. , vol.16 , pp. 55-59
    • Shiba, T.1    Ikeda, M.2    Hara, A.3    Yoshida, H.4    Kaneko, H.5    Takeuchi, S.6
  • 273
    • 0028356562 scopus 로고
    • Interleukin-8 is a potent eosinophil chemo-attractant
    • Shute J. Interleukin-8 is a potent eosinophil chemo-attractant. Clin. Exper. Allergy 24 (1994) 203-206
    • (1994) Clin. Exper. Allergy , vol.24 , pp. 203-206
    • Shute, J.1
  • 274
    • 0014199233 scopus 로고
    • Biosynthesis of heparin: Formation of a sulfated glycosaminoglycan with a microsomal preparation from mast tumor cells
    • Silbert J.E. Biosynthesis of heparin: Formation of a sulfated glycosaminoglycan with a microsomal preparation from mast tumor cells. J. Biol. Chem. 242 (1967) 5153-5157
    • (1967) J. Biol. Chem. , vol.242 , pp. 5153-5157
    • Silbert, J.E.1
  • 277
    • 0027178226 scopus 로고
    • Restoration of gut absorptive capacity following trauma-hemorrhagic shock by the adjuvant use of heparan sulfate
    • Singh G., Chaudry K.L., and Chaudry I.H. Restoration of gut absorptive capacity following trauma-hemorrhagic shock by the adjuvant use of heparan sulfate. J. Trauma 34 (1993) 645-652
    • (1993) J. Trauma , vol.34 , pp. 645-652
    • Singh, G.1    Chaudry, K.L.2    Chaudry, I.H.3
  • 278
    • 0029589219 scopus 로고
    • Lysolecithin-induced alteration of subendothelial heparan sulfate proteoglycans increases monocyte binding to matrix
    • Sivaram P., Obunike J.C., and Goldberg I.J. Lysolecithin-induced alteration of subendothelial heparan sulfate proteoglycans increases monocyte binding to matrix. J. Biol. Chem. 270 (1995) 29760-29765
    • (1995) J. Biol. Chem. , vol.270 , pp. 29760-29765
    • Sivaram, P.1    Obunike, J.C.2    Goldberg, I.J.3
  • 281
    • 0025299641 scopus 로고
    • Tumor necrosis factor α/cachectin stimulates eosinophil oxidant production and toxicity towards human endothelium
    • Slungaard A., Vercellotti G.M., Walker G., Nelson R.D., and Jacob H.S. Tumor necrosis factor α/cachectin stimulates eosinophil oxidant production and toxicity towards human endothelium. J. Exp. Med. 171 (1990) 2025-2041
    • (1990) J. Exp. Med. , vol.171 , pp. 2025-2041
    • Slungaard, A.1    Vercellotti, G.M.2    Walker, G.3    Nelson, R.D.4    Jacob, H.S.5
  • 282
    • 0028213567 scopus 로고
    • A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth
    • Small D.H., Nurcombe V., Reed G., Clarris H., Moir R., Beyreuther K., and Masters C.L. A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth. J. Neurosci. 14 (1994) 2117-2127
    • (1994) J. Neurosci. , vol.14 , pp. 2117-2127
    • Small, D.H.1    Nurcombe, V.2    Reed, G.3    Clarris, H.4    Moir, R.5    Beyreuther, K.6    Masters, C.L.7
  • 283
    • 0020320712 scopus 로고
    • Localization of two unique heparin binding domains of human plasma fibronectin with monoclonal antibodies
    • Smith D.E., and Furcht L.T. Localization of two unique heparin binding domains of human plasma fibronectin with monoclonal antibodies. J. Biol. Chem. 257 (1982) 6518-6524
    • (1982) J. Biol. Chem. , vol.257 , pp. 6518-6524
    • Smith, D.E.1    Furcht, L.T.2
  • 284
    • 0024387388 scopus 로고
    • Proteoglycans in the pathogenesis of Alzheimer's disease and other amyloidoses
    • Snow A.D., and Wight T.N. Proteoglycans in the pathogenesis of Alzheimer's disease and other amyloidoses. Neurobiol. Aging 10 (1989) 481-497
    • (1989) Neurobiol. Aging , vol.10 , pp. 481-497
    • Snow, A.D.1    Wight, T.N.2
  • 285
    • 0029047722 scopus 로고
    • Differential binding of vascular cell-derived proteoglycans (perlecan, biglycan, decorin and versican) to the beta-amyloid protein of Alzheimer's disease
    • Snow A.D., Kinsella M.G., Parkes E., Sekiguchi R.T., Miller J.D., Kimata K., and Wight T.N. Differential binding of vascular cell-derived proteoglycans (perlecan, biglycan, decorin and versican) to the beta-amyloid protein of Alzheimer's disease. Arch. Biochem. Biophys. 320 (1995) 84-95
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 84-95
    • Snow, A.D.1    Kinsella, M.G.2    Parkes, E.3    Sekiguchi, R.T.4    Miller, J.D.5    Kimata, K.6    Wight, T.N.7
  • 286
    • 0024339115 scopus 로고
    • Cationic dyes reveal proteoglycans structurally integrated within the characteristic lesions of Alzheimer's disease
    • Snow A.D., Lara S., Nochlin D., and Wight T.N. Cationic dyes reveal proteoglycans structurally integrated within the characteristic lesions of Alzheimer's disease. Acta neuropathologica. 78 (1989) 113-123
    • (1989) Acta neuropathologica. , vol.78 , pp. 113-123
    • Snow, A.D.1    Lara, S.2    Nochlin, D.3    Wight, T.N.4
  • 287
    • 0024273721 scopus 로고
    • The presence of heparan sulfate proteoglycan in the neuritic plaques and congophilic angiopathy in Alzheimer's disease
    • Snow A.D., Mar H., Nochlin D., Kimata K., Kato M., Suzuki S., Hassell J., and Wight T.N. The presence of heparan sulfate proteoglycan in the neuritic plaques and congophilic angiopathy in Alzheimer's disease. Am. J. Pathol. 133 (1988) 456-463
    • (1988) Am. J. Pathol. , vol.133 , pp. 456-463
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Kimata, K.4    Kato, M.5    Suzuki, S.6    Hassell, J.7    Wight, T.N.8
  • 288
    • 0025223441 scopus 로고
    • Early accumulation of heparan sulfate in neurons and in the beta amyloid protein-containing lesions of Alzheimer's disease and Down's syndrome
    • Snow A.D., Mar H., Nochlin D., Sekiguchi R.T., Kimata K., Koike Y., and Wight T.N. Early accumulation of heparan sulfate in neurons and in the beta amyloid protein-containing lesions of Alzheimer's disease and Down's syndrome. Am. J. Pathol. 137 (1990) 1253-1270
    • (1990) Am. J. Pathol. , vol.137 , pp. 1253-1270
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Sekiguchi, R.T.4    Kimata, K.5    Koike, Y.6    Wight, T.N.7
  • 289
    • 0028082136 scopus 로고
    • An important role of heparan sulfate proteoglycan (perlecan) in a model system of the deposition and persistence of fibrillar A beta-amyloid in rat brain
    • Snow A.D., Sekiguchi R.T., Nochlin D., Fraser P., Kinsella M.G., Mizutani A., Arai M., Schreier W.A., and Morgan D.G. An important role of heparan sulfate proteoglycan (perlecan) in a model system of the deposition and persistence of fibrillar A beta-amyloid in rat brain. Neuron 12 (1994) 219-234
    • (1994) Neuron , vol.12 , pp. 219-234
    • Snow, A.D.1    Sekiguchi, R.T.2    Nochlin, D.3    Fraser, P.4    Kinsella, M.G.5    Mizutani, A.6    Arai, M.7    Schreier, W.A.8    Morgan, D.G.9
  • 290
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer T.A. Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm. Cell 76 (1994) 301-314
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 291
    • 0028935791 scopus 로고
    • Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration
    • Springer T.A. Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration. Annu. Rev. Physiol. 57 (1995) 827-872
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 827-872
    • Springer, T.A.1
  • 292
    • 0027479415 scopus 로고
    • Heparin prevents postischemic endothelial cell dysfunction by a mechanism independent of its anticoagulant activity
    • Sternbergh III W.C., Makhoul R.G., and Adelman B. Heparin prevents postischemic endothelial cell dysfunction by a mechanism independent of its anticoagulant activity. J. Vasc. Surg. 17 (1993) 318-327
    • (1993) J. Vasc. Surg. , vol.17 , pp. 318-327
    • Sternbergh III, W.C.1    Makhoul, R.G.2    Adelman, B.3
  • 293
    • 0028969043 scopus 로고
    • Heparinoids with low anticoagulant potency attenuate postischemic endothelial cell dysfunction
    • Sternbergh III W.C., Sobel M., and Makhoul R.G. Heparinoids with low anticoagulant potency attenuate postischemic endothelial cell dysfunction. J. Vasc. Surg. 21 (1995) 477-483
    • (1995) J. Vasc. Surg. , vol.21 , pp. 477-483
    • Sternbergh III, W.C.1    Sobel, M.2    Makhoul, R.G.3
  • 294
    • 0028118405 scopus 로고
    • Cerebroglycan-An integral membrane heparan sulfate proteoglycan that is unique to the developing nervous system and expressed specifically during neuronal differentiation
    • Stipp C.S., Litwack E.D., and Lander A.D. Cerebroglycan-An integral membrane heparan sulfate proteoglycan that is unique to the developing nervous system and expressed specifically during neuronal differentiation. J. Cell Biol. 124 (1994) 149-160
    • (1994) J. Cell Biol. , vol.124 , pp. 149-160
    • Stipp, C.S.1    Litwack, E.D.2    Lander, A.D.3
  • 298
    • 0028302030 scopus 로고
    • Eosinophil adhesion to nasal polyp endothelium is P-selectin-dependent
    • Symon F.A., Walsh G.M., Watson S.R., and Wardlaw A.J. Eosinophil adhesion to nasal polyp endothelium is P-selectin-dependent. J. Exp. Med. 180 (1994) 371-376
    • (1994) J. Exp. Med. , vol.180 , pp. 371-376
    • Symon, F.A.1    Walsh, G.M.2    Watson, S.R.3    Wardlaw, A.J.4
  • 299
  • 300
    • 0027408343 scopus 로고
    • Proteoglycans on endothelial cells present adhesion-inducing cytokines to leukocytes
    • Tanaka Y., Adams D.H., and Shaw S. Proteoglycans on endothelial cells present adhesion-inducing cytokines to leukocytes. Immunol. Today 14 (1993) 111-115
    • (1993) Immunol. Today , vol.14 , pp. 111-115
    • Tanaka, Y.1    Adams, D.H.2    Shaw, S.3
  • 302
    • 0025873045 scopus 로고
    • Inhibition of leukocyte rolling in venules by protamine and sulfated polysaccharides
    • Tangelder G.J., and Arfors K.E. Inhibition of leukocyte rolling in venules by protamine and sulfated polysaccharides. Blood 77 (1991) 1565-1571
    • (1991) Blood , vol.77 , pp. 1565-1571
    • Tangelder, G.J.1    Arfors, K.E.2
  • 303
    • 0029942460 scopus 로고    scopus 로고
    • Chemokines and T lymphocyte activation: β Chemokines costimulate human T lymphocyte activation in vitro
    • Taub D.D., Turcovski-Corrales S.M., Key M.L., Longo D.L., and Murphy W.J. Chemokines and T lymphocyte activation: β Chemokines costimulate human T lymphocyte activation in vitro. J. Immunol. 156 (1996) 2095-2103
    • (1996) J. Immunol. , vol.156 , pp. 2095-2103
    • Taub, D.D.1    Turcovski-Corrales, S.M.2    Key, M.L.3    Longo, D.L.4    Murphy, W.J.5
  • 304
    • 0029095952 scopus 로고
    • The selectins: Vascular adhesion molecules
    • Tedder T.F., Steeber D.A., Chen A., and Engel P. The selectins: Vascular adhesion molecules. FASEB J. 9 (1995) 866-873
    • (1995) FASEB J. , vol.9 , pp. 866-873
    • Tedder, T.F.1    Steeber, D.A.2    Chen, A.3    Engel, P.4
  • 305
    • 0027493059 scopus 로고
    • Suppression by intradermal administration of heparin of eosinophil accumulation but not oedema formation in inflammatory reactions in guinea-pig skin
    • Teixeira M.M., and Hellewell P.G. Suppression by intradermal administration of heparin of eosinophil accumulation but not oedema formation in inflammatory reactions in guinea-pig skin. Br. J. Pharmacol. 110 (1993) 1496-1500
    • (1993) Br. J. Pharmacol. , vol.110 , pp. 1496-1500
    • Teixeira, M.M.1    Hellewell, P.G.2
  • 306
    • 0029996265 scopus 로고    scopus 로고
    • Adhesion mechanisms involved in C5a-induced eosinophil homotypic aggregation
    • Teixeira M.M., Rossi A.G., and Hellewell P.G. Adhesion mechanisms involved in C5a-induced eosinophil homotypic aggregation. J. Leukocyte Biol. 59 (1996) 389-396
    • (1996) J. Leukocyte Biol. , vol.59 , pp. 389-396
    • Teixeira, M.M.1    Rossi, A.G.2    Hellewell, P.G.3
  • 307
    • 0030586684 scopus 로고    scopus 로고
    • Eosinophil recruitment following allergen challenge is associated with the release of the chemokine RANTES into asthmatic airways
    • Teran L.M., Noso N., Carroll M., Davies D.E., Holgate S., and Schroder J.M. Eosinophil recruitment following allergen challenge is associated with the release of the chemokine RANTES into asthmatic airways. J. Immunol. 157 (1996) 1806-1812
    • (1996) J. Immunol. , vol.157 , pp. 1806-1812
    • Teran, L.M.1    Noso, N.2    Carroll, M.3    Davies, D.E.4    Holgate, S.5    Schroder, J.M.6
  • 308
    • 0027525087 scopus 로고
    • Aspirin versus heparin to prevent myocardial infarction during the acute phase of unstable angina
    • Theroux P., Waters D., Qiu S., McCans J., DeGuise P., and Juneau M. Aspirin versus heparin to prevent myocardial infarction during the acute phase of unstable angina. Circulation 88 (1993) 2045-2048
    • (1993) Circulation , vol.88 , pp. 2045-2048
    • Theroux, P.1    Waters, D.2    Qiu, S.3    McCans, J.4    DeGuise, P.5    Juneau, M.6
  • 309
    • 0017684443 scopus 로고
    • Tissue-specific distribution of sulfated mucopolysaccharides in mammals
    • Toledo O.M., and Dietrich C.P. Tissue-specific distribution of sulfated mucopolysaccharides in mammals. Biochim. Biophys. Acta 498 (1977) 114-122
    • (1977) Biochim. Biophys. Acta , vol.498 , pp. 114-122
    • Toledo, O.M.1    Dietrich, C.P.2
  • 311
    • 0028035107 scopus 로고
    • Induction of superoxide anion production from monocytes and neutrophils by activated platelets through the P-selectin-sialyl Lewis x interaction
    • Tsuji T., Nagata K., Koike J., Todoroki N., and Irimura T. Induction of superoxide anion production from monocytes and neutrophils by activated platelets through the P-selectin-sialyl Lewis x interaction. J. Leukocyte Biol. 56 (1994) 583-587
    • (1994) J. Leukocyte Biol. , vol.56 , pp. 583-587
    • Tsuji, T.1    Nagata, K.2    Koike, J.3    Todoroki, N.4    Irimura, T.5
  • 312
    • 0030294239 scopus 로고    scopus 로고
    • L-selectin binds to P-selectin glycoprotein ligand-1 on leukocytes: Interaction between the lectin, epidermal growth factor, and consensus repeat domains of the selectins determine ligand binding specificity
    • Tu L., Chen A., Delahunty M.D., Moore K.L., Watson S.R., McEver R.P., and Tedder T.F. L-selectin binds to P-selectin glycoprotein ligand-1 on leukocytes: Interaction between the lectin, epidermal growth factor, and consensus repeat domains of the selectins determine ligand binding specificity. J. Immunol. 157 (1996) 3995-4004
    • (1996) J. Immunol. , vol.157 , pp. 3995-4004
    • Tu, L.1    Chen, A.2    Delahunty, M.D.3    Moore, K.L.4    Watson, S.R.5    McEver, R.P.6    Tedder, T.F.7
  • 313
    • 0027480740 scopus 로고
    • Structure and biological activities of a heparin-derived hexasaccharide with high affinity for basic fibroblast growth factor
    • Tyrrell D.J., Ishihara M., Rao N., Horne A., Kiefer M.C., Stauber G.B., Lam L.H., and Stack R.J. Structure and biological activities of a heparin-derived hexasaccharide with high affinity for basic fibroblast growth factor. J. Biol. Chem. 268 (1993) 4684-4689
    • (1993) J. Biol. Chem. , vol.268 , pp. 4684-4689
    • Tyrrell, D.J.1    Ishihara, M.2    Rao, N.3    Horne, A.4    Kiefer, M.C.5    Stauber, G.B.6    Lam, L.H.7    Stack, R.J.8
  • 314
    • 0029059972 scopus 로고
    • Therapeutic uses of heparin beyond its traditional role as an anticoagulant
    • Tyrrell D.J., Kilfeather S., and Page C.P. Therapeutic uses of heparin beyond its traditional role as an anticoagulant. Trends Pharmacol. Sci. 16 (1995) 198-204
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 198-204
    • Tyrrell, D.J.1    Kilfeather, S.2    Page, C.P.3
  • 319
    • 0029086105 scopus 로고
    • A central role for microvillous receptor presentation in leukocyte adhesion under flow
    • von Andrian U., Hasslen S.R., Nelson R.D., Erlandsen S.L., and Butcher E.C. A central role for microvillous receptor presentation in leukocyte adhesion under flow. Cell 82 (1995) 989-999
    • (1995) Cell , vol.82 , pp. 989-999
    • von Andrian, U.1    Hasslen, S.R.2    Nelson, R.D.3    Erlandsen, S.L.4    Butcher, E.C.5
  • 320
    • 0028065619 scopus 로고
    • Potentiation of the oxidative burst of human neutrophils: A signaling role for L-selectin
    • Waddell T.K., Fialkow L., Chan C.K., Kishimoto T.K., and Downey G.P. Potentiation of the oxidative burst of human neutrophils: A signaling role for L-selectin. J. Biol. Chem. 269 (1994) 18485-18491
    • (1994) J. Biol. Chem. , vol.269 , pp. 18485-18491
    • Waddell, T.K.1    Fialkow, L.2    Chan, C.K.3    Kishimoto, T.K.4    Downey, G.P.5
  • 321
    • 0029075155 scopus 로고
    • Signaling functions of L-selectin: Enhancement of tyrosine phosphorylation and activation of MAP kinase
    • Waddell T.K., Fialkow L., Chan C.K., Kishimoto T.K., and Downey G.P. Signaling functions of L-selectin: Enhancement of tyrosine phosphorylation and activation of MAP kinase. J. Biol. Chem. 270 (1995) 15403-15411
    • (1995) J. Biol. Chem. , vol.270 , pp. 15403-15411
    • Waddell, T.K.1    Fialkow, L.2    Chan, C.K.3    Kishimoto, T.K.4    Downey, G.P.5
  • 322
    • 0029758146 scopus 로고    scopus 로고
    • Neutrophil-neutrophil interactions under hydrodynamic shear stress involve L-selectin and PSGL-1: A mechanism that amplifies initial leukocyte accumulation on P-selectin in vitro
    • Walcheck B., Moore K.L., McEver R.P., and Kishimoto T.K. Neutrophil-neutrophil interactions under hydrodynamic shear stress involve L-selectin and PSGL-1: A mechanism that amplifies initial leukocyte accumulation on P-selectin in vitro. J. Clin. Invest. 98 (1996) 1081-1087
    • (1996) J. Clin. Invest. , vol.98 , pp. 1081-1087
    • Walcheck, B.1    Moore, K.L.2    McEver, R.P.3    Kishimoto, T.K.4
  • 323
    • 0025823833 scopus 로고
    • Heparin and heparan sulphate are inhibitors of human leucocyte elastase
    • Walsh R.L., Dillon T.J., Scicchitano R., and McLennan G. Heparin and heparan sulphate are inhibitors of human leucocyte elastase. Clin. Sci. 81 (1991) 341-346
    • (1991) Clin. Sci. , vol.81 , pp. 341-346
    • Walsh, R.L.1    Dillon, T.J.2    Scicchitano, R.3    McLennan, G.4
  • 324
    • 0027517910 scopus 로고
    • Endothelial cell dysfunction occurs after hemorrhage in nonheparinized but not in preheparinized models
    • Wang P., Ba Z.F., and Chaudry I.H. Endothelial cell dysfunction occurs after hemorrhage in nonheparinized but not in preheparinized models. J. Surg. Res. 54 (1993) 499-506
    • (1993) J. Surg. Res. , vol.54 , pp. 499-506
    • Wang, P.1    Ba, Z.F.2    Chaudry, I.H.3
  • 325
    • 0025071509 scopus 로고
    • Preheparinization improves organ function after hemorrhage and resuscitation
    • Wang P., Singh G., Rana M.W., Ba Z.F., and Chaudry I.H. Preheparinization improves organ function after hemorrhage and resuscitation. Am. J. Physiol. 259 (1990) R645-R650
    • (1990) Am. J. Physiol. , vol.259
    • Wang, P.1    Singh, G.2    Rana, M.W.3    Ba, Z.F.4    Chaudry, I.H.5
  • 326
    • 0006539827 scopus 로고
    • A novel non-anticoagulant heparin (GM1892) restores cardiovascular and hepatocellular function following trauma-hemorrhage and decreases susceptibility to sepsis
    • Wang P., Zheng F., Reich S.S., Zhou M., Holme K.R., and Chaudry I.H. A novel non-anticoagulant heparin (GM1892) restores cardiovascular and hepatocellular function following trauma-hemorrhage and decreases susceptibility to sepsis. Surg. Forum Am. College Surgeons 45 (1994) 52-54
    • (1994) Surg. Forum Am. College Surgeons , vol.45 , pp. 52-54
    • Wang, P.1    Zheng, F.2    Reich, S.S.3    Zhou, M.4    Holme, K.R.5    Chaudry, I.H.6
  • 327
    • 0029880025 scopus 로고    scopus 로고
    • Effects of nonanticoagulant heparin on cardiovascular and hepatocellular function after hemorrhagic shock
    • Wang P., Zheng F., Reich S.S., Zhou M., Holme K.R., and Chaudry I.H. Effects of nonanticoagulant heparin on cardiovascular and hepatocellular function after hemorrhagic shock. Am. J. Physiol. 270 (1996) H1294-H1302
    • (1996) Am. J. Physiol. , vol.270
    • Wang, P.1    Zheng, F.2    Reich, S.S.3    Zhou, M.4    Holme, K.R.5    Chaudry, I.H.6
  • 330
    • 0029417189 scopus 로고
    • Multivalent binding of complement protein C1q to the amyloid beta-peptide (Aβ) promotes the nucleation phase of Aβ aggregation
    • Webster S., Glabe C., and Rogers J. Multivalent binding of complement protein C1q to the amyloid beta-peptide (Aβ) promotes the nucleation phase of Aβ aggregation. Biochem. Biophys. Res. Commun. 217 (1995) 869-875
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 869-875
    • Webster, S.1    Glabe, C.2    Rogers, J.3
  • 331
    • 0026529491 scopus 로고
    • Heparin and modified heparin inhibit complement activation in vivo
    • Weiler J.M., Edens R.E., Linhardt R.J., and Kapelanski D.P. Heparin and modified heparin inhibit complement activation in vivo. J. Immunol. 148 (1992) 3210-3215
    • (1992) J. Immunol. , vol.148 , pp. 3210-3215
    • Weiler, J.M.1    Edens, R.E.2    Linhardt, R.J.3    Kapelanski, D.P.4
  • 332
    • 0030017922 scopus 로고    scopus 로고
    • Gene expression of syndecans and betaglycan in isolated rat liver cells
    • Weiner O.H., Zoremba M., and Gressner A.M. Gene expression of syndecans and betaglycan in isolated rat liver cells. Cell Tissue Res. 285 (1996) 11-16
    • (1996) Cell Tissue Res. , vol.285 , pp. 11-16
    • Weiner, O.H.1    Zoremba, M.2    Gressner, A.M.3
  • 333
    • 0029763034 scopus 로고    scopus 로고
    • Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells
    • Wilkins P.P., McEver R.P., and Cummings R.D. Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells. J. Biol. Chem. 271 (1996) 18732-18742
    • (1996) J. Biol. Chem. , vol.271 , pp. 18732-18742
    • Wilkins, P.P.1    McEver, R.P.2    Cummings, R.D.3
  • 334
    • 0029132217 scopus 로고
    • Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin
    • Wilkins P.P., Moore K.L., McEver R.P., and Cummings R.D. Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin. J. Biol. Chem. 270 (1995) 22677-22680
    • (1995) J. Biol. Chem. , vol.270 , pp. 22677-22680
    • Wilkins, P.P.1    Moore, K.L.2    McEver, R.P.3    Cummings, R.D.4
  • 335
    • 0023889683 scopus 로고
    • Inhibition of allergic encephalomyelitis in rats by treatment with sulfated polysaccharides
    • Willenborg D.O., and Parish C.R. Inhibition of allergic encephalomyelitis in rats by treatment with sulfated polysaccharides. J. Immunol. 140 (1988) 3401-3405
    • (1988) J. Immunol. , vol.140 , pp. 3401-3405
    • Willenborg, D.O.1    Parish, C.R.2
  • 337
    • 4043167263 scopus 로고    scopus 로고
    • Use of a precise intratracheal delivery system to compare the acute tolerance of heparin and the heparinoid GM2000 in rabbits
    • Williams P.D., Tyrrell D.J., Storm N.E., Holme K.R., Salame R., and Banks C. Use of a precise intratracheal delivery system to compare the acute tolerance of heparin and the heparinoid GM2000 in rabbits. Toxicol. Methods 7 (1997) 1-7
    • (1997) Toxicol. Methods , vol.7 , pp. 1-7
    • Williams, P.D.1    Tyrrell, D.J.2    Storm, N.E.3    Holme, K.R.4    Salame, R.5    Banks, C.6
  • 338
    • 0028429960 scopus 로고
    • Differential binding of chemokines to glycosaminoglycan subpopulations
    • Witt D.P., and Lander A.D. Differential binding of chemokines to glycosaminoglycan subpopulations. Curr. Biol. 4 (1994) 394-400
    • (1994) Curr. Biol. , vol.4 , pp. 394-400
    • Witt, D.P.1    Lander, A.D.2
  • 340
    • 0023897313 scopus 로고
    • Heparin decreases ischemia-reperfusion injury in isolated canine gracilis model
    • Wright J.G., Kerr J.C., Valeri R., and Hobson II R.W. Heparin decreases ischemia-reperfusion injury in isolated canine gracilis model. Arch. Surg. 123 (1988) 470-472
    • (1988) Arch. Surg. , vol.123 , pp. 470-472
    • Wright, J.G.1    Kerr, J.C.2    Valeri, R.3    Hobson II, R.W.4
  • 341
    • 0028932509 scopus 로고
    • Isolation of the porcine heparin tetrasaccharides with glucuronate 2-O-sulfate-heparinase cleaves glucuro-nate 2-O-sulfate-containing disaccharides in highly sulfated blocks in heparin
    • Yamada S., Murakami T., Tsuda H., Yoshida K., and Sugahara K. Isolation of the porcine heparin tetrasaccharides with glucuronate 2-O-sulfate-heparinase cleaves glucuro-nate 2-O-sulfate-containing disaccharides in highly sulfated blocks in heparin. J. Biol. Chem. 270 (1995) 8696-8705
    • (1995) J. Biol. Chem. , vol.270 , pp. 8696-8705
    • Yamada, S.1    Murakami, T.2    Tsuda, H.3    Yoshida, K.4    Sugahara, K.5
  • 342
    • 0029857294 scopus 로고    scopus 로고
    • Reduction of brain injury using heparin to inhibit leukocyte accumulation in a rat model of transient focal cerebral ischemia. I. Protective mechanism
    • Yanaka K., Spellman S.R., McCarthy J.B., Oegema Jr. T.R., Low W.C., and Camarata P.J. Reduction of brain injury using heparin to inhibit leukocyte accumulation in a rat model of transient focal cerebral ischemia. I. Protective mechanism. J. Neurosurg. 85 (1996) 1102-1107
    • (1996) J. Neurosurg. , vol.85 , pp. 1102-1107
    • Yanaka, K.1    Spellman, S.R.2    McCarthy, J.B.3    Oegema Jr., T.R.4    Low, W.C.5    Camarata, P.J.6
  • 343
    • 0029908056 scopus 로고    scopus 로고
    • Reduction of brain injury using heparin to inhibit leukocyte accumulation in a rat model of transient focal cerebral ischemia. II. Dose-response effect and the therapeutic window
    • Yanaka K., Spellman S.R., McCarthy J.B., Low W.C., and Camarata P.J. Reduction of brain injury using heparin to inhibit leukocyte accumulation in a rat model of transient focal cerebral ischemia. II. Dose-response effect and the therapeutic window. J. Neurosurg. 85 (1996) 1108-1112
    • (1996) J. Neurosurg. , vol.85 , pp. 1108-1112
    • Yanaka, K.1    Spellman, S.R.2    McCarthy, J.B.3    Low, W.C.4    Camarata, P.J.5
  • 344
    • 0030910018 scopus 로고    scopus 로고
    • Glycosaminoglycans regulate elastase inhibition by oxidized secretory leukoprotease inhibitor
    • Ying Q.-L., Kemme M., Saunders D., and Simon S.R. Glycosaminoglycans regulate elastase inhibition by oxidized secretory leukoprotease inhibitor. Am. J. Physiol. 272 (1997) L533-L541
    • (1997) Am. J. Physiol. , vol.272
    • Ying, Q.-L.1    Kemme, M.2    Saunders, D.3    Simon, S.R.4
  • 345
    • 0024339121 scopus 로고
    • The ultrastructural localization of sulfated proteoglycans is identical in the amyloids of Alzheimer's disease and AA, AL, senile cardiac and medullary carcinoma-associated amyloidosis
    • Young I.D., Willmer J.P., and Kisilevsky R. The ultrastructural localization of sulfated proteoglycans is identical in the amyloids of Alzheimer's disease and AA, AL, senile cardiac and medullary carcinoma-associated amyloidosis. Acta Neuropathol. 78 (1989) 202-209
    • (1989) Acta Neuropathol. , vol.78 , pp. 202-209
    • Young, I.D.1    Willmer, J.P.2    Kisilevsky, R.3
  • 346
    • 0027976178 scopus 로고
    • Reduction of bacterial translocation and intestinal structural alterations by heparin in a murine burn injury model
    • Zapata-Sirvent R.L., Hansbrough J.F., Greenleaf G.E., Grayson L.S., and Wolf P. Reduction of bacterial translocation and intestinal structural alterations by heparin in a murine burn injury model. J. Trauma 36 (1994) 1-6
    • (1994) J. Trauma , vol.36 , pp. 1-6
    • Zapata-Sirvent, R.L.1    Hansbrough, J.F.2    Greenleaf, G.E.3    Grayson, L.S.4    Wolf, P.5
  • 347
    • 0020146126 scopus 로고
    • The use of anticoagulants in combined therapy of non-specific ulcerative colitis
    • Zavgorodnily L.G., and Mustyats A.P. The use of anticoagulants in combined therapy of non-specific ulcerative colitis. Klinicheskaia Meditsina (Moskva) 6 (1982) 74-80
    • (1982) Klinicheskaia Meditsina (Moskva) , vol.6 , pp. 74-80
    • Zavgorodnily, L.G.1    Mustyats, A.P.2
  • 348
    • 0029152283 scopus 로고
    • A novel nonanticoagulant heparin improves splenocyte and peritoneal macrophage immune function after trauma-hemorrhage and resucitation
    • Zellweger R., Ayala A., Zhu X.-L., Holme K.R., DeMaso C.M., and Chaudry I.H. A novel nonanticoagulant heparin improves splenocyte and peritoneal macrophage immune function after trauma-hemorrhage and resucitation. J. Surg. Res. 59 (1995) 211-218
    • (1995) J. Surg. Res. , vol.59 , pp. 211-218
    • Zellweger, R.1    Ayala, A.2    Zhu, X.-L.3    Holme, K.R.4    DeMaso, C.M.5    Chaudry, I.H.6
  • 349
    • 0028892362 scopus 로고
    • Repetitive Ser-Gly sequences enhance heparan sulfate assembly in proteoglycans
    • Zhang L.J., David G., and Esko J.D. Repetitive Ser-Gly sequences enhance heparan sulfate assembly in proteoglycans. J. Biol. Chem. 270 (1995) 27127-27135
    • (1995) J. Biol. Chem. , vol.270 , pp. 27127-27135
    • Zhang, L.J.1    David, G.2    Esko, J.D.3


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