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Volumn 31, Issue 5, 2012, Pages 308-316

Glycosaminoglycan backbone is not required for the modulation of hemostasis: Effect of different heparin derivatives and non-glycosaminoglycan analogs

Author keywords

Antithrombotic drugs; Endothelial cells; Extracellular matrix; Hemorrhagic activity; Smooth muscle cells

Indexed keywords

C3 (DRUG); ENOXAPARIN; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; HEPARIN; HEPARIN DERIVATIVE; PENTASACCHARIDE; PHOSPHOSULFOMANNAN; SYNTHETIC HEPARIN PENTASACCHARIDE; UNCLASSIFIED DRUG;

EID: 84861684346     PISSN: 0945053X     EISSN: 15691802     Source Type: Journal    
DOI: 10.1016/j.matbio.2012.03.001     Document Type: Article
Times cited : (8)

References (68)
  • 1
    • 0017044123 scopus 로고
    • Anticoagulant properties of heparin fractionated by affinity chromatography on matrix-bound antithrombin III and by gel filtration
    • Andersson L.O., Barrowcliffe T.W., Holmer E., Johnson E.A., Sims G.E. Anticoagulant properties of heparin fractionated by affinity chromatography on matrix-bound antithrombin III and by gel filtration. Thromb. Res. 1976, 9:575-583.
    • (1976) Thromb. Res. , vol.9 , pp. 575-583
    • Andersson, L.O.1    Barrowcliffe, T.W.2    Holmer, E.3    Johnson, E.A.4    Sims, G.E.5
  • 2
    • 0021943872 scopus 로고
    • The heparin induced thrombosis-thrombocytopenia syndrome (H.I.T.T.S.): a review
    • Arthur C.K., Isbister J.P., Aspery E.M. The heparin induced thrombosis-thrombocytopenia syndrome (H.I.T.T.S.): a review. Pathology 1985, 17:82-86.
    • (1985) Pathology , vol.17 , pp. 82-86
    • Arthur, C.K.1    Isbister, J.P.2    Aspery, E.M.3
  • 3
    • 76549234915 scopus 로고
    • Nine years' experience with heparin in acute venous thrombosis
    • Bauer G. Nine years' experience with heparin in acute venous thrombosis. Angiology 1950, 1:161-169.
    • (1950) Angiology , vol.1 , pp. 161-169
    • Bauer, G.1
  • 4
    • 0029918642 scopus 로고    scopus 로고
    • Clinical applications of new antithrombotic agents
    • Beijering R.J., ten Cate H., ten Cate J.W. Clinical applications of new antithrombotic agents. Ann. Hematol. 1996, 72:177-183.
    • (1996) Ann. Hematol. , vol.72 , pp. 177-183
    • Beijering, R.J.1    ten Cate, H.2    ten Cate, J.W.3
  • 6
    • 0011474913 scopus 로고
    • Heparin and the formation of white thrombi
    • Best C.H., Cowan C., Maclean D.L. Heparin and the formation of white thrombi. J. Physiol. 1938, 92:20-31.
    • (1938) J. Physiol. , vol.92 , pp. 20-31
    • Best, C.H.1    Cowan, C.2    Maclean, D.L.3
  • 7
    • 0019168039 scopus 로고
    • Fractionation and identification of heparin and other acidic mucopolysaccharides by a new discontinuous electrophoretic method
    • Bianchini P., Nader H., Takahashi H.K., Osima B., Straus A.H., Dietrich C.P. Fractionation and identification of heparin and other acidic mucopolysaccharides by a new discontinuous electrophoretic method. J. Chromatograph. A 1980, 196:455-462.
    • (1980) J. Chromatograph. A , vol.196 , pp. 455-462
    • Bianchini, P.1    Nader, H.2    Takahashi, H.K.3    Osima, B.4    Straus, A.H.5    Dietrich, C.P.6
  • 11
    • 0020074917 scopus 로고
    • Anti-clotting activity of endothelial cell cultures and heparan sulfate proteoglycans
    • Colburn P., Buonassisi V. Anti-clotting activity of endothelial cell cultures and heparan sulfate proteoglycans. Biochem. Biophys. Res. Commun. 1982, 104:220-227.
    • (1982) Biochem. Biophys. Res. Commun. , vol.104 , pp. 220-227
    • Colburn, P.1    Buonassisi, V.2
  • 12
    • 15244364003 scopus 로고    scopus 로고
    • Heparan sulfate-protein interactions: therapeutic potential through structure-function insights
    • Coombe D.R., Kett W.C. Heparan sulfate-protein interactions: therapeutic potential through structure-function insights. Cell. Mol. Life Sci. 2005, 62:410-424.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 410-424
    • Coombe, D.R.1    Kett, W.C.2
  • 13
    • 1642305211 scopus 로고
    • The significance of a smooth muscle component in hemostasis
    • Cruz W.O. The significance of a smooth muscle component in hemostasis. Proc. Soc. Exp. Biol. Med. 1965, 119:876-880.
    • (1965) Proc. Soc. Exp. Biol. Med. , vol.119 , pp. 876-880
    • Cruz, W.O.1
  • 15
    • 0017772139 scopus 로고
    • Identification of acidic mucopolysaccharides by agarose gel electrophoresis
    • Dietrich C.P., McDuffie N.M., Sampaio L.O. Identification of acidic mucopolysaccharides by agarose gel electrophoresis. J. Chromatogr. 1977, 130:299-304.
    • (1977) J. Chromatogr. , vol.130 , pp. 299-304
    • Dietrich, C.P.1    McDuffie, N.M.2    Sampaio, L.O.3
  • 17
    • 0002188917 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, New York, A. Varki, R. Cummings, J. Esko, H. Freeze, G. Hart, J. Marth (Eds.)
    • Esko J. Essentials of Glycobiology 1999, 441. Cold Spring Harbor Laboratory Press, New York. A. Varki, R. Cummings, J. Esko, H. Freeze, G. Hart, J. Marth (Eds.).
    • (1999) Essentials of Glycobiology , pp. 441
    • Esko, J.1
  • 20
    • 22244448718 scopus 로고    scopus 로고
    • Regulation of protein function by glycosaminoglycans - as exemplified by chemokines
    • Handel T.M., Johnson Z., Crown S.E., Lau E.K., Proudfoot A.E. Regulation of protein function by glycosaminoglycans - as exemplified by chemokines. Annu. Rev. Biochem. 2005, 74:385-410.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 385-410
    • Handel, T.M.1    Johnson, Z.2    Crown, S.E.3    Lau, E.K.4    Proudfoot, A.E.5
  • 21
    • 0032006909 scopus 로고    scopus 로고
    • Glycosaminoglycan-protein interactions: definition of consensus sites in glycosaminoglycan binding proteins
    • Hileman R.E., Fromm J.R., Weiler J.M., Linhardt R.J. Glycosaminoglycan-protein interactions: definition of consensus sites in glycosaminoglycan binding proteins. Bioessays 1998, 20:156-167.
    • (1998) Bioessays , vol.20 , pp. 156-167
    • Hileman, R.E.1    Fromm, J.R.2    Weiler, J.M.3    Linhardt, R.J.4
  • 22
    • 0021150941 scopus 로고
    • Heparin induced bleeding
    • Hirsh J. Heparin induced bleeding. Nouv. Rev. Fr. Hematol. 1984, 26:261-266.
    • (1984) Nouv. Rev. Fr. Hematol. , vol.26 , pp. 261-266
    • Hirsh, J.1
  • 23
    • 0024423930 scopus 로고
    • Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins
    • Huber R., Carrell R.W. Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins. Biochemistry 1989, 28:8951-8966.
    • (1989) Biochemistry , vol.28 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 24
    • 27144468308 scopus 로고    scopus 로고
    • Interaction of chemokines and glycosaminoglycans: a new twist in the regulation of chemokine function with opportunities for therapeutic intervention
    • Johnson Z., Proudfoot A.E., Handel T.M. Interaction of chemokines and glycosaminoglycans: a new twist in the regulation of chemokine function with opportunities for therapeutic intervention. Cytokine Growth Factor Rev. 2005, 16:625-636.
    • (2005) Cytokine Growth Factor Rev. , vol.16 , pp. 625-636
    • Johnson, Z.1    Proudfoot, A.E.2    Handel, T.M.3
  • 25
    • 76949134037 scopus 로고
    • Recent trends in anticoagulant therapy of thrombosis
    • Jorpes E. Recent trends in anticoagulant therapy of thrombosis. Acta Haematol. 1952, 7:257-270.
    • (1952) Acta Haematol. , vol.7 , pp. 257-270
    • Jorpes, E.1
  • 26
    • 0019076312 scopus 로고
    • Bleeding associated with antithrombotic therapy
    • Kelton J.G., Hirsh J. Bleeding associated with antithrombotic therapy. Semin. Hematol. 1980, 17:259-291.
    • (1980) Semin. Hematol. , vol.17 , pp. 259-291
    • Kelton, J.G.1    Hirsh, J.2
  • 27
    • 1642370756 scopus 로고    scopus 로고
    • Phosphomannopentaose sulfate (PI-88): heparan sulfate mimetic with clinical potential in multiple vascular pathologies
    • Khachigian L.M., Parish C.R. Phosphomannopentaose sulfate (PI-88): heparan sulfate mimetic with clinical potential in multiple vascular pathologies. Cardiovasc. Drug Rev. 2004, 22:1-6.
    • (2004) Cardiovasc. Drug Rev. , vol.22 , pp. 1-6
    • Khachigian, L.M.1    Parish, C.R.2
  • 29
    • 0024449163 scopus 로고
    • Antithrombin: structure, genomic organization, function and inherited deficiency
    • Lane D.A., Caso R. Antithrombin: structure, genomic organization, function and inherited deficiency. Baillieres Clin. Haematol. 1989, 2:961-998.
    • (1989) Baillieres Clin. Haematol. , vol.2 , pp. 961-998
    • Lane, D.A.1    Caso, R.2
  • 33
    • 33750498863 scopus 로고    scopus 로고
    • EJ-ras oncogene transfection of endothelial cells upregulates the expression of syndecan-4 and downregulates heparan sulfate sulfotransferases and epimerase
    • Lopes C.C., Toma L., Pinhal M.A., Porcionatto M.A., Sogayar M.C., Dietrich C.P., Nader H.B. EJ-ras oncogene transfection of endothelial cells upregulates the expression of syndecan-4 and downregulates heparan sulfate sulfotransferases and epimerase. Biochimie 2006, 88:1493-1504.
    • (2006) Biochimie , vol.88 , pp. 1493-1504
    • Lopes, C.C.1    Toma, L.2    Pinhal, M.A.3    Porcionatto, M.A.4    Sogayar, M.C.5    Dietrich, C.P.6    Nader, H.B.7
  • 35
    • 0038015257 scopus 로고    scopus 로고
    • Practical determination of hyaluronan by a new noncompetitive fluorescence-based assay on serum of normal and cirrhotic patients
    • Martins J.R., Passerotti C.C., Maciel R.M., Sampaio L.O., Dietrich C.P., Nader H.B. Practical determination of hyaluronan by a new noncompetitive fluorescence-based assay on serum of normal and cirrhotic patients. Anal. Biochem. 2003, 319:65-72.
    • (2003) Anal. Biochem. , vol.319 , pp. 65-72
    • Martins, J.R.1    Passerotti, C.C.2    Maciel, R.M.3    Sampaio, L.O.4    Dietrich, C.P.5    Nader, H.B.6
  • 36
    • 0034718216 scopus 로고    scopus 로고
    • Distribution of sulfated glycosaminoglycans in the animal kingdom: widespread occurrence of heparin-like compounds in invertebrates
    • Medeiros G.F., Mendes A., Castro R.A., Bau E.C., Nader H.B., Dietrich C.P. Distribution of sulfated glycosaminoglycans in the animal kingdom: widespread occurrence of heparin-like compounds in invertebrates. Biochim. Biophys. Acta 2000, 1475:287-294.
    • (2000) Biochim. Biophys. Acta , vol.1475 , pp. 287-294
    • Medeiros, G.F.1    Mendes, A.2    Castro, R.A.3    Bau, E.C.4    Nader, H.B.5    Dietrich, C.P.6
  • 37
    • 0035443891 scopus 로고    scopus 로고
    • Order out of complexity-protein structures that interact with heparin
    • Mulloy B., Linhardt R.J. Order out of complexity-protein structures that interact with heparin. Curr. Opin. Struct. Biol. 2001, 11:623-628.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 623-628
    • Mulloy, B.1    Linhardt, R.J.2
  • 38
    • 0003175467 scopus 로고
    • The use of heparin in thrombosis
    • Murray G.D., Best C.H. The use of heparin in thrombosis. Ann. Surg. 1938, 108:163-177.
    • (1938) Ann. Surg. , vol.108 , pp. 163-177
    • Murray, G.D.1    Best, C.H.2
  • 39
    • 0024319532 scopus 로고
    • Heparin stimulates the synthesis and modifies the sulfation pattern of heparan sulfate proteoglycan from endothelial cells
    • Nader H.B., Buonassisi V., Colburn P., Dietrich C.P. Heparin stimulates the synthesis and modifies the sulfation pattern of heparan sulfate proteoglycan from endothelial cells. J. Cell. Physiol. 1989, 140:305-310.
    • (1989) J. Cell. Physiol. , vol.140 , pp. 305-310
    • Nader, H.B.1    Buonassisi, V.2    Colburn, P.3    Dietrich, C.P.4
  • 41
    • 0032863091 scopus 로고    scopus 로고
    • New insights on the specificity of heparin and heparan sulfate lyases from Flavobacterium heparinum revealed by the use of synthetic derivatives of K5 polysaccharide from E. coli and 2-O-desulfated heparin
    • Nader H.B., Kobayashi E.Y., Chavante S.F., Tersariol I.L., Castro R.A., Shinjo S.K., Naggi A., Torri G., Casu B., Dietrich C.P. New insights on the specificity of heparin and heparan sulfate lyases from Flavobacterium heparinum revealed by the use of synthetic derivatives of K5 polysaccharide from E. coli and 2-O-desulfated heparin. Glycoconj. J. 1999, 16:265-270.
    • (1999) Glycoconj. J. , vol.16 , pp. 265-270
    • Nader, H.B.1    Kobayashi, E.Y.2    Chavante, S.F.3    Tersariol, I.L.4    Castro, R.A.5    Shinjo, S.K.6    Naggi, A.7    Torri, G.8    Casu, B.9    Dietrich, C.P.10
  • 42
    • 1642373288 scopus 로고    scopus 로고
    • Heparins and heparinoids: occurrence, structure and mechanism of antithrombotic and hemorrhagic activities
    • Nader H.B., Lopes C.C., Rocha H.A., Santos E.A., Dietrich C.P. Heparins and heparinoids: occurrence, structure and mechanism of antithrombotic and hemorrhagic activities. Curr. Pharm. Des. 2004, 10:951-966.
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 951-966
    • Nader, H.B.1    Lopes, C.C.2    Rocha, H.A.3    Santos, E.A.4    Dietrich, C.P.5
  • 44
    • 0024423886 scopus 로고
    • Structural requirements of heparin disaccharides responsible for hemorrhage: reversion of the antihemostatic effect by ATP
    • Nader H.B., Tersariol I.L., Dietrich C.P. Structural requirements of heparin disaccharides responsible for hemorrhage: reversion of the antihemostatic effect by ATP. FASEB J. 1989, 3:2420-2424.
    • (1989) FASEB J. , vol.3 , pp. 2420-2424
    • Nader, H.B.1    Tersariol, I.L.2    Dietrich, C.P.3
  • 45
    • 0025784018 scopus 로고
    • Effect of heparin and dextran sulfate on the synthesis and structure of heparan sulfate from cultured endothelial cells
    • Nader H.B., Toma L., Pinhal M.A., Buonassisi V., Colburn P., Dietrich C.P. Effect of heparin and dextran sulfate on the synthesis and structure of heparan sulfate from cultured endothelial cells. Semin. Thromb. Hemost. 1991, 17(Suppl 1):47-56.
    • (1991) Semin. Thromb. Hemost. , vol.17 , Issue.SUPPL. 1 , pp. 47-56
    • Nader, H.B.1    Toma, L.2    Pinhal, M.A.3    Buonassisi, V.4    Colburn, P.5    Dietrich, C.P.6
  • 46
    • 33644830185 scopus 로고    scopus 로고
    • Low-molecular-weight heparins and angiogenesis
    • Norrby K. Low-molecular-weight heparins and angiogenesis. APMIS 2006, 114:79-102.
    • (2006) APMIS , vol.114 , pp. 79-102
    • Norrby, K.1
  • 48
    • 0026690347 scopus 로고
    • Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement
    • Olson S.T., Bjork I., Sheffer R., Craig P.A., Shore J.D., Choay J. Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement. J. Biol. Chem. 1992, 267:12528-12538.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12528-12538
    • Olson, S.T.1    Bjork, I.2    Sheffer, R.3    Craig, P.A.4    Shore, J.D.5    Choay, J.6
  • 49
    • 0033565247 scopus 로고    scopus 로고
    • Identification of sulfated oligosaccharide-based inhibitors of tumor growth and metastasis using novel in vitro assays for angiogenesis and heparanase activity
    • Parish C.R., Freeman C., Brown K.J., Francis D.J., Cowden W.B. Identification of sulfated oligosaccharide-based inhibitors of tumor growth and metastasis using novel in vitro assays for angiogenesis and heparanase activity. Cancer Res. 1999, 59:3433-3441.
    • (1999) Cancer Res. , vol.59 , pp. 3433-3441
    • Parish, C.R.1    Freeman, C.2    Brown, K.J.3    Francis, D.J.4    Cowden, W.B.5
  • 50
    • 0025743779 scopus 로고
    • A new synthetic pentasaccharide with increased anti-factor Xa activity: possible role for anionic clusters in the interaction of heparin and antithrombin III
    • Petitou M., Lormeau J.C., Choay J. A new synthetic pentasaccharide with increased anti-factor Xa activity: possible role for anionic clusters in the interaction of heparin and antithrombin III. Semin. Thromb. Hemost. 1991, 17(Suppl. 2):143-146.
    • (1991) Semin. Thromb. Hemost. , vol.17 , Issue.SUPPL. 2 , pp. 143-146
    • Petitou, M.1    Lormeau, J.C.2    Choay, J.3
  • 52
    • 0028879620 scopus 로고
    • Minimum fragments of the heparin molecule able to produce the accumulation and change of the sulfation pattern of an antithrombotic heparan sulfate from endothelial cells
    • Pinhal M.A., Santos I.A., Silva I.F., Dietrich C.P., Nader H.B. Minimum fragments of the heparin molecule able to produce the accumulation and change of the sulfation pattern of an antithrombotic heparan sulfate from endothelial cells. Thromb. Haemost. 1995, 74:1169-1174.
    • (1995) Thromb. Haemost. , vol.74 , pp. 1169-1174
    • Pinhal, M.A.1    Santos, I.A.2    Silva, I.F.3    Dietrich, C.P.4    Nader, H.B.5
  • 53
    • 2442549670 scopus 로고    scopus 로고
    • Interactions of heparin/heparan sulfate with proteins: appraisal of structural factors and experimental approaches
    • Powell A.K., Yates E.A., Fernig D.G., Turnbull J.E. Interactions of heparin/heparan sulfate with proteins: appraisal of structural factors and experimental approaches. Glycobiology 2004, 14:17R-30R.
    • (2004) Glycobiology , vol.14
    • Powell, A.K.1    Yates, E.A.2    Fernig, D.G.3    Turnbull, J.E.4
  • 54
    • 0018962983 scopus 로고
    • Failure of aspirin at different doses to modify experimental thrombosis in rats
    • Reyers I., Mussoni L., Donati M.B., de Gaetano G. Failure of aspirin at different doses to modify experimental thrombosis in rats. Thromb. Res. 1980, 18:669-674.
    • (1980) Thromb. Res. , vol.18 , pp. 669-674
    • Reyers, I.1    Mussoni, L.2    Donati, M.B.3    de Gaetano, G.4
  • 57
    • 77952374032 scopus 로고    scopus 로고
    • Conformational degeneracy restricts the effective information content of heparan sulfate
    • Rudd T.R., Yates E.A. Conformational degeneracy restricts the effective information content of heparan sulfate. Mol. Biosyst. 2010, 6:902-908.
    • (2010) Mol. Biosyst. , vol.6 , pp. 902-908
    • Rudd, T.R.1    Yates, E.A.2
  • 60
    • 0027502741 scopus 로고
    • Mutagenesis of thrombin selectively modulates inhibition by serpins heparin cofactor II and antithrombin III. Interaction with the anion-binding exosite determines heparin cofactor II specificity
    • Sheehan J.P., Wu Q., Tollefsen D.M., Sadler J.E. Mutagenesis of thrombin selectively modulates inhibition by serpins heparin cofactor II and antithrombin III. Interaction with the anion-binding exosite determines heparin cofactor II specificity. J. Biol. Chem. 1993, 268:3639-3645.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3639-3645
    • Sheehan, J.P.1    Wu, Q.2    Tollefsen, D.M.3    Sadler, J.E.4
  • 62
    • 30744451472 scopus 로고    scopus 로고
    • Glycosaminoglycans and their proteoglycans: host-associated molecular patterns for initiation and modulation of inflammation
    • Taylor K.R., Gallo R.L. Glycosaminoglycans and their proteoglycans: host-associated molecular patterns for initiation and modulation of inflammation. FASEB J. 2006, 20:9-22.
    • (2006) FASEB J. , vol.20 , pp. 9-22
    • Taylor, K.R.1    Gallo, R.L.2
  • 63
    • 0026462656 scopus 로고
    • Interaction of heparin with myosin ATPase: possible involvement with the hemorrhagic activity and a correlation with antithrombin III high affinity-heparin molecules
    • Tersariol I.L., Dietrich C.P., Nader H.B. Interaction of heparin with myosin ATPase: possible involvement with the hemorrhagic activity and a correlation with antithrombin III high affinity-heparin molecules. Thromb. Res. 1992, 68:247-258.
    • (1992) Thromb. Res. , vol.68 , pp. 247-258
    • Tersariol, I.L.1    Dietrich, C.P.2    Nader, H.B.3
  • 65
    • 0035283092 scopus 로고    scopus 로고
    • A synthetic pentasaccharide for the prevention of deep-vein thrombosis after total hip replacement
    • Turpie A.G., Gallus A.S., Hoek J.A., Pentasaccharide I. A synthetic pentasaccharide for the prevention of deep-vein thrombosis after total hip replacement. N. Engl. J. Med. 2001, 344:619-625.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 619-625
    • Turpie, A.G.1    Gallus, A.S.2    Hoek, J.A.3    Pentasaccharide, I.4
  • 68
    • 0034671656 scopus 로고    scopus 로고
    • Heparinase I acts on a synthetic heparin pentasaccharide corresponding to the antithrombin III binding site
    • Yu G., LeBrun L., Gunay N.S., Hoppensteadt D., Walenga J.M., Fareed J., Linhardt R.J. Heparinase I acts on a synthetic heparin pentasaccharide corresponding to the antithrombin III binding site. Thromb. Res. 2000, 100:549-556.
    • (2000) Thromb. Res. , vol.100 , pp. 549-556
    • Yu, G.1    LeBrun, L.2    Gunay, N.S.3    Hoppensteadt, D.4    Walenga, J.M.5    Fareed, J.6    Linhardt, R.J.7


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