메뉴 건너뛰기




Volumn 11, Issue , 2011, Pages 959-971

The involvement of glycosaminoglycans in airway disease associated with cystic fibrosis

Author keywords

Airway inflammatory disease; Cystic fibrosis; Glycosaminoglycans; Neutrophil antimicrobial peptides and proteases

Indexed keywords

BETA DEFENSIN 2; CHONDROITIN SULFATE; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; HYALURONIC ACID; PROTEINASE;

EID: 79958171038     PISSN: None     EISSN: 1537744X     Source Type: Journal    
DOI: 10.1100/tsw.2011.81     Document Type: Short Survey
Times cited : (22)

References (129)
  • 2
    • 0029346937 scopus 로고
    • The relationship between infection and inflammation in the early stages of lung disease from cystic fibrosis
    • Balough, K., McCubbin, M., Weinberger, M., Smits, W., Ahrens, R., and Fick, R. (1995) The relationship between infection and inflammation in the early stages of lung disease from cystic fibrosis. Pediatr. Pulmonol. 20, 63-70.
    • (1995) Pediatr. Pulmonol. , vol.20 , pp. 63-70
    • Balough, K.1    McCubbin, M.2    Weinberger, M.3    Smits, W.4    Ahrens, R.5    Fick, R.6
  • 7
    • 77956354814 scopus 로고    scopus 로고
    • Hyposecretion of fluid from tracheal submucosal glands of CFTR-deficient pigs
    • Joo, N.S., Cho, H.J., Khansaheb, M., and Wine, J.J. (2010) Hyposecretion of fluid from tracheal submucosal glands of CFTR-deficient pigs. J. Clin. Invest. 120, 3161-3166.
    • (2010) J. Clin. Invest. , vol.120 , pp. 3161-3166
    • Joo, N.S.1    Cho, H.J.2    Khansaheb, M.3    Wine, J.J.4
  • 8
    • 77956379893 scopus 로고    scopus 로고
    • Disease phenotype of a ferret CFTR-knockout model of cystic fibrosis
    • Sun, X. et al. (2010) Disease phenotype of a ferret CFTR-knockout model of cystic fibrosis. J. Clin. Invest. 120, 3149-3160.
    • (2010) J. Clin. Invest. , vol.120 , pp. 3149-3160
    • Sun, X.1
  • 9
    • 77952974496 scopus 로고    scopus 로고
    • Cystic fibrosis pigs develop lung disease and exhibit defective bacterial eradication at birth
    • Stoltz, D.A. et al. (2010) Cystic fibrosis pigs develop lung disease and exhibit defective bacterial eradication at birth. Sci. Transl. Med. 2, 29-31.
    • (2010) Sci. Transl. Med. , vol.2 , pp. 29-31
    • Stoltz, D.A.1
  • 11
    • 0036529082 scopus 로고    scopus 로고
    • Endotoxin activity and inflammatory markers in the airways of young patients with cystic fibrosis
    • Muhlebach, M.S. and Noah, T.L. (2002) Endotoxin activity and inflammatory markers in the airways of young patients with cystic fibrosis. Am. J. Respir. Crit. Care Med. 165, 911-915. (Pubitemid 34774656)
    • (2002) American Journal of Respiratory and Critical Care Medicine , vol.165 , Issue.7 , pp. 911-915
    • Muhlebach, M.S.1    Noah, T.L.2
  • 12
    • 34247556420 scopus 로고    scopus 로고
    • Synthesis and medical applications of oligosaccharides
    • DOI 10.1038/nature05819, PII NATURE05819
    • Seeberger, P.H. and Werz, D.B. (2007) Synthesis and medical applications of oligosaccharides. Nature 446, 1046-1051. (Pubitemid 46676067)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1046-1051
    • Seeberger, P.H.1    Werz, D.B.2
  • 13
    • 34447627584 scopus 로고    scopus 로고
    • Matrix proteoglycans in development of pulmonary edema
    • Garg, H.G., Roughley, P.J., and Hales, C.A., Eds. Marcel Dekker. New York
    • Negrini, D., De Luca, G., Passi, A., and Miserocchi, G. (2002) Matrix proteoglycans in development of pulmonary edema. In Proteoglycans in Lung Disease. Garg, H.G., Roughley, P.J., and Hales, C.A., Eds. Marcel Dekker. New York. pp. 143-168.
    • (2002) Proteoglycans in Lung Disease , pp. 143-168
    • Negrini, D.1    De Luca, G.2    Passi, A.3    Miserocchi, G.4
  • 14
    • 17644421823 scopus 로고    scopus 로고
    • Invited review: Biomechanics of the lung parenchyma: Critical roles of collagen and mechanical forces
    • DOI 10.1152/japplphysiol.01087.2004
    • Suki, B., Ito, S., Stamenovic, D., Lutchen, K.R., and Ingenito, E.P. (2005) Biomechanics of the lung parenchyma: critical roles of collagen and mechanical forces. J. Appl. Physiol. 98, 1892-1899. (Pubitemid 40570805)
    • (2005) Journal of Applied Physiology , vol.98 , Issue.5 , pp. 1892-1899
    • Suki, B.1    Ito, S.2    Stamenovic, D.3    Lutchen, K.R.4    Ingenito, E.P.5
  • 16
    • 0032079824 scopus 로고    scopus 로고
    • The heparan sulfate binding sequence of interferon-gamma increased the on rate of the interferon-gamma-interferon-gamma receptor complex formation
    • DOI 10.1074/jbc.273.18.10919
    • Sadir, R., Forest, E., and Lortat-Jacob, H. (1998) The heparan sulfate binding sequence of interferon-gamma increased the on rate of the interferon-gamma-interferon-gamma receptor complex formation. J. Biol. Chem. 273, 10919-10925. (Pubitemid 28204930)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.18 , pp. 10919-10925
    • Sadir, R.1    Forest, E.2    Lortat-Jacob, H.3
  • 17
    • 0025976609 scopus 로고
    • Interferon-gamma binds to heparan sulfate by a cluster of amino acids located in the C-terminal part of the molecule
    • Lortat-Jacob, H. and Grimaud, J.A. (1991) Interferon-gamma binds to heparan sulfate by a cluster of amino acids located in the C-terminal part of the molecule. FEBS Lett. 280, 152-154.
    • (1991) FEBS Lett. , vol.280 , pp. 152-154
    • Lortat-Jacob, H.1    Grimaud, J.A.2
  • 18
    • 0030055212 scopus 로고    scopus 로고
    • Heparin decreases the blood clearance of interferon-gamma and increases its activity by limiting the processing of its carboxyl-terminal sequence
    • DOI 10.1074/jbc.271.27.16139
    • Lortat-Jacob, H., Baltzer, F., and Grimaud, J.A. (1996) Heparin decreases the blood clearance of interferon-gamma and increases its activity by limiting the processing of its carboxyl-terminal sequence. J. Biol. Chem. 271, 16139-16143. (Pubitemid 26236230)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.27 , pp. 16139-16143
    • Lortat-Jacob, H.1    Baltzer, F.2    Grimaud, J.-A.3
  • 20
    • 0033752698 scopus 로고    scopus 로고
    • Hyaluronic acid in cultured ovine tracheal cells and its effect on ciliary beat frequency in vitro
    • Lieb, T., Forteza, R., and Salathe, M. (2000) Hyaluronic acid in cultured ovine tracheal cells and its effect on ciliary beat frequency in vitro. J. Aerosol Med. 13, 231-237.
    • (2000) J. Aerosol Med. , vol.13 , pp. 231-237
    • Lieb, T.1    Forteza, R.2    Salathe, M.3
  • 21
    • 0028897008 scopus 로고
    • Glycosaminoglycan distribution in atherosclerotic saphenous vein grafts
    • Marquezini, M.V., Strunz, C.M., Dallan, L.A., and Toledo, O.M. (1995) Glycosaminoglycan distribution in atherosclerotic saphenous vein grafts. Cardiology 86, 143-146.
    • (1995) Cardiology , vol.86 , pp. 143-146
    • Marquezini, M.V.1    Strunz, C.M.2    Dallan, L.A.3    Toledo, O.M.4
  • 22
    • 0031962056 scopus 로고    scopus 로고
    • Dysregulation of proteoglycan production by intrahepatic biliary epithelial cells bearing defective (delta-F508) cystic fibrosis transmembrane conductance regulator
    • DOI 10.1002/hep.510270103
    • Bhaskar, K.R., Turner, B.S., Grubman, S.A., Jefferson, D.M., and LaMont, J.T. (1998) Dysregulation of proteoglycan production by intrahepatic biliary epithelial cells bearing defective (delta-f508) cystic fibrosis transmembrane conductance regulator. Hepatology 27, 7-14. (Pubitemid 28041527)
    • (1998) Hepatology , vol.27 , Issue.1 , pp. 7-14
    • Bhaskar, K.R.1    Turner, B.S.2    Grubman, S.A.3    Jefferson, D.M.4    LaMont, J.T.5
  • 25
    • 0037385068 scopus 로고    scopus 로고
    • Effect of chondroitinase ABC on purulent sputum from cystic fibrosis and other patients
    • DOI 10.1203/01.PDR.0000054780.11755.B9
    • Khatri, I.A., Bhaskar, K.R., Lamont, J.T., Sajjan, S.U., Ho, C.K., and Forstner, J. (2003) Effect of chondroitinase ABC on purulent sputum from cystic fibrosis and other patients. Pediatr. Res. 53, 619-627. (Pubitemid 36406732)
    • (2003) Pediatric Research , vol.53 , Issue.4 , pp. 619-627
    • Khatri, I.A.1    Bhaskar, K.R.2    Lamont, J.T.3    Sajjan, S.U.4    Ho, C.K.Y.5    Forstner, J.6
  • 27
    • 0019307796 scopus 로고
    • Hyaluronic acid. An indicator of pathological conditions of human lungs?
    • Sahu, S.C. (1980) Hyaluronic acid. An indicator of pathological conditions of human lungs? Inflammation 4, 107-112.
    • (1980) Inflammation , vol.4 , pp. 107-112
    • Sahu, S.C.1
  • 28
    • 0036204265 scopus 로고    scopus 로고
    • Serum hyaluronic acid concentrations are increased in cystic fibrosis patients with liver disease
    • DOI 10.1136/adc.86.3.190
    • Wyatt, H.A., Dhawan, A., Cheeseman, P., Mieli-Vergani, G., and Price, J.F. (2002) Serum hyaluronic acid concentrations are increased in cystic fibrosis patients with liver disease. Arch. Dis. Child. 86, 190-193. (Pubitemid 34250864)
    • (2002) Archives of Disease in Childhood , vol.86 , Issue.3 , pp. 190-193
    • Wyatt, H.A.1    Dhawan, A.2    Cheeseman, P.3    Mieli-Vergani, G.4    Price, J.F.5
  • 29
    • 33644969778 scopus 로고    scopus 로고
    • Aerosolised hyaluronic acid prevents exercise-induced bronchoconstriction, suggesting novel hypotheses on the correction of matrix defects in asthma
    • Petrigni, G. and Allegra, L. (2006) Aerosolised hyaluronic acid prevents exercise-induced bronchoconstriction, suggesting novel hypotheses on the correction of matrix defects in asthma. Pulm. Pharmacol. Ther. 19, 166-171.
    • (2006) Pulm. Pharmacol. Ther. , vol.19 , pp. 166-171
    • Petrigni, G.1    Allegra, L.2
  • 30
    • 0024819154 scopus 로고
    • Lung accumulation of hyaluronan parallels pulmonary edema in experimental alveolitis
    • Nettelbladt, O., Tengblad, A., and Hallgren, R. (1989) Lung accumulation of hyaluronan parallels pulmonary edema in experimental alveolitis. Am. J. Physiol. 257, L379-384.
    • (1989) Am. J. Physiol. , vol.257
    • Nettelbladt, O.1    Tengblad, A.2    Hallgren, R.3
  • 33
    • 0026640846 scopus 로고
    • Type VI collagen microfibrils: Evidence for a structural association with hyaluronan
    • Kielty, C.M., Whittaker, S.P., Grant, M.E., and Shuttleworth, C.A. (1992) Type VI collagen microfibrils: evidence for a structural association with hyaluronan. J. Cell Biol. 118, 979-990.
    • (1992) J. Cell Biol. , vol.118 , pp. 979-990
    • Kielty, C.M.1    Whittaker, S.P.2    Grant, M.E.3    Shuttleworth, C.A.4
  • 34
    • 0025038449 scopus 로고
    • Hyaluronan and its binding proteins, the hyaladherins
    • Toole, B.P. (1990) Hyaluronan and its binding proteins, the hyaladherins. Curr. Opin. Cell Biol. 2, 839-44.
    • (1990) Curr. Opin. Cell Biol. , vol.2 , pp. 839-844
    • Toole, B.P.1
  • 36
    • 0028930748 scopus 로고
    • Migration of bovine aortic smooth muscle cells after wounding injury. The role of hyaluronan and RHAMM
    • Savani, R.C. et al. (1995) Migration of bovine aortic smooth muscle cells after wounding injury. The role of hyaluronan and RHAMM. J. Clin. Invest. 95, 1158-1168.
    • (1995) J. Clin. Invest. , vol.95 , pp. 1158-1168
    • Savani, R.C.1
  • 38
    • 34547127890 scopus 로고    scopus 로고
    • Recognition of hyaluronan released in sterile injury involves a unique receptor complex dependent on toll-like receptor 4, CD44, and MD-2
    • DOI 10.1074/jbc.M606352200
    • Taylor, K.R., Yamasaki, K., Radek, K.A., Di Nardo, A., Goodarzi, H., Golenbock, D., Beutler, B., and Gallo, R.L. (2007) Recognition of hyaluronan released in sterile injury involves a unique receptor complex dependent on Toll-like receptor 4, CD44, and MD-2. J. Biol. Chem. 282, 18265-18275. (Pubitemid 47100227)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.25 , pp. 18265-18275
    • Taylor, K.R.1    Yamasaki, K.2    Radek, K.A.3    Di, N.A.4    Goodarzi, H.5    Golenbock, D.6    Beutler, B.7    Gallo, R.L.8
  • 40
    • 0033179160 scopus 로고    scopus 로고
    • Hyaluronate-enhanced hematopoiesis: Two different receptors trigger the release of interleukin-1beta and interleukin-6 from bone marrow macrophages
    • Khaldoyanidi, S., Moll, J., Karakhanova, S., Herrlich, P., and Ponta, H. (1999) Hyaluronate-enhanced hematopoiesis: two different receptors trigger the release of interleukin-1beta and interleukin-6 from bone marrow macrophages. Blood 94, 940-949. (Pubitemid 29361825)
    • (1999) Blood , vol.94 , Issue.3 , pp. 940-949
    • Khaldoyanidi, S.1    Moll, J.2    Karakhanova, S.3    Herrlich, P.4    Ponta, H.5
  • 41
    • 0033609860 scopus 로고    scopus 로고
    • Three isoforms of mammalian hyaluronan synthases have distinct enzymatic properties
    • Itano, N. et al. (1999) Three isoforms of mammalian hyaluronan synthases have distinct enzymatic properties. J. Biol. Chem. 274, 25085-25092.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25085-25092
    • Itano, N.1
  • 42
    • 0037113921 scopus 로고    scopus 로고
    • NF-kappaB activation mediates the cross-talk between extracellular matrix and interferon-gamma (IFN-gamma) leading to enhanced monokine induced by IFN-gamma (MIG) expression in macrophages
    • DOI 10.1074/jbc.M206007200
    • Horton, M.R., Boodoo, S., and Powell, J.D. (2002) NF-kappa B activation mediates the cross-talk between extracellular matrix and interferon-gamma (IFN-gamma) leading to enhanced monokine induced by IFN-gamma (MIG) expression in macrophages. J. Biol. Chem. 277, 43757-43762. (Pubitemid 36157794)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.46 , pp. 43757-43762
    • Horton, M.R.1    Boodoo, S.2    Powell, J.D.3
  • 43
    • 0031953083 scopus 로고    scopus 로고
    • Aerosolized hyaluronic acid decreases alveolar injury induced by human neutrophil elastase
    • Cantor, J.O., Cerreta, J.M., Armand, G., and Turino, G.M. (1998) Aerosolized hyaluronic acid decreases alveolar injury induced by human neutrophil elastase. Proc. Soc. Exp. Biol. Med. 217, 471-475.
    • (1998) Proc. Soc. Exp. Biol. Med. , vol.217 , pp. 471-475
    • Cantor, J.O.1    Cerreta, J.M.2    Armand, G.3    Turino, G.M.4
  • 44
    • 0032899955 scopus 로고    scopus 로고
    • Functions of hyaluronan in wound repair
    • DOI 10.1046/j.1524-475X.1999.00079.x
    • Chen, W.Y. and Abatangelo, G. (1999) Functions of hyaluronan in wound repair. Wound Repair Regen. 7, 79-89. (Pubitemid 29200045)
    • (1999) Wound Repair and Regeneration , vol.7 , Issue.2 , pp. 79-89
    • Chen, W.Y.J.1    Abatangelo, G.2
  • 45
    • 0027449412 scopus 로고
    • Intra-articular treatment with hyaluronic acid in osteoarthritis of the knee joint: A controlled clinical trial versus mucopolysaccharide polysulfuric acid ester
    • Graf, J., Neusel, E., Schneider, E., and Niethard, F.U. (1993) Intra-articular treatment with hyaluronic acid in osteoarthritis of the knee joint: a controlled clinical trial versus mucopolysaccharide polysulfuric acid ester. Clin. Exp. Rheumatol. 11, 367-372. (Pubitemid 23287156)
    • (1993) Clinical and Experimental Rheumatology , vol.11 , Issue.4 , pp. 367-372
    • Graf, J.1    Neusel, E.2    Schneider, E.3    Niethard, F.U.4
  • 46
    • 77954485569 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator can export hyaluronan
    • Schulz, T., Schumacher, U., Prante, C., Sextro, W., and Prehm, P. (2010) Cystic fibrosis transmembrane conductance regulator can export hyaluronan. Pathobiology 77, 200-209.
    • (2010) Pathobiology , vol.77 , pp. 200-209
    • Schulz, T.1    Schumacher, U.2    Prante, C.3    Sextro, W.4    Prehm, P.5
  • 47
    • 33646857682 scopus 로고    scopus 로고
    • Anion channel involved in induction of apoptosis and necrosis
    • Okada, Y., Maeno, E., and Mori, S. (2004) Anion channel involved in induction of apoptosis and necrosis. Adv. Exp. Med. Biol. 559, 205-209.
    • (2004) Adv. Exp. Med. Biol. , vol.559 , pp. 205-209
    • Okada, Y.1    Maeno, E.2    Mori, S.3
  • 48
    • 22244448718 scopus 로고    scopus 로고
    • Regulation of protein function by glycosaminoglycans - As exemplified by chemokines
    • DOI 10.1146/annurev.biochem.72.121801.161747
    • Handel, T.M., Johnson, Z., Crown, S.E., Lau, E.K., and Proudfoot, A.E. (2005) Regulation of protein function by glycosaminoglycans - as exemplified by chemokines. Annu. Rev. Biochem. 74, 385-410. (Pubitemid 40995512)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 385-410
    • Handel, T.M.1    Johnson, Z.2    Crown, S.E.3    Lau, E.K.4    Sweeney, M.5    Proudfoot, A.E.6
  • 49
    • 0024371484 scopus 로고
    • Binding of heparan sulfate to type V collagen. A mechanism of cell-substrate adhesion
    • LeBaron, R.G., Höök, A., Esko, J.D., Gay, S., and Höök, M. (1989) Binding of heparan sulfate to type V collagen. A mechanism of cell-substrate adhesion. J. Biol. Chem. 264, 7950-7956. (Pubitemid 19137273)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.14 , pp. 7950-7956
    • LeBaron, R.G.1    Hook, A.2    Esko, J.D.3    Gay, S.4    Hook, M.5
  • 50
    • 23044444804 scopus 로고    scopus 로고
    • Heparan sulfate: A complex polymer charged with biological activity
    • DOI 10.1021/cr010213m
    • Whitelock, J.M. and Iozzo, R.V. (2005) Heparan sulfate: a complex polymer charged with biological activity. Chem. Rev. 105, 2745-2764. (Pubitemid 41055329)
    • (2005) Chemical Reviews , vol.105 , Issue.7 , pp. 2745-2764
    • Whitelock, J.M.1    Iozzo, R.V.2
  • 51
    • 0031906297 scopus 로고    scopus 로고
    • Interleukin-5 binds to heparin/heparan sulfate. A model for an interaction with extracellular matrix
    • Lipscombe, R.J., Nakhoul, A.M., Sanderson, C.J., and Coombe, D.R. (1998) Interleukin-5 binds to heparin/heparan sulfate. A model for an interaction with extracellular matrix. J. Leukoc. Biol. 63, 342-350. (Pubitemid 28106848)
    • (1998) Journal of Leukocyte Biology , vol.63 , Issue.3 , pp. 342-350
    • Lipscombe, R.J.1    Nakhoul, A.-M.2    Sanderson, C.J.3    Coombe, D.R.4
  • 52
    • 0036963489 scopus 로고    scopus 로고
    • Increased in Vitro cytotoxicity of TNF-alpha analog LK-805 is based on the interaction with cell surface heparan sulfate proteoglycan
    • Menart, V., Fonda, I., Kenig, M., and Porekar, V.G. (2002) Increased in vitro cytotoxicity of TNF-alpha analog LK-805 is based on the interaction with cell surface heparan sulfate proteoglycan. Ann. N. Y. Acad. Sci. 973, 194-206. (Pubitemid 36125003)
    • (2002) Annals of the New York Academy of Sciences , vol.973 , pp. 194-206
    • Menart, V.1    Fonda, I.2    Kenig, M.3    Porekar, V.G.4
  • 53
    • 0034669968 scopus 로고    scopus 로고
    • Characterization of the heparin-binding properties of IL-6
    • Mummery, R.S. and Rider, C.C. (2000) Characterization of the heparin-binding properties of IL-6. J. Immunol. 165, 5671-5679.
    • (2000) J. Immunol. , vol.165 , pp. 5671-5679
    • Mummery, R.S.1    Rider, C.C.2
  • 54
    • 0037022198 scopus 로고    scopus 로고
    • Different affinities of glycosaminoglycan oligosaccharides for monomeric and dimeric interleukin-8: A model for chemokine regulation at inflammatory sites
    • DOI 10.1021/bi011944j
    • Goger, B., Halden, Y., Rek, A., Mosl, R., Pye, D., Gallagher, J., and Kungl, A.J. (2002) Different affinities of glycosaminoglycan oligosaccharides for monomeric and dimeric interleukin-8: a model for chemokine regulation at inflammatory sites. Biochemistry 41, 1640-1646. (Pubitemid 34112754)
    • (2002) Biochemistry , vol.41 , Issue.5 , pp. 1640-1646
    • Goger, B.1    Halden, Y.2    Rek, A.3    Mosl, R.4    Pye, D.5    Gallagher, J.6    Kungl, A.J.7
  • 55
    • 0042134798 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 supports IL-8-mediated neutrophil transendothelial migration by inhibition of the constitutive shedding of endothelial IL-8/heparan sulfate/syndecan-1 complexes
    • Marshall, L.J., Ramdin, L.S., Brooks, T., DPhil, P.C., and Shute, J.K. (2003) Plasminogen activator inhibitor-1 supports IL-8-mediated neutrophil transendothelial migration by inhibition of the constitutive shedding of endothelial IL-8/heparan sulfate/syndecan-1 complexes. J. Immunol. 171, 2057-2065. (Pubitemid 36966489)
    • (2003) Journal of Immunology , vol.171 , Issue.4 , pp. 2057-2065
    • Marshall, L.J.1    Ramdin, L.S.P.2    Brooks, T.3    DPhil, P.C.4    Shute, J.K.5
  • 56
    • 0033613247 scopus 로고    scopus 로고
    • Glycosaminoglycans interact selectively with chemokines and modulate receptor binding and cellular responses
    • Kuschert, G.S., Coulin, F., Power, C.A., Proudfoot, A.E., Hubbard, R.E., Hoogewerf, A.J., and Wells, T.N. (1999) Glycosaminoglycans interact selectively with chemokines and modulate receptor binding and cellular responses. Biochemistry 38, 12959-12968.
    • (1999) Biochemistry , vol.38 , pp. 12959-12968
    • Kuschert, G.S.1    Coulin, F.2    Power, C.A.3    Proudfoot, A.E.4    Hubbard, R.E.5    Hoogewerf, A.J.6    Wells, T.N.7
  • 57
    • 1542376200 scopus 로고    scopus 로고
    • A Structural and Dynamic Model for the Interaction of Interleukin-8 and Glycosaminoglycans: Support from Isothermal Fluorescence Titrations
    • DOI 10.1002/prot.10590
    • Krieger, E., Geretti, E., Brandner, B., Goger, B., Wells, T.N., and Kungl, A.J. (2004) A structural and dynamic model for the interaction of interleukin-8 and glycosaminoglycans: support from isothermal fluorescence titrations. Proteins 54, 768-775. (Pubitemid 38298795)
    • (2004) Proteins: Structure, Function and Genetics , vol.54 , Issue.4 , pp. 768-775
    • Krieger, E.1    Geretti, E.2    Brandner, B.3    Goger, B.4    Wells, T.N.5    Kungl, A.J.6
  • 58
    • 0025835670 scopus 로고
    • Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation
    • Rapraeger, A.C., Krufka, A., and Olwin, B.B. (1991) Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation. Science 252, 1705-1708. (Pubitemid 21917092)
    • (1991) Science , vol.252 , Issue.5013 , pp. 1705-1708
    • Rapraeger, A.C.1    Krufka, A.2    Olwin, B.B.3
  • 59
    • 77949329602 scopus 로고    scopus 로고
    • IL-8 dictates glycosaminoglycan binding and stability of IL-18 in cystic fibrosis
    • Reeves, E.P. et al. (2010) IL-8 dictates glycosaminoglycan binding and stability of IL-18 in cystic fibrosis. J. Immunol. 184, 1642-1652.
    • (2010) J. Immunol. , vol.184 , pp. 1642-1652
    • Reeves, E.P.1
  • 61
    • 39649120097 scopus 로고    scopus 로고
    • Targeting neutrophil elastase in cystic fibrosis
    • DOI 10.1517/14728222.12.2.145
    • Kelly, E., Greene, C.M., and McElvaney, N.G. (2008) Targeting neutrophil elastase in cystic fibrosis. Expert Opin. Ther. Targets 12, 145-157. (Pubitemid 351284958)
    • (2008) Expert Opinion on Therapeutic Targets , vol.12 , Issue.2 , pp. 145-157
    • Kelly, E.1    Greene, C.M.2    McElvaney, N.G.3
  • 62
    • 0035153078 scopus 로고    scopus 로고
    • Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cells
    • Plotkowski, M.C., Costa, A.O., Morandi, V., Barbosa, H.S., Nader, H.B., de Bentzmann, S., and Puchelle, E. (2001) Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cells. J. Med. Microbiol. 50, 183-190. (Pubitemid 32113169)
    • (2001) Journal of Medical Microbiology , vol.50 , Issue.2 , pp. 183-190
    • Plotkowski, M.C.1    Costa, A.O.2    Morandi, V.3    Barbosa, H.S.4    Nader, H.B.5    De Bentzmann, S.6    Puchelle, E.7
  • 63
    • 0037113896 scopus 로고    scopus 로고
    • Specific molecular interactions of oversulfated chondroitin sulfate E with various heparin-binding growth factors: Implications as a physiological binding partner in the brain and other tissues
    • DOI 10.1074/jbc.M207105200
    • Deepa, S.S., Umehara, Y., Higashiyama, S., Itoh, N., and Sugahara, K. (2002) Specific molecular interactions of oversulfated chondroitin sulfate E with various heparin-binding growth factors. Implications as a physiological binding partner in the brain and other tissues. J. Biol. Chem. 277, 43707-43716. (Pubitemid 36157787)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.46 , pp. 43707-43716
    • Deepa, S.S.1    Umehara, Y.2    Higashiyama, S.3    Itoh, N.4    Sugahara, K.5
  • 64
    • 0037066693 scopus 로고    scopus 로고
    • Oversulfated chondroitin/dermatan sulfates containing GlcAbeta1/IdoAalpha1-3GalNAc(4,6-O-disulfate) interact with L- and P-selectin and chemokines
    • DOI 10.1074/jbc.M200396200
    • Kawashima, H., Atarashi, K., Hirose, M., Hirose, J., Yamada, S., Sugahara, K., and Miyasaka, M. (2002) Oversulfated chondroitin/dermatan sulfates containing GlcAbeta1/IdoAalpha1-3GalNAc(4,6-O-disulfate) interact with L- and P-selectin and chemokines. J. Biol. Chem. 277, 12921-12930. (Pubitemid 34952659)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 12921-12930
    • Kawashima, H.1    Atarashi, K.2    Hirose, M.3    Hirose, J.4    Yamada, S.5    Sugahara, K.6    Miyasaka, M.7
  • 65
    • 28444463260 scopus 로고    scopus 로고
    • Regulation of the chondroitin/dermatan fine structure by transforming growth factor-beta1 through effects on polymer-modifying enzymes
    • DOI 10.1093/glycob/cwj027
    • Tiedemann, K., Olander, B., Eklund, E., Todorova, L., Bengtsson, M., Maccarana, M., Westergren-Thorsson, G., and Malmstrom, A. (2005) Regulation of the chondroitin/dermatan fine structure by transforming growth factor-beta1 through effects on polymer-modifying enzymes. Glycobiology 15, 1277-1285. (Pubitemid 41724332)
    • (2005) Glycobiology , vol.15 , Issue.12 , pp. 1277-1285
    • Tiedemann, K.1    Olander, B.2    Eklund, E.3    Todorova, L.4    Bengtsson, M.5    Maccarana, M.6    Westergren-Thorsson, G.7    Malmstrom, A.8
  • 66
    • 0020683593 scopus 로고
    • Mucus glycoproteins secreted by respiratory epithelial tissue from cystic fibrosis patients
    • Frates, R.C., Jr., Kaizu, T.T., and Last, J.A. (1983) Mucus glycoproteins secreted by respiratory epithelial tissue from cystic fibrosis patients. Pediatr. Res. 17, 30-34. (Pubitemid 13223450)
    • (1983) Pediatric Research , vol.17 , Issue.1 , pp. 30-34
    • Frates Jr., R.C.1    Kaizu, T.T.2    Last, J.A.3
  • 67
    • 0024345843 scopus 로고
    • Increased sulfation of glycoconjugates by cultured nasal epithelial cells from patients with cystic fibrosis
    • Cheng, P.W., Boat, T.F., Cranfill, K., Yankaskas, J.R., and Boucher, R.C. (1989) Increased sulfation of glycoconjugates by cultured nasal epithelial cells from patients with cystic fibrosis. J. Clin. Invest. 84, 68-72. (Pubitemid 19170096)
    • (1989) Journal of Clinical Investigation , vol.84 , Issue.1 , pp. 68-72
    • Cheng, P.-W.1    Boat, T.F.2    Cranfill, K.3    Yankaskas, J.R.4    Boucher, R.C.5
  • 68
    • 0029016145 scopus 로고
    • Alteration of sulfation of glycoconjugates, but not sulfate transport and intracellular inorganic sulfate content in cystic fibrosis airway epithelial cells
    • Mohapatra, N.K., Cheng, P.W., Parker, J.C., Paradiso, A.M., Yankaskas, J.R., Boucher, R.C., and Boat, T.F. (1995) Alteration of sulfation of glycoconjugates, but not sulfate transport and intracellular inorganic sulfate content in cystic fibrosis airway epithelial cells. Pediatr. Res. 38, 42-48.
    • (1995) Pediatr. Res. , vol.38 , pp. 42-48
    • Mohapatra, N.K.1    Cheng, P.W.2    Parker, J.C.3    Paradiso, A.M.4    Yankaskas, J.R.5    Boucher, R.C.6    Boat, T.F.7
  • 69
    • 0031259163 scopus 로고    scopus 로고
    • Organ-specific over-sulfation of glycosaminoglycans and altered extracellular matrix in a mouse model of cystic fibrosis
    • DOI 10.1006/bmme.1997.2630
    • Hill, W.G., Harper, G.S., Rozaklis, T., Boucher, R.C., and Hopwood, J.J. (1997) Organ-specific over-sulfation of glycosaminoglycans and altered extracellular matrix in a mouse model of cystic fibrosis. Biochem. Mol. Med. 62, 113-122. (Pubitemid 27495289)
    • (1997) Biochemical and Molecular Medicine , vol.62 , Issue.1 , pp. 113-122
    • Hill, W.G.1    Harper, G.S.2    Rozaklis, T.3    Boucher, R.C.4    Hopwood, J.J.5
  • 70
    • 0017105130 scopus 로고
    • Human respiratory tract secretion. Mucous glycoproteins of nonpurulent tracheobronchial secretions, and sputum of patients with bronchitis and cystic fibrosis
    • Boat, T.F., Cheng, P.W., Iyer, R.N., Carlson, D.M., and Polony, I. (1976) Human respiratory tract secretion. Mucous glycoproteins of nonpurulent tracheobronchial secretions, and sputum of patients with bronchitis and cystic fibrosis. Arch. Biochem. Biophys. 177, 95-104.
    • (1976) Arch. Biochem. Biophys. , vol.177 , pp. 95-104
    • Boat, T.F.1    Cheng, P.W.2    Iyer, R.N.3    Carlson, D.M.4    Polony, I.5
  • 71
    • 0016681625 scopus 로고
    • Arylsulfatase B deficiency in Maroteaux-Lamy syndrome: Cellular studies and carrier identification
    • Beratis, N.G., Turner, B.M., Weiss, R., and Hirschhorn, K. (1975) Arylsulfatase B deficiency in Maroteaux-Lamy syndrome: cellular studies and carrier identification. Pediatr. Res. 9, 475-480.
    • (1975) Pediatr. Res. , vol.9 , pp. 475-480
    • Beratis, N.G.1    Turner, B.M.2    Weiss, R.3    Hirschhorn, K.4
  • 72
    • 0038724018 scopus 로고    scopus 로고
    • Does deficiency of arylsulfatase B have a role in cystic fibrosis?
    • Tobacman, J.K. (2003) Does deficiency of arylsulfatase B have a role in cystic fibrosis? Chest 123, 2130-2139.
    • (2003) Chest , vol.123 , pp. 2130-2139
    • Tobacman, J.K.1
  • 73
    • 73949137686 scopus 로고    scopus 로고
    • Cell-bound IL-8 increases in bronchial epithelial cells after arylsulfatase B silencing due to sequestration with chondroitin-4-sulfate
    • Bhattacharyya, S., Solakyildirim, K., Zhang, Z., Chen, M.L., Linhardt, R.J., and Tobacman, J.K. (2009) Cell-bound IL-8 increases in bronchial epithelial cells after arylsulfatase B silencing due to sequestration with chondroitin-4-sulfate. Am. J. Respir. Cell Mol. Biol. 42, 51-61.
    • (2009) Am. J. Respir. Cell Mol. Biol. , vol.42 , pp. 51-61
    • Bhattacharyya, S.1    Solakyildirim, K.2    Zhang, Z.3    Chen, M.L.4    Linhardt, R.J.5    Tobacman, J.K.6
  • 74
    • 33947705107 scopus 로고    scopus 로고
    • Increased arylsulfatase B activity in cystic fibrosis cells following correction of CFTR
    • DOI 10.1016/j.cca.2007.01.021, PII S0009898107000368
    • Bhattacharyya, S., Look, D., and Tobacman, J.K. (2007) Increased arylsulfatase B activity in cystic fibrosis cells following correction of CFTR. Clin. Chim. Acta 380, 122-127. (Pubitemid 46498042)
    • (2007) Clinica Chimica Acta , vol.380 , Issue.1-2 , pp. 122-127
    • Bhattacharyya, S.1    Look, D.2    Tobacman, J.K.3
  • 75
    • 0034029645 scopus 로고    scopus 로고
    • Binding of selenoprotein P to heparin: Characterization with surface plasmon resonance
    • Arteel, G.E., Franken, S., Kappler, J., and Sies, H. (2000) Binding of selenoprotein P to heparin: characterization with surface plasmon resonance. Biol. Chem. 381, 265-268. (Pubitemid 30179561)
    • (2000) Biological Chemistry , vol.381 , Issue.3 , pp. 265-268
    • Arteel, G.E.1    Franken, S.2    Kappler, J.3    Sies, H.4
  • 76
    • 42449087252 scopus 로고    scopus 로고
    • Platelet endothelial cell adhesion molecule 1 (PECAM-1) and its interactions with glycosaminoglycans: 1. Molecular modeling studies
    • DOI 10.1021/bi702455e
    • Gandhi, N.S., Coombe, D.R., and Mancera, R.L. (2008) Platelet endothelial cell adhesion molecule 1 (PECAM-1) and its interactions with glycosaminoglycans: 1. Molecular modeling studies. Biochemistry 47, 4851-4862. (Pubitemid 351574992)
    • (2008) Biochemistry , vol.47 , Issue.17 , pp. 4851-4862
    • Gandhi, N.S.1    Coombe, D.R.2    Mancera, R.L.3
  • 77
    • 69749128729 scopus 로고    scopus 로고
    • Exhaled breath condensate pH and ammonia in cystic fibrosis and response to treatment of acute pulmonary exacerbations
    • Newport, S., Amin, N., and Dozor, A.J. (2009) Exhaled breath condensate pH and ammonia in cystic fibrosis and response to treatment of acute pulmonary exacerbations. Pediatr. Pulmonol. 44, 866-872.
    • (2009) Pediatr. Pulmonol. , vol.44 , pp. 866-872
    • Newport, S.1    Amin, N.2    Dozor, A.J.3
  • 78
    • 0036847496 scopus 로고    scopus 로고
    • Airways in cystic fibrosis are acidified: Detection by exhaled breath condensate
    • DOI 10.1136/thorax.57.11.926
    • Tate, S., MacGregor, G., Davis, M., Innes, J.A., and Greening, A.P. (2002) Airways in cystic fibrosis are acidified: detection by exhaled breath condensate. Thorax 57, 926-929. (Pubitemid 35316268)
    • (2002) Thorax , vol.57 , Issue.11 , pp. 926-929
    • Tate, S.1    MacGregor, G.2    Davis, M.3    Innes, J.A.4    Greening, A.P.5
  • 80
    • 0026681802 scopus 로고
    • Neutrophil elastase in respiratory epithelial lining fluid of individuals with cystic fibrosis induces interleukin-8 gene expression in a human bronchial epithelial cell line
    • Nakamura, H., Yoshimura, K., McElvaney, N.G., and Crystal, R.G. (1992) Neutrophil elastase in respiratory epithelial lining fluid of individuals with cystic fibrosis induces interleukin-8 gene expression in a human bronchial epithelial cell line. J. Clin. Invest. 89, 1478-1484.
    • (1992) J. Clin. Invest. , vol.89 , pp. 1478-1484
    • Nakamura, H.1    Yoshimura, K.2    McElvaney, N.G.3    Crystal, R.G.4
  • 81
    • 0022500794 scopus 로고
    • Immunolocalization of elastase in human emphysematous lungs
    • Damiano, V.V., Tsang, A., Kucich, U., Abrams, W.R., Rosenbloom, J., Kimbel, P., Fallahnejad, M., and Weinbaum, G. (1986) Immunolocalization of elastase in human emphysematous lungs. J. Clin. Invest. 78, 482-493. (Pubitemid 16074086)
    • (1986) Journal of Clinical Investigation , vol.78 , Issue.2 , pp. 482-493
    • Damiano, V.V.1    Tsang, A.2    Kucich, U.3
  • 82
    • 0021941090 scopus 로고
    • Elastase in tissue injury
    • Janoff, A. (1985) Elastase in tissue injury. Annu. Rev. Med. 36, 207-216.
    • (1985) Annu. Rev. Med. , vol.36 , pp. 207-216
    • Janoff, A.1
  • 83
    • 0027732683 scopus 로고
    • 2-chloride system
    • Klebanoff, S.J., Kinsella, M.G., and Wight, T.N. (1993) Degradation of endothelial cell matrix heparan sulfate proteoglycan by elastase and the myeloperoxidase-H2O2-chloride system. Am. J. Pathol. 143, 907-917. (Pubitemid 24058246)
    • (1993) American Journal of Pathology , vol.143 , Issue.3 , pp. 907-917
    • Klebanoff, S.J.1    Kinsella, M.G.2    Wight, T.N.3
  • 84
    • 36348929470 scopus 로고    scopus 로고
    • Secretory leucocyte protease inhibitor inhibits interferon-gamma-induced cathepsin S expression
    • DOI 10.1074/jbc.M706884200
    • Geraghty, P., Greene, C.M., O'Mahony, M., O'Neill, S.J., Taggart, C.C., and McElvaney, N.G. (2007) Secretory leucocyte protease inhibitor inhibits interferon-gamma-induced cathepsin S expression. J. Biol. Chem. 282, 33389-33395. (Pubitemid 350159551)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.46 , pp. 33389-33395
    • Geraghty, P.1    Greene, C.M.2    O'Mahony, M.3    O'Neill, S.J.4    Taggart, C.C.5    McElvaney, N.G.6
  • 85
    • 0027495712 scopus 로고
    • Pharmacokinetics of recombinant secretory leukoprotease inhibitor aerosolized to normals and individuals with cystic fibrosis
    • McElvaney, N.G., Doujaiji, B., Moan, M.J., Burnham, M.R., Wu, M.C., and Crystal, R.G. (1993) Pharmacokinetics of recombinant secretory leukoprotease inhibitor aerosolized to normals and individuals with cystic fibrosis. Am. Rev. Respir. Dis. 148, 1056-1060. (Pubitemid 23301230)
    • (1993) American Review of Respiratory Disease , vol.148 , Issue.4 , pp. 1056-1060
    • McElvaney, N.G.1    Doujaiji, B.2    Moan, M.J.3    Burnham, M.R.4    Wu, M.C.5    Crystal, R.G.6
  • 86
    • 31544470902 scopus 로고    scopus 로고
    • 1-antitrypsin therapy in cystic fibrosis
    • DOI 10.1002/ppul.20345
    • Martin, S.L., Downey, D., Bilton, D., Keogan, M.T., Edgar, J., and Elborn, J.S. (2006) Safety and efficacy of recombinant alpha(1)-antitrypsin therapy in cystic fibrosis. Pediatr. Pulmonol. 41, 177-183. (Pubitemid 43165448)
    • (2006) Pediatric Pulmonology , vol.41 , Issue.2 , pp. 177-183
    • Martin, S.L.1    Downey, D.2    Bilton, D.3    Keogan, M.T.4    Edgar, J.5    Elborn, J.S.6
  • 88
    • 0027493879 scopus 로고
    • Inhibition of the human leukocyte endopeptidases elastase and cathepsin G and of porcine pancreatic elastase by N-oleoyl derivatives of heparin
    • DOI 10.1016/0006-2952(93)90321-M
    • Baici, A., Diczhazi, C., Neszmelyi, A., Moczar, E., and Hornebeck, W. (1993) Inhibition of the human leukocyte endopeptidases elastase and cathepsin G and of porcine pancreatic elastase by N-oleoyl derivatives of heparin. Biochem. Pharmacol. 46, 1545-1549. (Pubitemid 23338486)
    • (1993) Biochemical Pharmacology , vol.46 , Issue.9 , pp. 1545-1549
    • Baici, A.1    Diczhazi, C.2    Neszmelyi, A.3    Moczar, E.4    Hornebeck, W.5
  • 90
    • 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. (1990) Sulfated polysaccharides prevent human leukocyte elastase-induced acute lung injury and emphysema in hamsters. Am. Rev. Respir. Dis. 142, 407-412. (Pubitemid 20235954)
    • (1990) American Review of Respiratory Disease , vol.142 , Issue.2 , pp. 407-412
    • Rao, N.V.1    Kennedy, T.P.2    Rao, G.3    Ky, N.4    Hoidal, J.R.5
  • 91
    • 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. (1991) Prevention of leucocyte elastase-induced emphysema in mice by heparin fragments. Eur. Respir. J. 4, 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
  • 92
    • 0029149155 scopus 로고
    • Influence of heparin thromboprophylaxis on plasma leucocyte elastase levels following lobectomy for lung carcinoma
    • Tian, Y., Gebitekin, C., Martin, P., Satur, C.M., Mearns, A., and Walker, D.R. (1995) Influence of heparin thromboprophylaxis on plasma leucocyte elastase levels following lobectomy for lung carcinoma. Blood Coagul. Fibrinolysis 6, 527-530.
    • (1995) Blood Coagul. Fibrinolysis , vol.6 , pp. 527-530
    • Tian, Y.1    Gebitekin, C.2    Martin, P.3    Satur, C.M.4    Mearns, A.5    Walker, D.R.6
  • 93
    • 0033609813 scopus 로고    scopus 로고
    • Elastase-mediated release of heparan sulfate proteoglycans from pulmonary fibroblast cultures. A mechanism for basic fibroblast growth factor (bFGF) release and attenuation of bfgf binding following elastase-induced injury
    • Buczek-Thomas, J.A. and Nugent, M.A. (1999) Elastase-mediated release of heparan sulfate proteoglycans from pulmonary fibroblast cultures. A mechanism for basic fibroblast growth factor (bFGF) release and attenuation of bfgf binding following elastase-induced injury. J. Biol. Chem. 274, 25167-25172.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25167-25172
    • Buczek-Thomas, J.A.1    Nugent, M.A.2
  • 94
    • 0028897054 scopus 로고
    • Digestion of proteoglycans in porcine pancreatic elastase-induced emphysema in rats
    • van de Lest, C.H., Versteeg, E.M., Veerkamp, J.H., and van Kuppevelt, T.H. (1995) Digestion of proteoglycans in porcine pancreatic elastase-induced emphysema in rats. Eur. Respir. J. 8, 238-245.
    • (1995) Eur. Respir. J. , vol.8 , pp. 238-245
    • Van De Lest, C.H.1    Versteeg, E.M.2    Veerkamp, J.H.3    Van Kuppevelt, T.H.4
  • 95
    • 33746637530 scopus 로고    scopus 로고
    • New insights into the inhibition of human neutrophil elastase by heparin
    • DOI 10.1021/bi060338r
    • Spencer, J.L., Stone, P.J., and Nugent, M.A. (2006) New insights into the inhibition of human neutrophil elastase by heparin. Biochemistry 45, 9104-9120. (Pubitemid 44156373)
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9104-9120
    • Spencer, J.L.1    Stone, P.J.2    Nugent, M.A.3
  • 96
    • 0025823833 scopus 로고
    • Heparin and heparan sulphate are inhibitors of human leucocyte elastase
    • Walsh, R.L., Dillon, T.J., Scicchitano, R., and McLennan, G. (1991) Heparin and heparan sulphate are inhibitors of human leucocyte elastase. Clin. Sci. (Lond.) 81, 341-346.
    • (1991) Clin. Sci. (Lond.) , vol.81 , pp. 341-346
    • Walsh, R.L.1    Dillon, T.J.2    Scicchitano, R.3    McLennan, G.4
  • 97
    • 0030582198 scopus 로고    scopus 로고
    • Inhibition of human leukocyte elastase activity by heparins: Influence of charge density
    • Volpi, N. (1996) Inhibition of human leukocyte elastase activity by heparins: influence of charge density. Biochim. Biophys. Acta 1290, 299-307.
    • (1996) Biochim. Biophys. Acta , vol.1290 , pp. 299-307
    • Volpi, N.1
  • 98
    • 0038702237 scopus 로고    scopus 로고
    • Inhibition of PMN-elastase activity by semisynthetic glucan sulfates
    • Becker, M., Franz, G., and Alban, S. (2003) Inhibition of PMN-elastase activity by semisynthetic glucan sulfates. Thromb. Haemost. 89, 915-925. (Pubitemid 36608876)
    • (2003) Thrombosis and Haemostasis , vol.89 , Issue.5 , pp. 915-925
    • Becker, M.1    Franz, G.2    Alban, S.3
  • 99
    • 29144505345 scopus 로고    scopus 로고
    • Interactions of low-molecular-weight semi-synthetic sulfated heparins with human leukocyte elastase and human Cathepsin G
    • DOI 10.1016/j.bcp.2005.10.027, PII S0006295205006994
    • Sissi, C., Lucatello, L., Naggi, A., Torri, G., and Palumbo, M. (2006) Interactions of low-molecular-weight semi-synthetic sulfated heparins with human leukocyte elastase and human cathepsin G. Biochem. Pharmacol. 71, 287-93. (Pubitemid 41817289)
    • (2006) Biochemical Pharmacology , vol.71 , Issue.3 , pp. 287-293
    • Sissi, C.1    Lucatello, L.2    Naggi, A.3    Torri, G.4    Palumbo, M.5
  • 100
    • 0037468524 scopus 로고    scopus 로고
    • Heparin-like dextran derivatives as well as glycosaminoglycans inhibit the enzymatic activity of human cathepsin G
    • DOI 10.1016/S0014-5793(03)00064-4
    • Ledoux, D., Merciris, D., Barritault, D., and Caruelle, J.P. (2003) Heparin-like dextran derivatives as well as glycosaminoglycans inhibit the enzymatic activity of human cathepsin G. FEBS Lett. 537, 23-29. (Pubitemid 36246670)
    • (2003) FEBS Letters , vol.537 , Issue.1-3 , pp. 23-29
    • Ledoux, D.1    Merciris, D.2    Barritault, D.3    Caruelle, J.-P.4
  • 101
    • 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. (1997) Glycosaminoglycans regulate elastase inhibition by oxidized secretory leukoprotease inhibitor. Am. J. Physiol. 272, L533-541.
    • (1997) Am. J. Physiol. , vol.272
    • Ying, Q.L.1    Kemme, M.2    Saunders, D.3    Simon, S.R.4
  • 104
    • 37249064399 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan-involving immunomodulation by cathelicidin antimicrobial peptides LL-37 and PR-39
    • DOI 10.1100/tsw.2007.285
    • Kaneider, N.C., Djanani, A., and Wiedermann, C.J. (2007) Heparan sulfate proteoglycan-involving immunomodulation by cathelicidin antimicrobial peptides LL-37 and PR-39. TheScientificWorldJOURNAL 7, 1832-1838. (Pubitemid 350277600)
    • (2007) TheScientificWorldJournal , vol.7 , pp. 1832-1838
    • Kaneider, N.C.1    Djanani, A.2    Wiedermann, C.J.3
  • 105
    • 27144462218 scopus 로고    scopus 로고
    • Sputum cathelicidin, urokinase plasminogen activation system components, and cytokines discriminate cystic fibrosis, COPD, and asthma inflammation
    • DOI 10.1378/chest.128.4.2316
    • Xiao, W., Hsu, Y.P., Ishizaka, A., Kirikae, T., and Moss, R.B. (2005) Sputum cathelicidin, urokinase plasminogen activation system components, and cytokines discriminate cystic fibrosis, COPD, and asthma inflammation. Chest 128, 2316-2326. (Pubitemid 41507575)
    • (2005) Chest , vol.128 , Issue.4 , pp. 2316-2326
    • Xiao, W.1    Hsu, Y.-P.2    Ishizaka, A.3    Kirikae, T.4    Moss, R.B.5
  • 106
    • 0030942221 scopus 로고    scopus 로고
    • Purification and characterization of defensins from cystic fibrosis sputum
    • Soong, L.B., Ganz, T., Ellison, A., and Caughey, G.H. (1997) Purification and characterization of defensins from cystic fibrosis sputum. Inflamm. Res. 46, 98-102.
    • (1997) Inflamm. Res. , vol.46 , pp. 98-102
    • Soong, L.B.1    Ganz, T.2    Ellison, A.3    Caughey, G.H.4
  • 107
    • 31544463056 scopus 로고    scopus 로고
    • Glycosaminoglycans inhibit the antibacterial activity of LL-37 in biological fluids
    • DOI 10.1093/jac/dki460
    • Baranska-Rybak, W., Sonesson, A., Nowicki, R., and Schmidtchen, A. (2006) Glycosaminoglycans inhibit the antibacterial activity of LL-37 in biological fluids. J. Antimicrob. Chemother. 57, 260-265. (Pubitemid 43160167)
    • (2006) Journal of Antimicrobial Chemotherapy , vol.57 , Issue.2 , pp. 260-265
    • Baranska-Rybak, W.1    Sonesson, A.2    Nowicki, R.3    Schmidtchen, A.4
  • 108
    • 68949117860 scopus 로고    scopus 로고
    • LL-37 complexation with glycosaminoglycans in cystic fibrosis lungs inhibits antimicrobial activity, which can be restored by hypertonic saline
    • Bergsson, G. et al. (2009) LL-37 complexation with glycosaminoglycans in cystic fibrosis lungs inhibits antimicrobial activity, which can be restored by hypertonic saline. J. Immunol. 183, 543-551.
    • (2009) J. Immunol. , vol.183 , pp. 543-551
    • Bergsson, G.1
  • 109
    • 0037860827 scopus 로고    scopus 로고
    • Neutrophil elastase up-regulates human beta-defensin-2 expression in human bronchial epithelial cells
    • DOI 10.1016/S0014-5793(03)00577-5
    • Griffin, S., Taggart, C.C., Greene, C.M., O'Neill, S., and McElvaney, N.G. (2003) Neutrophil elastase up-regulates human beta-defensin-2 expression in human bronchial epithelial cells. FEBS Lett. 546, 233-236. (Pubitemid 36782417)
    • (2003) FEBS Letters , vol.546 , Issue.2-3 , pp. 233-236
    • Griffin, S.1    Taggart, C.C.2    Greene, C.M.3    O'Neill, S.4    McElvaney, N.G.5
  • 110
    • 27644445147 scopus 로고    scopus 로고
    • Respiratory epithelial cells require Toll-like receptor 4 for induction of human beta-defensin 2 by lipopolysaccharide
    • MacRedmond, R., Greene, C., Taggart, C.C., McElvaney, N., and O'Neill, S. (2005) Respiratory epithelial cells require Toll-like receptor 4 for induction of human beta-defensin 2 by lipopolysaccharide. Respir. Res. 6, 116.
    • (2005) Respir. Res. , vol.6 , pp. 116
    • MacRedmond, R.1    Greene, C.2    Taggart, C.C.3    McElvaney, N.4    O'Neill, S.5
  • 111
    • 77950249584 scopus 로고    scopus 로고
    • Binding a heparin derived disaccharide to defensin inspired peptides: Insights to antimicrobial inhibition from gas-phase measurements
    • McCullough, B.J. et al. (2010) Binding a heparin derived disaccharide to defensin inspired peptides: insights to antimicrobial inhibition from gas-phase measurements. Phys. Chem. Chem. Phys. 12, 3589-3596.
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 3589-3596
    • McCullough, B.J.1
  • 112
    • 0035131955 scopus 로고    scopus 로고
    • Dermatan sulphate is released by proteinases of common pathogenic bacteria and inactivates antibacterial alpha-defensin
    • DOI 10.1046/j.1365-2958.2001.02251.x
    • Schmidtchen, A., Frick, I.M., and Bjorck, L. (2001) Dermatan sulphate is released by proteinases of common pathogenic bacteria and inactivates antibacterial alpha-defensin. Mol. Microbiol. 39, 708-713. (Pubitemid 32162156)
    • (2001) Molecular Microbiology , vol.39 , Issue.3 , pp. 708-713
    • Schmidtchen, A.1    Frick, I.-M.2    Bjorck, L.3
  • 113
    • 78650129716 scopus 로고    scopus 로고
    • Interaction of human beta-defensin 2 (HBD2) with glycosaminoglycans
    • Seo, E.S. et al. (2010) Interaction of human beta-defensin 2 (HBD2) with glycosaminoglycans. Biochemistry 49, 10486-10495.
    • (2010) Biochemistry , vol.49 , pp. 10486-10495
    • Seo, E.S.1
  • 114
    • 27144468308 scopus 로고    scopus 로고
    • Interaction of chemokines and glycosaminoglycans: A new twist in the regulation of chemokine function with opportunities for therapeutic intervention
    • DOI 10.1016/j.cytogfr.2005.04.006, PII S1359610105000602, Chemokines
    • Johnson, Z., Proudfoot, A.E., and Handel, T.M. (2005) Interaction of chemokines and glycosaminoglycans: a new twist in the regulation of chemokine function with opportunities for therapeutic intervention. Cytokine Growth Factor Rev. 16, 625-636. (Pubitemid 41509199)
    • (2005) Cytokine and Growth Factor Reviews , vol.16 , Issue.6 , pp. 625-636
    • Johnson, Z.1    Proudfoot, A.E.2    Handel, T.M.3
  • 115
    • 0028004630 scopus 로고
    • Glycosamioglycan-protein interactions, a question of specificity
    • Spillmann, D.L. and Lindahl, U. (1994) Glycosamioglycan-protein interactions, a question of specificity. Curr. Opin. Struct. Biol. 4, 677-682.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 677-682
    • Spillmann, D.L.1    Lindahl, U.2
  • 117
    • 0031650702 scopus 로고    scopus 로고
    • Bio-specific sequences and domains in heparan sulphate and the regulation of cell growth and adhesion
    • DOI 10.1016/S0945-053X(98)90096-8
    • Lyon, M. and Gallagher, J.T. (1998) Bio-specific sequences and domains in heparan sulphate and the regulation of cell growth and adhesion. Matrix Biol. 17, 485-493. (Pubitemid 28566883)
    • (1998) Matrix Biology , vol.17 , Issue.7 , pp. 485-493
    • Lyon, M.1    Gallagher, J.T.2
  • 118
    • 0035922668 scopus 로고    scopus 로고
    • Comparison of hypertonic saline and alternate-day or daily recombinant human deoxyribonuclease in children with cystic fibrosis: A randomised trial
    • DOI 10.1016/S0140-6736(01)06412-1
    • Suri, R. et al. (2001) Comparison of hypertonic saline and alternate-day or daily recombinant human deoxyribonuclease in children with cystic fibrosis: a randomised trial. Lancet 358, 1316-1321. (Pubitemid 33016495)
    • (2001) Lancet , vol.358 , Issue.9290 , pp. 1316-1321
    • Suri, R.1    Metcalfe, C.2    Lees, B.3    Grieve, R.4    Flather, M.5    Normand, C.6    Thompson, S.7    Bush, A.8    Wallis, C.9
  • 120
    • 0030845454 scopus 로고    scopus 로고
    • Rheology of cystic fibrosis sputum after in vitro treatment with hypertonic saline alone and in combination with recombinant human deoxyribonuclease I
    • King, M., Dasgupta, B., Tomkiewicz, R.P., and Brown, N.E. (1997) Rheology of cystic fibrosis sputum after in vitro treatment with hypertonic saline alone and in combination with recombinant human deoxyribonuclease I. Am. J. Respir. Crit. Care Med. 156, 173-177. (Pubitemid 27293184)
    • (1997) American Journal of Respiratory and Critical Care Medicine , vol.156 , Issue.1 , pp. 173-177
    • King, M.1    Dasgupta, B.2    Tomkiewicz, R.P.3    Brown, N.E.4
  • 121
    • 38449109697 scopus 로고    scopus 로고
    • Mucoactive agents for airway mucus hypersecretory diseases
    • discussion 1193-1197
    • Rogers, D.F. (2007) Mucoactive agents for airway mucus hypersecretory diseases. Respir. Care 52, 1176-1193; discussion 1193-1197.
    • (2007) Respir. Care , vol.52 , pp. 1176-1193
    • Rogers, D.F.1
  • 124
    • 45849088060 scopus 로고    scopus 로고
    • The spray drying of unfractionated heparin: Optimization of the operating parameters
    • DOI 10.1080/03639040701657552, PII 793955669
    • Shur, J., Nevell, T.G., Shute, J.K., and Smith, J.R. (2008) The spray drying of unfractionated heparin: optimization of the operating parameters. Drug Dev. Ind. Pharm. 34, 559-568. (Pubitemid 351878680)
    • (2008) Drug Development and Industrial Pharmacy , vol.34 , Issue.6 , pp. 559-568
    • Shur, J.1    Nevell, T.G.2    Shute, J.K.3    Smith, J.R.4
  • 127
    • 0031054407 scopus 로고    scopus 로고
    • Examination of the mechanism by which heparin antagonizes activation of a model endothelium by interferon-gamma (IPN-gamma)
    • Douglas, M.S., Rix, D.A., Dark, J.H., Talbot, D., and Kirby, J.A. (1997) Examination of the mechanism by which heparin antagonizes activation of a model endothelium by interferon-gamma (IFN-gamma). Clin. Exp. Immunol. 107, 578-584. (Pubitemid 27102150)
    • (1997) Clinical and Experimental Immunology , vol.107 , Issue.3 , pp. 578-584
    • Douglas, M.S.1    Rix, D.A.2    Dark, J.H.3    Talbot, D.4    Kirby, J.A.5
  • 128
    • 22544457169 scopus 로고    scopus 로고
    • Modulation of acute inflammation by targeting glycosaminoglycan-cytokine interactions
    • DOI 10.1016/j.intimp.2005.04.010, PII S1567576905001153
    • Cripps, J.G., Crespo, F.A., Romanovskis, P., Spatola, A.F., and Fernandez-Botran, R. (2005) Modulation of acute inflammation by targeting glycosaminoglycan-cytokine interactions. Int. Immunopharmacol. 5, 1622-1632. (Pubitemid 41019433)
    • (2005) International Immunopharmacology , vol.5 , Issue.11 , pp. 1622-1632
    • Cripps, J.G.1    Crespo, F.A.2    Romanovskis, P.3    Spatola, A.F.4    Fernandez-Botran, R.5
  • 129
    • 78751670809 scopus 로고    scopus 로고
    • Hyaluronan as an immune regulator in human diseases
    • Jiang, D., Liang, J., and Noble, P.W. (2011) Hyaluronan as an immune regulator in human diseases. Physiol. Rev. 91, 221-264.
    • (2011) Physiol. Rev. , vol.91 , pp. 221-264
    • Jiang, D.1    Liang, J.A.2    Noble, P.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.