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Volumn 16, Issue 2, 2011, Pages 707-722

The cell-elastin-elastase(s) interacting triade directs elastolysis

Author keywords

Degradation; Elastase; Elastin; Elastokine; Elastolysis; Matrikine; Review

Indexed keywords

CELL SURFACE RECEPTOR; CYSTEINE PROTEINASE; ELASTIN; LEUKOCYTE ELASTASE; METALLOPROTEINASE; PANCREATIC ELASTASE; SERINE PROTEINASE; UNSATURATED FATTY ACID;

EID: 79955047967     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3714     Document Type: Article
Times cited : (21)

References (131)
  • 1
    • 0021705548 scopus 로고
    • Interaction between elastin and elastases and its role in the aging of the arterial wall, skin and other connective tissues. A review
    • DOI 10.1016/0047-6374(84)90015-0
    • Robert, L., M.P. Jacob, C. Francès, G. Godeau and W. Hornebeck: Interaction between elastin and elastases and its role in the aging of the arterial wall, skin and other connective tissues. Mech Ageing Dev 28, 155-166 (1984) (Pubitemid 15175749)
    • (1984) Mechanisms of Ageing and Development , vol.28 , Issue.2-3 , pp. 155-166
    • Robert, L.1    Jacob, M.P.2    Frances, C.3
  • 2
    • 0033180390 scopus 로고    scopus 로고
    • Aging of the vascular wall and atherosclerosis
    • Robert, L.: Aging of the vascular wall and atherosclerosis. Exp Gerontol 34, 491-501 (1999)
    • (1999) Exp Gerontol , vol.34 , pp. 491-501
    • Robert, L.1
  • 3
    • 0021919760 scopus 로고
    • Elastases and emphysema. Current assessment of the protease-antiprotease hypothesis
    • Janoff, A.: Elastases and emphysema. Current assessment of the protease-antiprotease hypothesis. Am Rev Respir Dis 132, 417-433 (1985) (Pubitemid 15229406)
    • (1985) American Review of Respiratory Disease , vol.132 , Issue.2 , pp. 417-433
    • Janoff, A.1
  • 4
    • 0021359164 scopus 로고
    • Elastin and elastic fibers in normal and pathologic skin
    • Frances, C. and L. Robert: Elastin and elastic fibers in normal and pathological skin. Int J Dermatol 23,166-179 (1984) (Pubitemid 14172208)
    • (1984) International Journal of Dermatology , vol.23 , Issue.3 , pp. 166-179
    • Frances, C.1    Robert, L.2
  • 6
    • 0002016013 scopus 로고
    • Elastases: Catalytic and biological properties
    • Regulation of matrix accumulation (Mecham R.P., ed.), Academic Press: New York
    • Bieth, J.G.: Elastases: catalytic and biological properties. In: Biology of extracellular matrix, vol.1: Regulation of matrix accumulation (Mecham R.P., ed.) Academic Press: New York, 217-230 (1986)
    • (1986) Biology of Extracellular Matrix , vol.1 , pp. 217-230
    • Bieth, J.G.1
  • 7
    • 70349101984 scopus 로고    scopus 로고
    • Role of the elastin receptor complex (SGal/cathA/Neu1) in skin repair and regeneration
    • Antonicelli, F., G. Bellon, S. Lorimier and W. Hornebeck: Role of the elastin receptor complex (SGal/cathA/Neu1) in skin repair and regeneration. Wound Repair Regen 17, 631-638 (2009)
    • (2009) Wound Repair Regen , vol.17 , pp. 631-638
    • Antonicelli, F.1    Bellon, G.2    Lorimier, S.3    Hornebeck, W.4
  • 8
    • 33745559712 scopus 로고    scopus 로고
    • Neutrophil serine proteases: Specific regulators of inflammation
    • DOI 10.1038/nri1841, PII N1841
    • Pham, C.T.: Neutrophil serine proteases: specific regulators of inflammation. Nat Rev Immunol 6, 541-550 (2006) (Pubitemid 43980526)
    • (2006) Nature Reviews Immunology , vol.6 , Issue.7 , pp. 541-550
    • Pham, C.T.N.1
  • 11
    • 0035988813 scopus 로고    scopus 로고
    • Matrix-directed regulation of pericellular proteolysis and tumor progression
    • DOI 10.1016/S1044-579X(02)00026-3
    • Hornebeck, W., H. Emonard, J.C. Monboisse and G. Bellon: Matrix-directed regulation of pericellular proteolysis and tumor progression. Semin Cancer Biol 12, 231-241 (2002) (Pubitemid 34833066)
    • (2002) Seminars in Cancer Biology , vol.12 , Issue.3 , pp. 231-241
    • Hornebeck, W.1    Emonard, H.2    Monboisse, J.-C.3    Bellon, G.4
  • 13
    • 0001468901 scopus 로고
    • Elastase and elastase inhibitor
    • Balo, J. and I. Banga: Elastase and elastase inhibitor. Nature 164, 491 (1949)
    • (1949) Nature , vol.164 , pp. 491
    • Balo, J.1    Banga, I.2
  • 14
    • 0023105553 scopus 로고
    • Characterization of pancreatic elastase II cDNAs: Two elastase II mRNAs are expressed in human pancreas
    • Kawashima, I., K. Shimoda and Y. Takihuchi: Characterization of pancreatic elastase II cDNAs: two elastase II mRNAs are expressed in human pancreas. DNA 6, 163-172 (1987) (Pubitemid 17054409)
    • (1987) DNA , vol.6 , Issue.2 , pp. 163-172
    • Kawashima, I.1    Tani, T.2    Shimoda, K.3    Takiguchi, Y.4
  • 15
    • 0030927748 scopus 로고    scopus 로고
    • Evolutionary silencing of the human elastase I gene (ELA1)
    • DOI 10.1093/hmg/6.6.897
    • Rose, S.D. and R. MacDonald: Evolutionary silencing of the human elastase I gene (ELA1). Hum Mol Genet 6, 897-903 (1997) (Pubitemid 27239074)
    • (1997) Human Molecular Genetics , vol.6 , Issue.6 , pp. 897-903
    • Rose, S.D.1    MacDonald, R.J.2
  • 16
    • 33646153277 scopus 로고    scopus 로고
    • Inactivity of recombinant ELA2B provides a new example of evolutionary elastase silencing in humans
    • Szepessy, E. and M. Sahin-Toth: Inactivity of recombinant ELA2B provides a new example of evolutionary elastase silencing in humans. Pancreatology 6, 117-122 (2006)
    • (2006) Pancreatology , vol.6 , pp. 117-122
    • Szepessy, E.1    Sahin-Toth, M.2
  • 17
    • 0034045031 scopus 로고    scopus 로고
    • Human elastase 1: Evidence for expression in the skin and the identification of a frequent frameshift polymorphism
    • DOI 10.1046/j.1523-1747.2000.00825.x
    • Talas, U., J. Dunlop, S. Khalaf, I.M. Leigh and D.P. Kelsell: Human elastase 1: Evidence for expression in the skin and identification of a frequent frameshift polymorphism. J. Invest Dermatol 114, 165-170 (2000) (Pubitemid 30195990)
    • (2000) Journal of Investigative Dermatology , vol.114 , Issue.1 , pp. 165-170
    • Talas, U.1    Dunlop, J.2    Khalaf, S.3    Leigh, I.M.4    Kelsell, D.P.5
  • 18
    • 38849143983 scopus 로고    scopus 로고
    • Neutrophil elastase, proteinase 3 and cathepsin G: Physicochemical properties, activity and physiopathological functions
    • DOI 10.1016/j.biochi.2007.10.009, PII S0300908407003033
    • Korkmaz, B., T. Moreau and F. Gauthier: Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties and physiopathological functions. Biochimie 90, 227-242 (2008) (Pubitemid 351187763)
    • (2008) Biochimie , vol.90 , Issue.2 , pp. 227-242
    • Korkmaz, B.1    Moreau, T.2    Gauthier, F.3
  • 19
    • 0033056463 scopus 로고    scopus 로고
    • The cell biology of leukocyte-mediated proteolysis
    • Owen, C.A. and E.J. Campbell: The cell biology of leukocyte-mediated proteolysis. J Leukoc Biol 65, 137-150 (1999) (Pubitemid 29077006)
    • (1999) Journal of Leukocyte Biology , vol.65 , Issue.2 , pp. 137-150
    • Owen, C.A.1    Campbell, E.J.2
  • 20
    • 16244397365 scopus 로고    scopus 로고
    • Neutrophil serine proteases: Potential key regulators of cell signalling during inflammation
    • Wiedow, O. and U. Meyer-Hoffert: Neutrophil serine proteases: potential key regulators of cell signalling during inflammation. J Intern Med 257, 319-328 (2005) (Pubitemid 40461184)
    • (2005) Journal of Internal Medicine , vol.257 , Issue.4 , pp. 319-328
    • Wiedow, O.1    Meyer-Hoffert, U.2
  • 21
    • 0026754577 scopus 로고
    • Three human elastase-like genes coordinately expressed in the myelomonocyte lineage are organized as a single genetic locus on 19pter
    • Zimmer, M., R.L. Medcalf, T.M. Fink, C. Mattmann, P. Lichter and D.E. Jenne: Three human elastase-like genes coordinately expressed in the myelomonocyte lineage are organized as a single genetic locus on 19pter. Proc Natl Acad Sci U.S.A 89, 8215-8219 (1992)
    • (1992) Proc Natl Acad Sci U.S.A , vol.89 , pp. 8215-8219
    • Zimmer, M.1    Medcalf, R.L.2    Fink, T.M.3    Mattmann, C.4    Lichter, P.5    Jenne, D.E.6
  • 22
    • 34347271912 scopus 로고    scopus 로고
    • The sulfate groups of chondroitin sulfate- and heparan sulfate-containing proteoglycans in neutrophil plasma membranes are novel binding sites for human leukocyte elastase and cathepsin G
    • DOI 10.1074/jbc.M608346200
    • Campbell, E.J. and C.A. Owen: The sulfate groups of chondroitin sulfate-and heparan sulfate-containing proteoglycan in neutrophil plasma membranes are novel binding sites for human leukocyte elastase and cathepsin G. J Biol Chem 282, 14645-14654 (2007) (Pubitemid 47100453)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.19 , pp. 14645-14654
    • Campbell, E.J.1    Owen, C.A.2
  • 24
    • 0016823808 scopus 로고
    • Isolation, purification and properties of aortic elastase
    • Hornebeck,W., J.C. Derouette and L. Robert: Isolation, purification and properties of aortic elastase. FEBS Lett 58, 66-70 (1975)
    • (1975) FEBS Lett , vol.58 , pp. 66-70
    • Derouette, J.C.1    Robert, L.2
  • 25
    • 0021078783 scopus 로고
    • Properties and subcellular localization of elastase-like activities of arterial smooth muscle cells in culture
    • DOI 10.1016/0304-4165(83)90360-4
    • Leake, D.S., W. Hornebeck, D. Brechemier, L. Robert and T.J. Peters: Properties and subcellular localization of elastase-like activities of arterial smooth cells in culture. Biochim Biophys Acta 761, 41-47 (1983) (Pubitemid 14202803)
    • (1983) Biochimica et Biophysica Acta - General Subjects , vol.761 , Issue.1 , pp. 41-47
    • Leake, D.S.1    Hornebeck, W.2    Brechemier, D.3
  • 26
    • 0028040868 scopus 로고
    • The endogenous vascular elastase that governs development and progression of monocrotaline-induced pulmonary hypertension in rats is a novel enzyme related to the serine proteinase adipsin
    • Zhu, L., D. Wigle, A. Hinek, J. Kobayashi, M. Zuker, H. Dodo, F.W. Keeley and M. Rabinovitch: The endogenous vascular elastase that governs development and progression of monocrotaline-induced hypertension in rats is a novel enzyme related to the serine proteinase adipsin. J. Clin Invest 94, 1163-1171(1994) (Pubitemid 24286459)
    • (1994) Journal of Clinical Investigation , vol.94 , Issue.3 , pp. 1163-1171
    • Zhu, L.1    Wigle, D.2    Hinek, A.3    Kobayashi, J.4    Ye, C.5    Zuker, M.6    Dodo, H.7    Keeley, F.W.8    Rabinovitch, M.9
  • 27
    • 0022628541 scopus 로고
    • Elastinolytic activity of human cathepsin L
    • Mason, RW, D.A. Johnson, A.J. Barrett and H.A. Chapman: Elastinolytic activity of human cathepsin L. Biochem J 233, 925-927 (1986) (Pubitemid 16116171)
    • (1986) Biochemical Journal , vol.233 , Issue.3 , pp. 925-927
    • Mason, R.W.1    Johnson, D.A.2    Barrett, A.J.3
  • 28
    • 4344670363 scopus 로고    scopus 로고
    • Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
    • DOI 10.1074/jbc.M403986200
    • Yasuda, Y., Z. Li, D. Greenbaum, M. Bogyo, E. Weber and D. Bromme: Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. J Biol Chem 279, 36761-36770 (2004) (Pubitemid 39129024)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36761-36770
    • Yasuda, Y.1    Li, Z.2    Greenbaum, D.3    Bogyo, M.4    Weber, E.5    Bromme, D.6
  • 29
    • 0027050951 scopus 로고
    • The specificity and elastinolytic activities of bovine cathepsins S and H
    • DOI 10.1016/0003-9861(92)90283-3
    • Xin, X.Q., B. Gunesekera and R.W. Mason: The specificity and elastinolytic activities of bovine cathepsins S and H. Arch Biochem Biophys 299, 334-339 (1992) (Pubitemid 23029039)
    • (1992) Archives of Biochemistry and Biophysics , vol.299 , Issue.2 , pp. 334-339
    • Xin, X.-Q.1    Gunesekera, B.2    Mason, R.W.3
  • 30
    • 0028673153 scopus 로고
    • Cathepsin S and related lysosomal endopeptidases
    • Kirschke, H. and B. Wiederanders: Cathepsin S and related lysosomal endopeptidases. Methods Enzymol 244, 500-511 (1994)
    • (1994) Methods Enzymol , vol.244 , pp. 500-511
    • Kirschke, H.1    Wiederanders, B.2
  • 31
  • 32
    • 0033776087 scopus 로고    scopus 로고
    • Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides
    • Guay, J., J.P. Falgueyret, A. Ducret, M.D. Percival and J.A. Mancini: Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides. Eur J Biochem 267, 6311-6318 (2000)
    • (2000) Eur J Biochem , vol.267 , pp. 6311-6318
    • Guay, J.1    Falgueyret, J.P.2    Ducret, A.3    Percival, M.D.4    Mancini, J.A.5
  • 33
    • 34249106050 scopus 로고    scopus 로고
    • Inhibition of cathepsin L-like proteases by cathepsin V propeptide
    • DOI 10.1515/BC.2007.053
    • Burden, R.E., P. Snoddy, C.A. Jefferies, B. Walker and C.J. Scott: Inhibition of cathepsin L-like proteases by cathepsin V propeptide. Biol Chem 388, 541-545 (2007) (Pubitemid 46800258)
    • (2007) Biological Chemistry , vol.388 , Issue.5 , pp. 541-545
    • Burden, R.E.1    Snoddy, P.2    Jefferies, C.A.3    Walker, B.4    Scott, C.J.5
  • 34
    • 27744440521 scopus 로고    scopus 로고
    • Caspases from apoptotic myocytes degrade extracellular matrix: A novel remodeling paradigm
    • Cowan, K.N., W.C. Leung, C. Mar, R. Bhattacharjee, Y. Zhu, and M. Rabinovitch: Caspases from apoptotic myocytes degrade extracellular matrix: a novel remodeling paradigm. FASEB J 19, 1848-1858 (2005)
    • (2005) FASEB J , vol.19 , pp. 1848-1858
    • Cowan, K.N.1    Leung, W.C.2    Mar, C.3    Bhattacharjee, R.4    Zhu, Y.5    Rabinovitch, M.6
  • 35
    • 45049083085 scopus 로고    scopus 로고
    • Mapping of macrophage elastase cleavage sites in insoluble human skin elastin
    • Taddese, S., A.S. Weiss, R.H.H. Neubert and C.E.H. Schmelzer: Mapping of macrophage elastase cleavage sites in insoluble human skin elastin. Matrix Biol 27, 420-428 (2008)
    • (2008) Matrix Biol , vol.27 , pp. 420-428
    • Taddese, S.1    Weiss, A.S.2    Neubert, R.H.H.3    Schmelzer, C.E.H.4
  • 37
    • 0019160540 scopus 로고
    • Degradation of connective tissue matrices by macrophages
    • Werb, Z., D.F. Bainton and P.A. Jones: Degradation of connective tissue matrices by macrophages. J Exp Med 152, 1537-1553 (1980)
    • (1980) J Exp Med , vol.152 , pp. 1537-1553
    • Werb, Z.1    Bainton, D.F.2    Jones, P.A.3
  • 38
    • 0025895193 scopus 로고
    • Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and-2 and punctuated metalloproteinase (PUMP)
    • Murphy, G, M.I. Cockett, R.V. Ward and A.J. Docherty: Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and-2 and punctuated metalloproteinase (PUMP) Biochem J 277, 277-279 (1991)
    • (1991) Biochem J , vol.277 , pp. 277-279
    • Murphy, G.1    Cockett, M.I.2    Ward, R.V.3    Docherty, A.J.4
  • 41
    • 0029005284 scopus 로고
    • Human macrophage metalloelastase. Genomic organization, chromosomal location, gene linkage, and tissue-specific expression
    • Belaaouaj, A., J.M. Shipley, D.K. Kobayashi, D.B. Zimonjic, N. Popescu, G.A. Silverman and S.D. Shapiro: Human macrophage metalloelastase. Genomic organization, chromosomal location, gene linkage, and tissue-specific expression. J Biol Chem 270, 14568-14575 (1995)
    • (1995) J Biol Chem , vol.270 , pp. 14568-14575
    • Belaaouaj, A.1    Shipley, J.M.2    Kobayashi, D.K.3    Zimonjic, D.B.4    Popescu, N.5    Silverman, G.A.6    Shapiro, S.D.7
  • 43
    • 0025952928 scopus 로고
    • Complete structure of the human gene for 92-kDa type IV collagenase divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells
    • Huhtala, P., A.Tuuttila, L.T. Chow, J. Lohi, J. Keski-Oja and K. Tryggvason: Complete structure of the human gene for 92-kDa type IV collagenase. Divergent regulation of expression for the 92-and 72-kilodalton enzyme genes in HT-1080 cells. J Biol Chem 266, 16485-16490 (1991) (Pubitemid 21907825)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.25 , pp. 16485-16490
    • Huhtala, P.1    Tuuttila, A.2    Chow, L.T.3    Lohi, J.4    Keski-Oja, J.5    Tryggvason, K.6
  • 44
    • 0026630048 scopus 로고
    • Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase and activation of the proenzyme with stromelysin
    • Goldberg, G.I., A. Strongin, I.E. Collier, L.T. Genrich and B.L. Marmer: Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase and activation of the proenzyme with stromelysin. J Biol Chem 267, 4583-4591 (1992)
    • (1992) J Biol Chem , vol.267 , pp. 4583-4591
    • Goldberg, G.I.1    Strongin, A.2    Collier, I.E.3    Genrich, L.T.4    Marmer, B.L.5
  • 46
    • 0026096865 scopus 로고
    • On the structure and chromosome location of the 72-and 92-kDa human type IV collagenase genes
    • Collier, I.E., G.A. Bruns, G.I. Goldberg and D.S. Gerhard: On the structure and chromosome location of the 72-and 92-kDa human type IV collagenase genes. Genomics 9, 429-434 (1991)
    • (1991) Genomics , vol.9 , pp. 429-434
    • Collier, I.E.1    Bruns, G.A.2    Goldberg, G.I.3    Gerhard, D.S.4
  • 47
    • 0035801473 scopus 로고    scopus 로고
    • Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion
    • DOI 10.1093/emboj/20.17.4782
    • Itoh, Y., A. Takamura, N. Ito, H. Sato, N. Suenaga, T. Aoki and M. Seiki: Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. EMBO J 20, 4782-4793 (2001) (Pubitemid 32848631)
    • (2001) EMBO Journal , vol.20 , Issue.17 , pp. 4782-4793
    • Itoh, Y.1    Takamura, A.2    Ito, N.3    Maru, Y.4    Sato, H.5    Suenaga, N.6    Aoki, T.7    Seiki, M.8
  • 48
    • 0030068937 scopus 로고    scopus 로고
    • The structural basis for the elastolytic activity of the 92-kDa and 72-kDa gelatinases. Role of the fibronectin type II-like repeats
    • Shipley, J.M., G.A. Doyle, C.J. Fliszar, Q.Z. Ye, L.L. Johnson, S.D. Shapiro, H.G. Welgus and R.M. Senior: The structural basis for the elastolytic activity of the 92-kDa and 72-kDa gelatinases. Role of the fibronectin type II-like repeats. J Biol Chem 271, 4335-4341 (1996)
    • (1996) J Biol Chem , vol.271 , pp. 4335-4341
    • Shipley, J.M.1    Doyle, G.A.2    Fliszar, C.J.3    Ye, Q.Z.4    Johnson, L.L.5    Shapiro, S.D.6    Welgus, H.G.7    Senior, R.M.8
  • 50
    • 0026775558 scopus 로고
    • Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanism proposed for other matrix metalloproteinases
    • Crabbe, T., F. Willenbrock, D. Eaton, P. Hynds, A.F. Carne, G. Murphy and A.J.P. Docherty: Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanism proposed for other matrix metalloproteinases. Biochemistry 31, 8500-8507 (1992)
    • (1992) Biochemistry , vol.31 , pp. 8500-8507
    • Crabbe, T.1    Willenbrock, F.2    Eaton, D.3    Hynds, P.4    Carne, A.F.5    Murphy, G.6    Docherty, A.J.P.7
  • 52
    • 72949133071 scopus 로고
    • The reaction between elastase and elastic tissue. 4. Soluble elastins
    • Hall, D.A. and J.W. Czerkawski: The reaction between elastase and elastic tissue. 4. Soluble elastins. Biochem J 80, 121-128 (1961)
    • (1961) Biochem J , vol.80 , pp. 121-128
    • Hall, D.A.1    Czerkawski, J.W.2
  • 53
    • 0016366804 scopus 로고
    • Partial purification and properties of porcine pancreatic elastase II
    • Ardelt, W.: Partial purification and properties of porcine pancreatic elastase II. Biochim Biophys Acta 341, 318-326 (1974)
    • (1974) Biochim Biophys Acta , vol.341 , pp. 318-326
    • Ardelt, W.1
  • 54
    • 0015244369 scopus 로고
    • The non-electrostatic nature of the adsorption of elastase and other basic proteins on elastin
    • Gertler, A.: The non-electrostatic nature of the adsorption of elastase and other basic proteins on elastin. Eur J Biochem 20, 541-546 (1971)
    • (1971) Eur J Biochem , vol.20 , pp. 541-546
    • Gertler, A.1
  • 56
    • 0015980135 scopus 로고
    • Cinétique hétérogène de l'interaction élastine-élastase
    • Robert, B., W. Hornebeck and L. Robert: Cinétique hétérogène de l'interaction élastine- élastase. Biochimie 56, 239-244 (1974)
    • (1974) Biochimie , vol.56 , pp. 239-244
    • Robert, B.1    Hornebeck, W.2    Robert, L.3
  • 57
    • 0025024729 scopus 로고
    • Interaction of human leukocyte elastase with soluble and insoluble protein substrates. A practical kinetic approach
    • DOI 10.1016/0167-4838(90)90133-Z
    • Baici A.: Interaction of human leukocyte elastase with soluble and insoluble substrates. A practical kinetic approach. Biochim Biophys Acta 1040, 355-364 (1990) (Pubitemid 20298386)
    • (1990) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1040 , Issue.3 , pp. 355-364
    • Baici, A.1
  • 58
    • 0036008407 scopus 로고    scopus 로고
    • 1- proteinase inhibitor: A mechanism for the incomplete inhibition of ongoing elastolysis
    • Ying, Q.L. and S.R. Simon: Elastolysis by proteinase 3 and its inhibition by alpha(1)-proteinase inhibitor: a mechanism for the incomplete inhibition of ongoing elastolysis. Am J Respir Cell Mol Biol 26, 356-361 (2002) (Pubitemid 34170062)
    • (2002) American Journal of Respiratory Cell and Molecular Biology , vol.26 , Issue.3 , pp. 356-361
    • Ying, Q.-L.1    Simon, S.R.2
  • 59
    • 0019800423 scopus 로고
    • Stimulation of the elastolytic activity of leukocyte elastase by leukocyte cathepsin G
    • Boudier, C., C. Holle and J.G. Bieth: Stimulation of the elastolytic activity of leukocyte elastase by leukocyte cathepsin G. J Biol Chem 256, 10256-10258 (1981)
    • (1981) J Biol Chem , vol.256 , pp. 10256-10258
    • Boudier, C.1    Holle, C.2    Bieth, J.G.3
  • 60
    • 0020955341 scopus 로고
    • Regulation of elastolysis of insoluble elastin by human leukocyte elastase: Stimulation by lysine-rich ligands, anionic detergents, and ionic strength
    • Lonky, S.A. and H. Wohl: Regulation of elastolysis of insoluble elastin by human leukocyte elastase: stimulation by lysine-rich ligands, anionic detergents and ionic strength. Biochemistry 22, 3714-3720 (1983) (Pubitemid 13032718)
    • (1983) Biochemistry , vol.22 , Issue.15 , pp. 3714-3720
    • Lonky, S.A.1    Wohl, H.2
  • 61
    • 67650264154 scopus 로고    scopus 로고
    • A proposed interaction mechanism between elastin-derived peptides and the elastin/laminin receptor-binding domain
    • Moroy, G., A. Ostuni, A. Pepe, A.M. Tamburro, A.J. Alix and S. Héry-Huynh: A proposed interaction mechanism between elastin-derived peptides and the elastin/laminin receptor-binding domain. Proteins 76, 461-476 (2009)
    • (2009) Proteins , vol.76 , pp. 461-476
    • Moroy, G.1    Ostuni, A.2    Pepe, A.3    Tamburro, A.M.4    Alix, A.J.5    Héry-Huynh, S.6
  • 63
    • 0030907533 scopus 로고    scopus 로고
    • Binding of 92 kDa and 72 kDa progelatinases to insoluble elastin modulates their proteolytic activation
    • Emonard, H. and W. Hornebeck: Binding of 92 kDa and 72 kDa progelatinases to insoluble elastin modulates their proteolytic activation. Biol Chem 378, 265-271 (1997) (Pubitemid 27230612)
    • (1997) Biological Chemistry , vol.378 , Issue.3-4 , pp. 265-271
    • Emonard, H.1    Hornebeck, W.2
  • 64
    • 0037013250 scopus 로고    scopus 로고
    • Substrate binding of gelatinase B induces its enzymatic activity in the presence of intact propeptide
    • DOI 10.1074/jbc.M110931200
    • Bannikov, G.A., T.V. Karelina, I.E. Collier, B.L. Marmer and G.I. Goldberg: Substrate binding of gelatinase B induces its enzymatic activity in the presence of intact propeptide. J Biol Chem 277, 16022-16027 (2002) (Pubitemid 34967885)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 16022-16027
    • Bannikov, G.A.1    Karelina, T.V.2    Collier, I.E.3    Marmer, B.L.4    Goldberg, G.I.5
  • 65
    • 0029010660 scopus 로고
    • Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human type IV collagenase. High affinity binding to native type i collagen but not native type IV collagen
    • Steffensen, B. and C.M. Overall: Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human type IV collagenase. High affinity binding to native type I collagen but not native type IV collagen. J Biol Chem 270, 11555-11566 (1995)
    • (1995) J Biol Chem , vol.270 , pp. 11555-11566
    • Steffensen, B.1    Overall, C.M.2
  • 67
    • 0019985854 scopus 로고
    • Effect of different elastase inhibitors on leukocyte elastase pre-adsorbed to elastin
    • Hornebeck, W. and H.P. Schnebli: Effect of different elastase inhibitors on leukocyte elastase pre-adsorbed to elastin. Hoppe Seylers Z Physiol Chem 363, 455-458(1982) (Pubitemid 12084589)
    • (1982) Hoppe-Seyler's Zeitschrift fur Physiologische Chemie , vol.363 , Issue.4 , pp. 455-458
    • Hornebeck, W.1    Schnebli, H.P.2
  • 68
    • 0023220530 scopus 로고
    • 1- proteinase inhibitor and bronchial antileukoprotease: Different results using insoluble elastin or synthetic low molecular weight substrates
    • Kramps, J.A., H.M. Morrison, D. Burnett, J.H. Dijkman and R.A. Stockley: Determination of elastase inhibitory activity of alpha 1-proteinase inhibitor and bronchial antileukoprotease: different results using insoluble elastin or synthetic low molecular weight substrates. Scand J Clin Lab Invest 47, 405-410 (1987) (Pubitemid 17096912)
    • (1987) Scandinavian Journal of Clinical and Laboratory Investigation , vol.47 , Issue.4 , pp. 405-410
    • Kramps, J.A.1    Morrison, H.M.2    Burnett, D.3
  • 69
    • 0025390464 scopus 로고
    • Inhibition of human leukocyte elastase bound to elastin: Relative ineffectiveness and two mechanisms of inhibitory activity
    • Morrison, H.M., H.G. Welgus, R.A. Stockley, D. Burnett and E.J. Campbell: Inhibition of human leukocyte elastase bound to elastin: relative ineffectiveness and two mechanisms of inhibitory activity. Am J Respir Cell Mol Biol 2, 263-269 (1990)
    • (1990) Am J Respir Cell Mol Biol , vol.2 , pp. 263-269
    • Morrison, H.M.1    Welgus, H.G.2    Stockley, R.A.3    Burnett, D.4    Campbell, E.J.5
  • 70
    • 0022461518 scopus 로고
    • 1-proteinase inhibitor and bronchial inhibitor. Potent inhibition of elastin-bound elastase by bronchial inhibitor
    • Bruch, M. and J.G. Bieth: Influence of elastin on the inhibition of leucocyte elastase by alpha 1-proteinase inhibitor and bronchial inhibitor. Potent inhibition of elastin-bound elastase by bronchial inhibitor. Biochem J 238, 269-273 (1986) (Pubitemid 16025004)
    • (1986) Biochemical Journal , vol.238 , Issue.1 , pp. 269-273
    • Bruch, M.1    Bieth, J.G.2
  • 72
    • 0034193629 scopus 로고    scopus 로고
    • Analysis of the ex vivo specificity of human gelatinases A and B towards skin collagen and elastic fibers by computerized morphometry
    • DOI 10.1016/S0945-053X(00)00057-3, PII S0945053X00000573
    • Berton, A., G. Godeau, H. Emonard, K. Baba, P. Bellon, W. Hornebeck and G. Bellon: Analysis of the ex vivo specificity of human gelatinases A and B towards skin collagen and elastic fibers by computerized morphometry Matrix Biol 19, 139-148 (2000) (Pubitemid 30332437)
    • (2000) Matrix Biology , vol.19 , Issue.2 , pp. 139-148
    • Berton, A.1    Godeau, G.2    Emonard, H.3    Baba, K.4    Bellon, P.5    Hornebeck, W.6    Bellon, G.7
  • 73
    • 70450159308 scopus 로고    scopus 로고
    • Shed syndecan-1 restricts neutrophil elastase from alpha-1 antitrypsin inhibition in neutrophilic airway inflammation
    • Chan, S.C., V.O. Leung, M.S. Ip and D.K. Shum: Shed syndecan-1 restricts neutrophil elastase from alpha-1 antitrypsin inhibition in neutrophilic airway inflammation. Am J Respir Cell Mol Biol 41, 620-628 (2009)
    • (2009) Am J Respir Cell Mol Biol , vol.41 , pp. 620-628
    • Chan, S.C.1    Leung, V.O.2    Ip, M.S.3    Shum, D.K.4
  • 74
    • 43049166916 scopus 로고    scopus 로고
    • Human neutrophil elastase: Mediator and therapeutic target in atherosclerosis
    • Henriksen, P.A. and J.M. Sallenave: Human neutrophil elastase: mediator and therapeutic target in atherosclerosis. Int J Biochem Cell Biol 40, 1095-1100 (2008)
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1095-1100
    • Henriksen, P.A.1    Sallenave, J.M.2
  • 75
    • 43049139847 scopus 로고    scopus 로고
    • Leukocyte cell surface proteinases: Regulation of expression, functions and mechanisms of surface localization
    • Owen, C.A.: Leukocyte cell surface proteinases: regulation of expression, functions and mechanisms of surface localization. Int J Biochem Cell Biol 40, 1246-1272 (2008)
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1246-1272
    • Owen, C.A.1
  • 76
    • 59449107340 scopus 로고    scopus 로고
    • Membrane-type1 matrix metalloproteinase regulates macrophage-dependent elastolytic activity and aneurysm formation in vivo
    • Xiong, W., R. Knispel, J. MacTaggart, T.C. Greiner, S. J. Weiss and B. T. Baxter: Membrane-type1 matrix metalloproteinase regulates macrophage-dependent elastolytic activity and aneurysm formation in vivo. J Biol Chem 284, 1765-1771 (2009)
    • (2009) J Biol Chem , vol.284 , pp. 1765-1771
    • Xiong, W.1    Knispel, R.2    MacTaggart, J.3    Greiner, T.C.4    Weiss, S.J.5    Baxter, B.T.6
  • 78
    • 0025820288 scopus 로고
    • Mechanisms of interaction between human skin fibroblasts and elastin: Differences between elastin fibres and derived peptides
    • Groult, V., W. Hornebeck, P. Ferrari, J.M. Tixier, L. Robert and M.P. Jacob: Mechanisms of interaction between human skin fibroblasts and elastin: differences between elastin fibres and derived peptides. Cell Biochem Funct 9, 171-182 (1991)
    • (1991) Cell Biochem Funct , vol.9 , pp. 171-182
    • Groult, V.1    Hornebeck, W.2    Ferrari, P.3    Tixier, J.M.4    Robert, L.5    Jacob, M.P.6
  • 79
    • 0035226657 scopus 로고    scopus 로고
    • Effect of elastin peptides on the production of matrix metalloproteinase-2 by human skin fibroblasts in culture
    • Huet, E., B. Brassart, J. Wallach, L. Debelle, B. Haye, H. Emonard and W. Hornebeck: Effect of elastin peptides on the production of matrix metalloproteinase-2 by human skin fibroblasts in culture. J Soc Biol 195, 165-172 (2001)
    • (2001) J Soc Biol , vol.195 , pp. 165-172
    • Huet, E.1    Brassart, B.2    Wallach, J.3    Debelle, L.4    Haye, B.5    Emonard, H.6    Hornebeck, W.7
  • 81
    • 33750495804 scopus 로고    scopus 로고
    • A critical role for the membrane-type 1 matrix metalloproteinase in collagen phagocytosis
    • DOI 10.1091/mbc.E06-06-0486
    • Lee, H., C.M. Overall, C.A. McCullough and J.A. Sodek: A critical role for the membrane-type 1 matrix metalloproteinase in collagen phagocytosis. Mol Biol Cell 17, 4812-4826 (2006) (Pubitemid 44665750)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.11 , pp. 4812-4826
    • Lee, H.1    Overall, C.M.2    McCulloch, C.A.3    Sodek, J.4
  • 84
    • 0042330309 scopus 로고    scopus 로고
    • Inducible expression of tissue inhibitor of metalloproteinases-resistant matrix metalloproteinase-9 on the cell surface of neutrophils
    • DOI 10.1165/rcmb.2003-0034OC
    • Owen, C.A., Z. Hu, B. Barrick and S.D. Shapiro: Inducible expression of tissue inhibitor of metalloproteinases-resistantmatrix metalloproteinase-9 on the cell surface of neutrophils. Am J Respir Cell Mol Biol 29, 283-294 (2003) (Pubitemid 37093986)
    • (2003) American Journal of Respiratory Cell and Molecular Biology , vol.29 , Issue.3 , pp. 283-294
    • Owen, C.A.1    Hu, Z.2    Barrick, B.3    Shapiro, S.D.4
  • 87
    • 46249116531 scopus 로고    scopus 로고
    • RECK, a novel matrix metalloproteinase regulator
    • Meng, N., H. Zhang and X.F. Sun: RECK, a novel matrix metalloproteinase regulator. Histol Histopathol 23, 1003-1010 (2008)
    • (2008) Histol Histopathol , vol.23 , pp. 1003-1010
    • Meng, N.1    Zhang, H.2    Sun, X.F.3
  • 88
    • 15244352841 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase (MMP) activity by the low-density lipoprotein receptor-related protein (LRP). A new function for an "old friend"
    • DOI 10.1016/j.biochi.2004.11.013
    • Emonard, H., G. Bellon, P. de Diesbach, M. Mettlen, W. Hornebeck and P.J. Courtoy: Regulation of matrix metalloproteinase (MMP) activity by the low density lipoprotein receptor-related protein (LRP). A new function for an old friend. Biochimie 87, 369-376 (2005) (Pubitemid 40387616)
    • (2005) Biochimie , vol.87 , Issue.3-4 SPEC. ISS. , pp. 369-376
    • Emonard, H.1    Bellon, G.2    De Diesbach, P.3    Mettlen, M.4    Hornebeck, W.5    Courtoy, P.J.6
  • 89
    • 0035896646 scopus 로고    scopus 로고
    • Extracellular matrix metalloproteinase 2 levels are regulated by the low density lipoprotein-related scavenger receptor and thrombospondin 2
    • Yang, Z., D.K. Strickland and P. Bornstein: Extracellular matrix metalloproteinase 2 levels are regulated by the low density lipoprotein-related scavenger receptor and thrombospondin 2. J Biol Chem 276, 8403-8408 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 8403-8408
    • Yang, Z.1    Strickland, D.K.2    Bornstein, P.3
  • 91
    • 0035805530 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein modulates levels of matrix metalloproteinase 9( MMP-9) by mediating its cellular catabolism
    • Hahn-Dantona, E., J.F. Ruiz, P. Bornstein and D.K. Strickland: The low density lipoprotein receptor-related protein modulates levels of matrix metalloproteinase 9( MMP-9) by mediating its cellular catabolism. J Biol Chem 276, 15498-15503 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 15498-15503
    • Hahn-Dantona, E.1    Ruiz, J.F.2    Bornstein, P.3    Strickland, D.K.4
  • 93
    • 0023938183 scopus 로고
    • The elastin receptor: A galactoside-binding protein
    • Hinek, A., D.S. Wrenn, R.P. Mecham and S.H. Barondes: The elastin receptor: a galactoside-binding protein. Science 239, 1539-1541 (1988)
    • (1988) Science , vol.239 , pp. 1539-1541
    • Hinek, A.1    Wrenn, D.S.2    Mecham, R.P.3    Barondes, S.H.4
  • 94
    • 43049104500 scopus 로고    scopus 로고
    • Fragments of extracellular matrix as mediators of inflammation
    • Adair-Kirk, T.L. and R.M. Senior: Fragments of extracellular matrix as mediators of inflammation. Int J Biochem Cell Biol 40, 1101-1110 (2008)
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1101-1110
    • Adair-Kirk, T.L.1    Senior, R.M.2
  • 95
    • 0008490902 scopus 로고    scopus 로고
    • Biological roles of the non-integrin elastin/laminin receptor
    • Hinek, A.: Biological roles of the non-integrin elastin/laminin receptor. Biol Chem 377, 471-480 (1996)
    • (1996) Biol Chem , vol.377 , pp. 471-480
    • Hinek, A.1
  • 98
    • 22144457065 scopus 로고    scopus 로고
    • Elastin-derived peptides and TGF-β1 induce osteogenic responses in smooth muscle cells
    • DOI 10.1016/j.bbrc.2005.06.119, PII S0006291X05013495
    • Simionescu, A., K. Philips and N. Vyavahare: Elastin-derived peptides and TGF-beta 1 induce osteogenic responses in smooth muscle cells. Biochem Biophys Res Commun 334, 524-532 (2005) (Pubitemid 40982398)
    • (2005) Biochemical and Biophysical Research Communications , vol.334 , Issue.2 , pp. 524-532
    • Simionescu, A.1    Philips, K.2    Vyavahare, N.3
  • 99
    • 34547691571 scopus 로고    scopus 로고
    • Osteogenic responses in fibroblasts activated by elastin degradation products and transforming growth factor-β1: Role of myofibroblasts in vascular calcification
    • DOI 10.2353/ajpath.2007.060930
    • Simionescu, A., D.T. Simionescu and N.T. Vyavahare: Osteogenic responses in fibroblasts activated by elastin degradation products and transforming growth factor beta1. Am J. Pathol 171, 116-123 (2007) (Pubitemid 47339232)
    • (2007) American Journal of Pathology , vol.171 , Issue.1 , pp. 116-123
    • Simionescu, A.1    Simionescu, D.T.2    Vyavahare, N.R.3
  • 100
    • 40749112316 scopus 로고    scopus 로고
    • Locally generated VGVAPG and VAPG elastin-derived peptides amplify melanoma invasion via the galectin-3 receptor
    • DOI 10.1002/ijc.23296
    • Pocza, P., H. Suli-Vargha, Z. Darvas and A. Falus: Locally generated VGVAPG and VAPG elastin-derived peptides amplify melanoma invasion via the galectin-3 receptor. Int J Cancer 122, 1972-1980 (2008) (Pubitemid 351441185)
    • (2008) International Journal of Cancer , vol.122 , Issue.9 , pp. 1972-1980
    • Pocza, P.1    Suli-Vargha, H.2    Darvas, Z.3    Falus, A.4
  • 101
    • 0029056536 scopus 로고
    • Stimulation of cell proliferation and autoregulation of elastin expression by elastin peptide VGGVG in cultured chick vascular smooth muscle cells
    • Wachi, H., Y. Seyama, S. Yamashita, H. Suganami, Y. Uemura, K. Okamoto, H. Yamada and S. Tajima: Stimulation of cell proliferation and autoregulation of elastin expression by elastin peptide VGGVG in cultured chick vascular smooth muscle cells. FEBS Lett 368, 215-219 (1995)
    • (1995) FEBS Lett , vol.368 , pp. 215-219
    • Wachi, H.1    Seyama, Y.2    Yamashita, S.3    Suganami, H.4    Uemura, Y.5    Okamoto, K.6    Yamada, H.7    Tajima, S.8
  • 102
    • 34247377719 scopus 로고    scopus 로고
    • Induction of macrophage migration through lactose-insentive receptor by elastin-derived nonapeptides and their analog
    • DOI 10.1002/psc.845
    • Maeda, I., N. Mizoiri, M.P. Briones and K. Okamoto: Induction of macrophage migration through lactoseinsensitive receptor by elastin-derived nonapeptides and their analog. J Peptide Sci 13, 263-268 (2007) (Pubitemid 46638197)
    • (2007) Journal of Peptide Science , vol.13 , Issue.4 , pp. 263-268
    • Maeda, I.1    Mizoiri, N.2    Briones, M.P.P.3    Okamoto, K.4
  • 105
    • 34347389467 scopus 로고    scopus 로고
    • Binding of elastin peptides to S-Gal protects the heart against ischemia/reperfusion injury by triggering the RISK pathway
    • DOI 10.1096/fj.06-6477com
    • Robinet, A., H. Millart, F. Oszust, W. Hornebeck and G. Bellon: Binding of elastin peptides to S-gal protects the heart against ischemia/reperfusion injury by triggering the RISK pathway. FASEB J 21, 1968-1978 (2007) (Pubitemid 47026433)
    • (2007) FASEB Journal , vol.21 , Issue.9 , pp. 1968-1978
    • Robinet, A.1    Millart, H.2    Oszust, F.3    Hornebeck, W.4    Bellon, G.5
  • 106
    • 0030788508 scopus 로고    scopus 로고
    • Elastin degradation products induce adventitial angiogenesis in the Anidjar/Dobrin rat aneurysm model
    • DOI 10.1016/S0039-6060(97)90262-2
    • Nackman, G.B., F.J. Karkowski, V.J. Halpern, H.P. Gaetz, and M.D. Tilson: Elastin degradation products induce adventitial angiogenesis in the Anidjar/Dobrin rat aneurysm model. Surgery 122, 39-44 (1997) (Pubitemid 27295165)
    • (1997) Surgery , vol.122 , Issue.1 , pp. 39-44
    • Nackman, G.B.1    Karkowski, F.J.2    Halpern, V.J.3    Gaetz, H.P.4    Tilson, M.D.5
  • 107
    • 0036479572 scopus 로고    scopus 로고
    • Monocyte chemotactic activity in human abdominal aortic aneurysms: Role of elastin degradation peptides and the 67-kD cell surface elastin receptor
    • DOI 10.1067/mva.2002.120382
    • Hance KA, M. Tataria, SJ Ziporin, JK Lee and RW Thompson. Monocyte chemotactic activity in human abdominal aneurysms: Role of elastin degradation peptides and the 67-kD surface elastin receptor. J. Vasc. Surg. 35, 254-261 ( 2002) (Pubitemid 44718627)
    • (2002) Journal of Vascular Surgery , vol.35 , Issue.2 , pp. 254-261
    • Hance, K.A.1    Tataria, M.2    Ziporin, S.J.3    Lee, J.K.4    Thompson, R.W.5
  • 109
    • 33750029459 scopus 로고    scopus 로고
    • Study of human lung elastin degradation by different elastases using high-performance liquid chromatography/mass spectrometry
    • DOI 10.1016/j.ab.2006.07.011, PII S0003269706005240
    • Barroso, B., N. Abello and R. Bischoff: Study of human lung elastin degradation by different elastases using high-performance liquid chromatography/mass spectrometry. Anal Biochem 358, 216-224 (2006) (Pubitemid 44573072)
    • (2006) Analytical Biochemistry , vol.358 , Issue.2 , pp. 216-224
    • Barroso, B.1    Abello, N.2    Bischoff, R.3
  • 110
    • 62749084929 scopus 로고    scopus 로고
    • In vitro degradation of human tropoelastin by MMP-12 and the generation of matrikines from domain 24
    • Taddese, S., A.S. Weiss, G. Jahreis, R.H.H. Neubert, and C.E.H. Schmelzer: In vitro degradation of human tropoelastin by MMP-12 and the generation of matrikines from domain 24. Matrix Biol 28, 84-91 (2009)
    • (2009) Matrix Biol , vol.28 , pp. 84-91
    • Taddese, S.1    Weiss, A.S.2    Jahreis, G.3    Neubert, R.H.H.4    Schmelzer, C.E.H.5
  • 111
    • 0034257889 scopus 로고    scopus 로고
    • The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo
    • Liu, Z., X. Zhou, S.D. Shapiro, J.M. Shipley, S.S. Twining, R.M. Senior and Z. Werb: The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo. Cell 102, 647-655 (2000)
    • (2000) Cell , vol.102 , pp. 647-655
    • Liu, Z.1    Zhou, X.2    Shapiro, S.D.3    Shipley, J.M.4    Twining, S.S.5    Senior, R.M.6    Werb, Z.7
  • 112
    • 0029019838 scopus 로고
    • Preferential inactivation of tissue inhibitor of metalloproteinases-1 that is bound to the precursor of matrix metalloproteinase 9 (progelatinase B) by human neutrophil elastase
    • Itoh, Y. and H. Nagase: Preferential inactivation of tissue inhibitor of metalloproteinases-1 that is bound to the precursor of matrix metalloproteinase 9 (progelatinase B) by human neutrophil elastase. J Biol Chem 270, 16518-16521 (1995)
    • (1995) J Biol Chem , vol.270 , pp. 16518-16521
    • Itoh, Y.1    Nagase, H.2
  • 113
    • 77951951482 scopus 로고    scopus 로고
    • Human neutrophil elastase-mediated cleavage sites of MMP-9 and TIMP-1: Implications to cystic fibrosis proteolytic dysfunction
    • Epub
    • Jackson PL, X. Xu, L. Wilson, NM Weathington, JP Clancy, JE Blalock and A; Gaggar: Human neutrophil elastase-mediated cleavage sites of MMP-9 and TIMP-1: implications to cystic fibrosis proteolytic dysfunction. Mol. Med.( Epub) 2010
    • (2010) Mol. Med.
    • Jackson, P.L.1    Xu, X.2    Wilson, L.3    Weathington, N.M.4    Clancy, J.P.5    Blalock, J.E.6    Gaggar, A.7
  • 114
    • 67651112138 scopus 로고    scopus 로고
    • Control of melanoma invasiveness by anticollagenolytic agents: A reappraisal of an old concept
    • Bourguet, E., J. Sapi, H. Emonard and W. Hornebeck: Control of melanoma invasiveness by anticollagenolytic agents: a reappraisal of an old concept. Anticancer Agents Med Chem 9, 576-597(2009)
    • (2009) Anticancer Agents Med Chem , vol.9 , pp. 576-597
    • Bourguet, E.1    Sapi, J.2    Emonard, H.3    Hornebeck, W.4
  • 115
    • 50649119519 scopus 로고    scopus 로고
    • Selective modulation of Matrix metalloproteinase 9(MMP-9) functions via exosite inhibition
    • Lauer-Fields, J.L., J.K. Whitehead, S. Li, R.P. Hammer, K. Brew and G.B. Fields: Selective modulation of Matrix metalloproteinase 9(MMP-9) functions via exosite inhibition. J Biol Chem 283, 20087-20095 (2008)
    • (2008) J Biol Chem , vol.283 , pp. 20087-20095
    • Lauer-Fields, J.L.1    Whitehead, J.K.2    Li, S.3    Hammer, R.P.4    Brew, K.5    Fields, G.B.6
  • 116
    • 0035827538 scopus 로고    scopus 로고
    • Involvement of fibronectin type II repeats in the efficient inhibition of gelatinases A and B by longchain unsaturated fatty acids
    • Berton, A., V. Rigot, E. Huet, M. Decarme, Y. Eeckhout, L. Patthy, G. Godeau, W. Hornebeck, G. Bellon and H. Emonard: Involvement of fibronectin type II repeats in the efficient inhibition of gelatinases A and B by longchain unsaturated fatty acids. J Biol Chem 276, 20458-20465 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 20458-20465
    • Berton, A.1    Rigot, V.2    Huet, E.3    Decarme, M.4    Eeckhout, Y.5    Patthy, L.6    Godeau, G.7    Hornebeck, W.8    Bellon, G.9    Emonard, H.10
  • 117
    • 1642534351 scopus 로고    scopus 로고
    • Inhibition of plasmin-mediated prostromelysin-1 activation by interaction of long chain unsaturated fatty acids with kringle 5
    • DOI 10.1016/j.bcp.2003.09.033
    • Huet, E., J.H. Cauchard, A. Berton, A. Robinet, M. Decarme and W. Hornebeck: Inhibition of plasminmediated prostromelysin-1 activation by interaction of long chain unsaturated fatty acids with kringle 5. Biochem Pharmacol 67, 643-654 (2004) (Pubitemid 38125249)
    • (2004) Biochemical Pharmacology , vol.67 , Issue.4 , pp. 643-654
    • Huet, E.1    Cauchard, J.-H.2    Berton, A.3    Robinet, A.4    Decarme, M.5    Hornebeck, W.6    Bellon, G.7
  • 118
    • 0027356136 scopus 로고
    • Protective effect of oleoyl peptide conjugates against elastolysis by neutrophil elastase and kappa elastin-induced monocyte chemotaxis
    • Rasoamanantena, P., E. Moczar, L. Robert, S.M. Wei, G. Godeau and W. Hornebeck: Protective effect of oleoyl peptide conjugates against elastolysis by neutrophil elastase and kappa elastin-induced monocyte chemotaxis. Am J Respir Cell Mol Biol 8, 50-55 (1993)
    • (1993) Am J Respir Cell Mol Biol , vol.8 , pp. 50-55
    • Rasoamanantena, P.1    Moczar, E.2    Robert, L.3    Wei, S.M.4    Godeau, G.5    Hornebeck, W.6
  • 119
    • 0025027737 scopus 로고
    • Inhibitors directed to binding domains in neutrophil elastase
    • Tyagi, S.C. and S.R. Simon: Inhibitors directed to binding domains in neutrophil elastase. Biochemistry 29, 9970-9977 (1990) (Pubitemid 20348534)
    • (1990) Biochemistry , vol.29 , Issue.42 , pp. 9970-9977
    • Tyagi, S.C.1    Simon, S.R.2
  • 120
    • 33746637530 scopus 로고    scopus 로고
    • New insights into the inhibition of human neutrophil elastase by heparin
    • DOI 10.1021/bi060338r
    • Spencer, J.L., P.J. Stone and M.A. Nugent: New insights insight into the inhibition of human neutrophil elastase by heparin. Biochemistry 45, 9104-9120 (2006) (Pubitemid 44156373)
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9104-9120
    • Spencer, J.L.1    Stone, P.J.2    Nugent, M.A.3
  • 122
    • 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., C. Diczyazi, A. Neszmelyi, E. Moczar and W. Hornebeck: 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 (1993) (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
  • 123
    • 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., L. Lucatello, A. Naggi, G. Torri and M. Palumbo: Interactions of low-molecular weight semisynthetic sulfated heparins with human leukocyte elastase and human cathepsin G. Biochem Pharmacol 71, 287-293 (2008) (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
  • 124
    • 0034635483 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)
    • DOI 10.1074/jbc.275.6.4183
    • Hu, W-H. and J.F. Woessner Jr: Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7). J Biol Chem 275, 4183-4191 (2000) (Pubitemid 30094653)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.6 , pp. 4183-4191
    • Yu, W.-H.1    Woessner Jr., J.F.2
  • 125
    • 0027133565 scopus 로고
    • Human progelatinase A can be activated by autolysis at a rate that is concentration-dependent and enhanced by heparin bound to the C-terminal domain
    • DOI 10.1111/j.1432-1033.1993.tb18393.x
    • Crabbe, T., C. Ioannou and A.J.P. Docherty: Human proGelatinase A can be activated by autolysis at a rate that is concentration-dependent and enhanced by heparin bound to the C-terminal domain. Eur J Biochem 218, 431-438 (1993) (Pubitemid 24003757)
    • (1993) European Journal of Biochemistry , vol.218 , Issue.2 , pp. 431-438
    • Crabbe, T.1    Ioannou, C.2    Docherty, A.J.P.3
  • 126
    • 70350458704 scopus 로고    scopus 로고
    • Control of promatrilysin (MMP7) activation and substrate-specific activity by sulfated glycosaminoglycans
    • Ra, H.J., S. Harju-Baker, F. Zhang, R.J. Linhardt, C.L. Wilson and W.C. Parks: Control of promatrilysin (MMP7) activation and substrate-specific activity by sulfated glycosaminoglycans. J Biol Chem 284, 27924-27932 (2009)
    • (2009) J Biol Chem , vol.284 , pp. 27924-27932
    • Ra, H.J.1    Harju-Baker, S.2    Zhang, F.3    Linhardt, R.J.4    Wilson, C.L.5    Parks, W.C.6
  • 129
    • 37549071494 scopus 로고    scopus 로고
    • A heparin binding motif on the pro-domain of human procathepsin L mediates zymogen destabilization and activation
    • Fairhead, M., S.M. Kelly and C.F. van der Walls: A heparin binding motif on the pro-domain of human procathepsin L mediates zymogen destabilization and activation. Biochem Biophys Res Commun 366, 862-867 (2007)
    • (2007) Biochem Biophys Res Commun , vol.366 , pp. 862-867
    • Fairhead, M.1    Kelly, S.M.2    Van Der Walls, C.F.3
  • 130
    • 77950468070 scopus 로고    scopus 로고
    • Heparin enhances serpin inhibition of the cysteine protease cathepsin L
    • Higgins, W.J., D.M. Fox, P.S. Kowalski, J.E. Nielsen and D.M. Worrall: Heparin enhances serpin inhibition of the cysteine protease cathepsin L. J Biol Chem 285, 3722-3729 (2010)
    • (2010) J Biol Chem , vol.285 , pp. 3722-3729
    • Higgins, W.J.1    Fox, D.M.2    Kowalski, P.S.3    Nielsen, J.E.4    Worrall, D.M.5
  • 131
    • 84944052122 scopus 로고    scopus 로고
    • 2nd edition. Eds: Barrett A.J., Rawlings N.D. Woessner J.F., Academic Press, London, England.
    • Handbook of Proteolytic Enzymes, 2nd edition. Eds: Barrett A.J., Rawlings N.D. Woessner J.F. Academic Press, London, England. (2004)
    • (2004) Handbook of Proteolytic Enzymes


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