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Volumn 15, Issue 12, 2009, Pages 1295-1308

A fresh prospect of extracellular matrix hydrolytic enzymes and their substrates

Author keywords

Adamalysins; ADAMTS; Cathepsins; Heparanase; Hyaluronidases; Kallikreins; Matrix metalloproteinases; Urokinase type plasminogen activator

Indexed keywords

ADAM PROTEIN; ADAMALYSIN; CATHEPSIN; HEPARANASE; HYALURONIDASE; KALLIKREIN; MATRIPTASE; MATRIX METALLOPROTEINASE; PLASMIN; PROSTATE SPECIFIC ANTIGEN; STRATUM CORNEUM CHYMOTRYPTIC ENZYME; TISSUE PLASMINOGEN ACTIVATOR; UNCLASSIFIED DRUG; UROKINASE; VASCULAR ENDOTHELIAL CADHERIN;

EID: 65649087873     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161209787846676     Document Type: Review
Times cited : (43)

References (203)
  • 1
    • 0031657808 scopus 로고    scopus 로고
    • Matrix proteoglycans: From molecular design to cellular function
    • Iozzo RV. Matrix proteoglycans: from molecular design to cellular function. Annu Rev Biochem 1998; 76: 609-52.
    • (1998) Annu Rev Biochem , vol.76 , pp. 609-652
    • Iozzo, R.V.1
  • 2
    • 0038575443 scopus 로고    scopus 로고
    • Extracellular matrix remodeling: The role of matrix metalloproteinases
    • Stamenkovic I. Extracellular matrix remodeling: the role of matrix metalloproteinases. J Pathol 2003; 200: 448-64.
    • (2003) J Pathol , vol.200 , pp. 448-464
    • Stamenkovic, I.1
  • 3
    • 34447520043 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases
    • Hu J, Van den Steen PE, Sang QX, Opdenakker G. Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases. Nat Rev Drug Discov 2007; 6: 480-98.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 480-498
    • Hu, J.1    Van den Steen, P.E.2    Sang, Q.X.3    Opdenakker, G.4
  • 4
    • 34648815810 scopus 로고    scopus 로고
    • Emerging roles of proteases in tumour suppression
    • López-Otín C, Matrisian LM. Emerging roles of proteases in tumour suppression. Nat Rev Cancer 2007; 7: 800-8.
    • (2007) Nat Rev Cancer , vol.7 , pp. 800-808
    • López-Otín, C.1    Matrisian, L.M.2
  • 5
    • 34547569807 scopus 로고    scopus 로고
    • Multistep pericellular proteolysis controls the transition from individual to collective cancer cell invasion
    • Wolf K, Wu YI, Liu Y, Geiger J, Tam E, Overall C, et al. Multistep pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nat Cell Biol 2007; 9: 893-904.
    • (2007) Nat Cell Biol , vol.9 , pp. 893-904
    • Wolf, K.1    Wu, Y.I.2    Liu, Y.3    Geiger, J.4    Tam, E.5    Overall, C.6
  • 8
    • 53449084679 scopus 로고    scopus 로고
    • Matrix metalloproteinases in venous tissue remodeling and varicose vein formation
    • Raffetto JD, Khalil RA. Matrix metalloproteinases in venous tissue remodeling and varicose vein formation. Curr Vasc Pharmacol 2008; 6: 158-72.
    • (2008) Curr Vasc Pharmacol , vol.6 , pp. 158-172
    • Raffetto, J.D.1    Khalil, R.A.2
  • 9
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • Rawlings ND, Barrett AJ. Evolutionary families of metallopeptidases. Methods Enzymol 1995; 248: 183-228.
    • (1995) Methods Enzymol , vol.248 , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 10
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H, Woesner JF. Matrix metalloproteinases. J Biol Chem 1999; 274: 21491-4.
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woesner, J.F.2
  • 11
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart HE, Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci USA 1990; 87: 5578-82.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 12
    • 4444304939 scopus 로고    scopus 로고
    • Regulation of matrix biology by matrix metalloproteinases
    • Mott JD, Werb Z. Regulation of matrix biology by matrix metalloproteinases. Curr Opin Cell Biol 2004; 16: 558-64.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 558-564
    • Mott, J.D.1    Werb, Z.2
  • 13
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw A, Ewald AJ, Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol 2007; 8: 221-33.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 14
    • 33846821908 scopus 로고    scopus 로고
    • Proteomic discovery of protease substrates
    • Schilling O, Overall CM. Proteomic discovery of protease substrates. Curr Opin Chem Biol 2007; 11: 36-45.
    • (2007) Curr Opin Chem Biol , vol.11 , pp. 36-45
    • Schilling, O.1    Overall, C.M.2
  • 15
    • 0035464206 scopus 로고    scopus 로고
    • Adipocyte produces matrix metalloproteinases 2 and 9: Involvement in adipose differentiation
    • Bouloumié A, Sengenès C, Portolan G, Galitzky J, Lafontan M. Adipocyte produces matrix metalloproteinases 2 and 9: involvement in adipose differentiation. Diabetes 2001; 50: 2080-6.
    • (2001) Diabetes , vol.50 , pp. 2080-2086
    • Bouloumié, A.1    Sengenès, C.2    Portolan, G.3    Galitzky, J.4    Lafontan, M.5
  • 16
    • 0038823617 scopus 로고    scopus 로고
    • Matrix metalloproteinases are differentially expressed in adipose tissue during obesity and modulate adipocyte differentiation
    • Chavey C, Mari B, Monthouel MN, Bonnafous S, Anglard P, Van Obberghen E et al. Matrix metalloproteinases are differentially expressed in adipose tissue during obesity and modulate adipocyte differentiation. J Biol Chem 2003; 278: 11888-96.
    • (2003) J Biol Chem , vol.278 , pp. 11888-11896
    • Chavey, C.1    Mari, B.2    Monthouel, M.N.3    Bonnafous, S.4    Anglard, P.5    Van Obberghen, E.6
  • 18
    • 33845897434 scopus 로고    scopus 로고
    • Inhibition of human preadipocytes proteasomal activity by HIV protease inhibitors or specific inhibitor lactacystin leads to a defect in adipogenesis, which involves matrix metalloproteinase-9
    • De Barros S, Zakaroff-Girard A, Lafontan M, Galitzky J, Bourlier V. Inhibition of human preadipocytes proteasomal activity by HIV protease inhibitors or specific inhibitor lactacystin leads to a defect in adipogenesis, which involves matrix metalloproteinase-9. J Pharmacol Exp Ther 2007; 320: 291-9.
    • (2007) J Pharmacol Exp Ther , vol.320 , pp. 291-299
    • De Barros, S.1    Zakaroff-Girard, A.2    Lafontan, M.3    Galitzky, J.4    Bourlier, V.5
  • 19
    • 45749117243 scopus 로고    scopus 로고
    • A functional role of gelatinase A in the development of nutritionarlly induced obesity in mice
    • Van Hul M, Lijnen HR. A functional role of gelatinase A in the development of nutritionarlly induced obesity in mice. J Thromb Haemost 2008; 6: 1198-206.
    • (2008) J Thromb Haemost , vol.6 , pp. 1198-1206
    • Van Hul, M.1    Lijnen, H.R.2
  • 20
    • 0030834283 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNF alpha and Notch
    • Blobel CP. Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNF alpha and Notch. Cell 1997; 90: 589-92.
    • (1997) Cell , vol.90 , pp. 589-592
    • Blobel, C.P.1
  • 21
    • 0032571315 scopus 로고    scopus 로고
    • Specific interaction of the recombinant disintegrin-like domain MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3
    • Zhang XP, Kamata T, Yokoyama K, Puzon-McLaughlin W, Takada Y. Specific interaction of the recombinant disintegrin-like domain MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3. J Biol Chem 1998; 273: 7345-50.
    • (1998) J Biol Chem , vol.273 , pp. 7345-7350
    • Zhang, X.P.1    Kamata, T.2    Yokoyama, K.3    Puzon-McLaughlin, W.4    Takada, Y.5
  • 22
    • 0037124066 scopus 로고    scopus 로고
    • Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta1: Implications for sperm-egg binding and other cell interactions
    • Eto K, Huet C, Tarui T, Kupriyanov S, Liu HZ, Puzon-McLaughlin W et al. Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta1: implications for sperm-egg binding and other cell interactions. J Biol Chem 2002; 277: 17804-10.
    • (2002) J Biol Chem , vol.277 , pp. 17804-17810
    • Eto, K.1    Huet, C.2    Tarui, T.3    Kupriyanov, S.4    Liu, H.Z.5    Puzon-McLaughlin, W.6
  • 23
    • 0030951614 scopus 로고    scopus 로고
    • A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion
    • Yuan R, Primakoff P, Myles DG. A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion. J Cell Biol 1997; 137: 105-12.
    • (1997) J Cell Biol , vol.137 , pp. 105-112
    • Yuan, R.1    Primakoff, P.2    Myles, D.G.3
  • 24
    • 23744452775 scopus 로고    scopus 로고
    • A disintegrin and metalloprotease 21 (ADAM21) is associated with neurogenesis and axonal growth in developing and adult rodent CNS
    • Yang P, Baker KA, Hagg T. A disintegrin and metalloprotease 21 (ADAM21) is associated with neurogenesis and axonal growth in developing and adult rodent CNS. J Comp Neurol 2005; 490: 163-79.
    • (2005) J Comp Neurol , vol.490 , pp. 163-179
    • Yang, P.1    Baker, K.A.2    Hagg, T.3
  • 25
    • 31344453693 scopus 로고    scopus 로고
    • Integrins, membrane-type matrix metalloproteinases and ADAMs: Potential implications for cardiac remodeling
    • Manso AM, Elsherif L, Kang SM, Ross RS. Integrins, membrane-type matrix metalloproteinases and ADAMs: potential implications for cardiac remodeling. Cardiovasc Res 2006; 69: 574-84.
    • (2006) Cardiovasc Res , vol.69 , pp. 574-584
    • Manso, A.M.1    Elsherif, L.2    Kang, S.M.3    Ross, R.S.4
  • 28
    • 21644449866 scopus 로고    scopus 로고
    • ADAMTS proteinases: A multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis
    • Jones GC, Riley GP. ADAMTS proteinases: a multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis. Arthritis Res Ther 2005; 7: 160-9.
    • (2005) Arthritis Res Ther , vol.7 , pp. 160-169
    • Jones, G.C.1    Riley, G.P.2
  • 30
    • 33745731954 scopus 로고    scopus 로고
    • Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold
    • Takeda S, Igarashi T, Mori H, Araki S. Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold. EMBO J 2006; 25: 2388-96.
    • (2006) EMBO J , vol.25 , pp. 2388-2396
    • Takeda, S.1    Igarashi, T.2    Mori, H.3    Araki, S.4
  • 31
    • 0037160539 scopus 로고    scopus 로고
    • Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrain and thrombospondin-1 domains
    • Cal S, Obaya AJ, Llamazares M, Garabaya C, Quesada V, López-Otín C. Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrain and thrombospondin-1 domains. Gene 2002; 283: 49-62.
    • (2002) Gene , vol.283 , pp. 49-62
    • Cal, S.1    Obaya, A.J.2    Llamazares, M.3    Garabaya, C.4    Quesada, V.5    López-Otín, C.6
  • 32
    • 4143112912 scopus 로고    scopus 로고
    • A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: The ADAMTS family
    • Apte SS. A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family. Int J Biochem Cell Biol 2004; 36: 981-5.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 981-985
    • Apte, S.S.1
  • 34
    • 0032577568 scopus 로고    scopus 로고
    • ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region
    • Kuno K, Matsushima K. ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region. J Biol Chem 1998; 273: 13912-7.
    • (1998) J Biol Chem , vol.273 , pp. 13912-13917
    • Kuno, K.1    Matsushima, K.2
  • 35
    • 0032978988 scopus 로고    scopus 로고
    • ADAMTS: A novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats
    • Tang BL, Hong W. ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats. FEBS Lett 1999; 445: 223-5.
    • (1999) FEBS Lett , vol.445 , pp. 223-225
    • Tang, B.L.1    Hong, W.2
  • 36
    • 0033551844 scopus 로고    scopus 로고
    • Cloning and characterization of ADAMTS11, an aggregcanase from the ADAMTS family
    • Abbaszade I, Liu RQ, Yang F, Rosenfeld SA, Ross OH, Link JR et al. Cloning and characterization of ADAMTS11, an aggregcanase from the ADAMTS family. J Biol Chem 1999; 274: 23443-50.
    • (1999) J Biol Chem , vol.274 , pp. 23443-23450
    • Abbaszade, I.1    Liu, R.Q.2    Yang, F.3    Rosenfeld, S.A.4    Ross, O.H.5    Link, J.R.6
  • 37
    • 0033520318 scopus 로고    scopus 로고
    • ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family
    • Hurskainen TL, Hirohata S, Seldin MF, Apte SS. ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family. J Biol Chem 1999; 274: 25555-63.
    • (1999) J Biol Chem , vol.274 , pp. 25555-25563
    • Hurskainen, T.L.1    Hirohata, S.2    Seldin, M.F.3    Apte, S.S.4
  • 38
    • 0035947652 scopus 로고    scopus 로고
    • Identification, characterization, and intracellular processing of ADAM-TS12, a novel human disintegrin with a complex structural organization involving multiple thrombospondin-1 repeats
    • Cal S, Arguelles JM, Fernandez PL, López-Otín C. Identification, characterization, and intracellular processing of ADAM-TS12, a novel human disintegrin with a complex structural organization involving multiple thrombospondin-1 repeats. J Biol Chem 2001; 276: 17932-40.
    • (2001) J Biol Chem , vol.276 , pp. 17932-17940
    • Cal, S.1    Arguelles, J.M.2    Fernandez, P.L.3    López-Otín, C.4
  • 39
    • 0035798582 scopus 로고    scopus 로고
    • Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura
    • Zheng X, Chung D, Takayama TK, Majerus EM, Sadler JE, Fujikawa K. Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura. J Biol Chem 2001; 276: 41059-63.
    • (2001) J Biol Chem , vol.276 , pp. 41059-41063
    • Zheng, X.1    Chung, D.2    Takayama, T.K.3    Majerus, E.M.4    Sadler, J.E.5    Fujikawa, K.6
  • 40
    • 0033542457 scopus 로고    scopus 로고
    • Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans
    • Blelloch R, Kimble J. Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans. Nature 1999; 399: 586-90.
    • (1999) Nature , vol.399 , pp. 586-590
    • Blelloch, R.1    Kimble, J.2
  • 43
    • 40749104234 scopus 로고    scopus 로고
    • The regulation of the ADAMTS4 and ADAMTS5 aggrecanases in osteoarthritis: A review
    • Bondeson J, Wainwright S, Hughes C, Caterson B. The regulation of the ADAMTS4 and ADAMTS5 aggrecanases in osteoarthritis: a review. Clin Exp Rheumatol 2008; 26: 139-45.
    • (2008) Clin Exp Rheumatol , vol.26 , pp. 139-145
    • Bondeson, J.1    Wainwright, S.2    Hughes, C.3    Caterson, B.4
  • 44
    • 0942266125 scopus 로고    scopus 로고
    • Soeki T, Tamura Y, Shinohara H, Sakabe K, Onose Y, Fukuda N. Elevated concentration of soluble vascular endothelial cadherin is associated with coronary atherosclerosis. Cir J 2004; 68: 1-5.
    • Soeki T, Tamura Y, Shinohara H, Sakabe K, Onose Y, Fukuda N. Elevated concentration of soluble vascular endothelial cadherin is associated with coronary atherosclerosis. Cir J 2004; 68: 1-5.
  • 45
    • 45149117638 scopus 로고    scopus 로고
    • ADAM10 regulates endothelial permeability and T-Cell transmigration by proteolysis of vascular endothelial cadherin
    • Schulz B, Pruessmeyer J, Maretzky T, Ludwig A, Blobel CP, Saftig P et al. ADAM10 regulates endothelial permeability and T-Cell transmigration by proteolysis of vascular endothelial cadherin. Circ Res 2008; 102: 1192-201.
    • (2008) Circ Res , vol.102 , pp. 1192-1201
    • Schulz, B.1    Pruessmeyer, J.2    Maretzky, T.3    Ludwig, A.4    Blobel, C.P.5    Saftig, P.6
  • 46
    • 0038650592 scopus 로고    scopus 로고
    • Increased expression of disintegrin-metalloproteinases ADAM-15 and ADAM-9 following upregulation of integrins alpha5beta1 and alphavbeta3 in atherosclerosis
    • Al-Fakhri N, Wilhelm J, Hahn M, Heidt M, Hehrlein FW, Endisch AM et al. Increased expression of disintegrin-metalloproteinases ADAM-15 and ADAM-9 following upregulation of integrins alpha5beta1 and alphavbeta3 in atherosclerosis. J Cell Biochem 2003; 89: 808-23.
    • (2003) J Cell Biochem , vol.89 , pp. 808-823
    • Al-Fakhri, N.1    Wilhelm, J.2    Hahn, M.3    Heidt, M.4    Hehrlein, F.W.5    Endisch, A.M.6
  • 47
    • 33744797970 scopus 로고    scopus 로고
    • The TNF alpha converting enzyme (TACE/ADAM17) is expressed in the atherosclerotic lesions of apolipoprotein E-deficient mice: Possible contribution to elevated plasma levels of soluble TNF alpha receptors
    • Canault M, Peiretti F, Kopp F, Bonardo B, Bonzi MR, Coudeyre JC et al. The TNF alpha converting enzyme (TACE/ADAM17) is expressed in the atherosclerotic lesions of apolipoprotein E-deficient mice: possible contribution to elevated plasma levels of soluble TNF alpha receptors. Atherosclerosis 2006; 187: 82-91.
    • (2006) Atherosclerosis , vol.187 , pp. 82-91
    • Canault, M.1    Peiretti, F.2    Kopp, F.3    Bonardo, B.4    Bonzi, M.R.5    Coudeyre, J.C.6
  • 48
    • 36349026433 scopus 로고    scopus 로고
    • Microparticles of human atherosclerotic plaques enhance the shedding of the tumor necrosis factor-alpha converting enzyme/ADAM17 substrates, tumor necrosis factor and tumor necrosis factor receptor-1
    • Canault M, Leroyer AS, Peiretti F, Lesèche G, Tedgui A, Bonardo B et al. Microparticles of human atherosclerotic plaques enhance the shedding of the tumor necrosis factor-alpha converting enzyme/ADAM17 substrates, tumor necrosis factor and tumor necrosis factor receptor-1. Am J Pathol 2007; 171: 1713-23.
    • (2007) Am J Pathol , vol.171 , pp. 1713-1723
    • Canault, M.1    Leroyer, A.S.2    Peiretti, F.3    Lesèche, G.4    Tedgui, A.5    Bonardo, B.6
  • 49
    • 40449132187 scopus 로고    scopus 로고
    • ADAM-15: A metalloproteinase that mediates inflammation
    • Charrier-Hisamuddin L, Laboisse CL, Merlin D. ADAM-15: a metalloproteinase that mediates inflammation. FASEB J 2008; 22: 641-53.
    • (2008) FASEB J , vol.22 , pp. 641-653
    • Charrier-Hisamuddin, L.1    Laboisse, C.L.2    Merlin, D.3
  • 50
    • 38349140386 scopus 로고    scopus 로고
    • ADAMTS-4 and -8 are inflammatory regulated enzymes expressed in macrophage-rich areas of human atherosclerotic plaques
    • Wågsäter D, Björk H, Zhu C, Björkegren J, Valen G, Hamsten A et al. ADAMTS-4 and -8 are inflammatory regulated enzymes expressed in macrophage-rich areas of human atherosclerotic plaques. Atherosclerosis 2008; 196: 514-22.
    • (2008) Atherosclerosis , vol.196 , pp. 514-522
    • Wågsäter, D.1    Björk, H.2    Zhu, C.3    Björkegren, J.4    Valen, G.5    Hamsten, A.6
  • 51
    • 40549091250 scopus 로고    scopus 로고
    • ADAM-12 (meltrin alpha) is involved in chondrocyte proliferation via cleavage of insulin-like growth factor binding protein 5 in osteoarthritic cartilage
    • Okada A, Mochizuki S, Yatabe T, Kimura T, Shiomi T, Fujita Y et al. ADAM-12 (meltrin alpha) is involved in chondrocyte proliferation via cleavage of insulin-like growth factor binding protein 5 in osteoarthritic cartilage. Arthritis Rheum 2008; 58: 778-89.
    • (2008) Arthritis Rheum , vol.58 , pp. 778-789
    • Okada, A.1    Mochizuki, S.2    Yatabe, T.3    Kimura, T.4    Shiomi, T.5    Fujita, Y.6
  • 52
    • 39449131916 scopus 로고    scopus 로고
    • Will the real aggrecanase(s) step up: Evaluating the criteria that define aggrecanase activity in osteoarthritis
    • Tortorella MD, Malfait AM. Will the real aggrecanase(s) step up: evaluating the criteria that define aggrecanase activity in osteoarthritis. Curr Pharm Biotechnol 2008; 9: 16-23.
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 16-23
    • Tortorella, M.D.1    Malfait, A.M.2
  • 55
    • 0029067409 scopus 로고
    • Characterization and partial amino acid sequencing of a 107-kDa procollagen I N-proteinase purified by affinity chromatography on immobilized type XIV collagen
    • Colige A, Beschin A, Samyn B, Goebels Y, Van Beeumen J, Nusgens BV et al. Characterization and partial amino acid sequencing of a 107-kDa procollagen I N-proteinase purified by affinity chromatography on immobilized type XIV collagen. J Biol Chem 1995; 270: 16724-30.
    • (1995) J Biol Chem , vol.270 , pp. 16724-16730
    • Colige, A.1    Beschin, A.2    Samyn, B.3    Goebels, Y.4    Van Beeumen, J.5    Nusgens, B.V.6
  • 56
    • 0030959540 scopus 로고    scopus 로고
    • cDNA cloning and expression of bovine procollagen I N-proteinase: A new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components
    • Colige A, Li SW, Sieron AL, Nusgens BV, Prockop DJ, Lapiere CM. cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components. Proc Natl Acad Sci USA 1997; 94: 2374-9.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2374-2379
    • Colige, A.1    Li, S.W.2    Sieron, A.L.3    Nusgens, B.V.4    Prockop, D.J.5    Lapiere, C.M.6
  • 57
    • 0037805608 scopus 로고    scopus 로고
    • Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase
    • Wang WM, Lee S, Steiglitz BM, Scott IC, Lebares CC, Allen ML et al. Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase. J Biol Chem 2003; 278: 19549-57.
    • (2003) J Biol Chem , vol.278 , pp. 19549-19557
    • Wang, W.M.1    Lee, S.2    Steiglitz, B.M.3    Scott, I.C.4    Lebares, C.C.5    Allen, M.L.6
  • 58
    • 0035943639 scopus 로고    scopus 로고
    • Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis
    • Fernandes RJ, Hirohata S, Engle JM, Colige A, Cohn DH, Eyre DR et al. Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis. J Biol Chem 2001; 276: 31502-9.
    • (2001) J Biol Chem , vol.276 , pp. 31502-31509
    • Fernandes, R.J.1    Hirohata, S.2    Engle, J.M.3    Colige, A.4    Cohn, D.H.5    Eyre, D.R.6
  • 60
    • 0034840936 scopus 로고    scopus 로고
    • The role of ADAM-TS4 (aggrecanase-1) and ADAMTS-5 (aggrecanse-2) in a model of cartilage degradation
    • Tortorella MD, Malfait AM, Deccico C, Arner E. The role of ADAM-TS4 (aggrecanase-1) and ADAMTS-5 (aggrecanse-2) in a model of cartilage degradation. Osteoarthritis Cartilage 2001; 9: 539-52.
    • (2001) Osteoarthritis Cartilage , vol.9 , pp. 539-552
    • Tortorella, M.D.1    Malfait, A.M.2    Deccico, C.3    Arner, E.4
  • 61
    • 33845702259 scopus 로고    scopus 로고
    • ADAMTS-7: A metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein
    • Liu CJ, Kong W, Ilalov K, Yu S, Xu K, Prazak L et al. ADAMTS-7: a metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein. FASEB J 2006; 20: 988-90.
    • (2006) FASEB J , vol.20 , pp. 988-990
    • Liu, C.J.1    Kong, W.2    Ilalov, K.3    Yu, S.4    Xu, K.5    Prazak, L.6
  • 63
    • 0038237345 scopus 로고    scopus 로고
    • Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1
    • Somerville RP, Longpre JM, Jungers KA, Engle JM, Ross M, Evanko S et al. Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1. J Biol Chem 2003; 278: 9503-13.
    • (2003) J Biol Chem , vol.278 , pp. 9503-9513
    • Somerville, R.P.1    Longpre, J.M.2    Jungers, K.A.3    Engle, J.M.4    Ross, M.5    Evanko, S.6
  • 64
    • 10944243756 scopus 로고    scopus 로고
    • Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation
    • Somerville RP, Jungers KA, Apte SS. Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation. J Biol Chem 2004; 279: 51208-17.
    • (2004) J Biol Chem , vol.279 , pp. 51208-51217
    • Somerville, R.P.1    Jungers, K.A.2    Apte, S.S.3
  • 65
    • 33744909868 scopus 로고    scopus 로고
    • ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein
    • Liu CJ, Kong W, Xu K, Luan Y, Ilalov K, Sehgal B et al. ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. J Biol Chem 2006; 281: 15800-8.
    • (2006) J Biol Chem , vol.281 , pp. 15800-15808
    • Liu, C.J.1    Kong, W.2    Xu, K.3    Luan, Y.4    Ilalov, K.5    Sehgal, B.6
  • 66
    • 0035885972 scopus 로고    scopus 로고
    • Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family
    • Fujikawa K, Suzuki H, McMullen B, Chung D. Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family. Blood 2001; 98: 1662-6.
    • (2001) Blood , vol.98 , pp. 1662-1666
    • Fujikawa, K.1    Suzuki, H.2    McMullen, B.3    Chung, D.4
  • 67
    • 0037155146 scopus 로고    scopus 로고
    • Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3
    • Colige A, Vandenberghe I, Thiry M, Lambert CA, Van Beeumen J, Li SW et al. Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3. J Biol Chem 2002; 277: 5756-66.
    • (2002) J Biol Chem , vol.277 , pp. 5756-5766
    • Colige, A.1    Vandenberghe, I.2    Thiry, M.3    Lambert, C.A.4    Van Beeumen, J.5    Li, S.W.6
  • 68
    • 65649118017 scopus 로고    scopus 로고
    • Yamaji N, Nishimura K, Abe K, Ohara O, Nagase T, Nomura N. Novel metalloprotease having aggrecanase activity. In Pat, Yamanouchi Pharmeutical Co. Ltd, Japan 2001.
    • Yamaji N, Nishimura K, Abe K, Ohara O, Nagase T, Nomura N. Novel metalloprotease having aggrecanase activity. In Pat, Yamanouchi Pharmeutical Co. Ltd, Japan 2001.
  • 69
    • 0038644928 scopus 로고    scopus 로고
    • Identification and characterization of ADAMTS-20 defines a novel subfamily of metalloproteinases- disintegrins with multiple thrombospondin-1 repeats and a unique GON domain
    • Llamazares M, Cal S, Quesada V, López-Otín C. Identification and characterization of ADAMTS-20 defines a novel subfamily of metalloproteinases- disintegrins with multiple thrombospondin-1 repeats and a unique GON domain. J Biol Chem 2003; 278: 13382-9.
    • (2003) J Biol Chem , vol.278 , pp. 13382-13389
    • Llamazares, M.1    Cal, S.2    Quesada, V.3    López-Otín, C.4
  • 70
    • 33847010576 scopus 로고    scopus 로고
    • Aggrecan degradation in human articular cartilage explants is mediated by both ADAMTS-4 and ADAMTS-5
    • Song RH, Tortorella MD, Malfait AM, Alston JT, Yang Z, Arner EC et al. Aggrecan degradation in human articular cartilage explants is mediated by both ADAMTS-4 and ADAMTS-5. Arthritis Rheum 2007; 56: 575-85.
    • (2007) Arthritis Rheum , vol.56 , pp. 575-585
    • Song, R.H.1    Tortorella, M.D.2    Malfait, A.M.3    Alston, J.T.4    Yang, Z.5    Arner, E.C.6
  • 71
  • 72
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MCH class II-associated invariant chain processing and peptide loading
    • Riese RJ, Wolf PR, Brömme D, Natkin LR, Villadangos JA, Ploegh HL et al. Essential role for cathepsin S in MCH class II-associated invariant chain processing and peptide loading. Immunity 1996; 4: 357-66.
    • (1996) Immunity , vol.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.R.2    Brömme, D.3    Natkin, L.R.4    Villadangos, J.A.5    Ploegh, H.L.6
  • 73
    • 0027272006 scopus 로고
    • The lysosomal system in neuronal cell death: A review
    • Nixon RA, Cataldo AM. The lysosomal system in neuronal cell death: a review. Ann N Y Acad Sci 1993; 679: 87-109.
    • (1993) Ann N Y Acad Sci , vol.679 , pp. 87-109
    • Nixon, R.A.1    Cataldo, A.M.2
  • 75
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • Turk B, Turk V, Turk D. Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol Chem 1997; 378: 141-150.
    • (1997) Biol Chem , vol.378 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 76
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: More than scavengers
    • Turk B, Turk D, Turk V. Lysosomal cysteine proteases: more than scavengers. Biochim Biophys Acta 2000; 1477: 98-111.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 77
    • 18544398901 scopus 로고    scopus 로고
    • A classical enzyme active center motif lacks catalytic competence until modulated electrostatically
    • Pinitglang S, Watts AB, Patel M, Reid JD, Noble MA, Gul S et al. A classical enzyme active center motif lacks catalytic competence until modulated electrostatically. Biochemistry 1997; 36: 9968-82.
    • (1997) Biochemistry , vol.36 , pp. 9968-9982
    • Pinitglang, S.1    Watts, A.B.2    Patel, M.3    Reid, J.D.4    Noble, M.A.5    Gul, S.6
  • 78
    • 0028309017 scopus 로고
    • The proregion of cathepsin L is required for proper folding, stability, and ER exit
    • Tao K, Stearns NA, Dong J, Wu QL, Sahagian GG. The proregion of cathepsin L is required for proper folding, stability, and ER exit. Arch Biochem Biophys 1994; 311: 19-27.
    • (1994) Arch Biochem Biophys , vol.311 , pp. 19-27
    • Tao, K.1    Stearns, N.A.2    Dong, J.3    Wu, Q.L.4    Sahagian, G.G.5
  • 79
    • 0024284209 scopus 로고
    • Biosyntheses and processing of lysosomal cysteine proteinases in rat macrophages
    • Kominami E, Tsukahara T, Hara K, Katunuma N. Biosyntheses and processing of lysosomal cysteine proteinases in rat macrophages. FEBS Lett 1988; 231: 225-8.
    • (1988) FEBS Lett , vol.231 , pp. 225-228
    • Kominami, E.1    Tsukahara, T.2    Hara, K.3    Katunuma, N.4
  • 80
    • 0023905240 scopus 로고
    • Identification of latent procathespins B and L in microsomal lumen: Characterization of enzymatic activation and proteolytic processing in vitro
    • Nishimura Y, Kawabata T, Kato K. Identification of latent procathespins B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro. Arch Biochem Biophys 1988; 261: 64-71.
    • (1988) Arch Biochem Biophys , vol.261 , pp. 64-71
    • Nishimura, Y.1    Kawabata, T.2    Kato, K.3
  • 81
    • 0026664252 scopus 로고    scopus 로고
    • Rowan AD, Mason P, Mach L, Mort JS. Rat procathepsin B. Proteolytic processing to the mature form in vitro. J Biol Chem 1992; 267: 15993-9.
    • Rowan AD, Mason P, Mach L, Mort JS. Rat procathepsin B. Proteolytic processing to the mature form in vitro. J Biol Chem 1992; 267: 15993-9.
  • 82
    • 33646513917 scopus 로고    scopus 로고
    • Cysteine cathepsins in the immune response
    • Zavašnik-Bergant T, Turk B. Cysteine cathepsins in the immune response. Tissue Antigens 2006; 67: 349-55.
    • (2006) Tissue Antigens , vol.67 , pp. 349-355
    • Zavašnik-Bergant, T.1    Turk, B.2
  • 83
    • 0025871926 scopus 로고
    • Multiple proteolytic action of rat liver cathepsin B: Specificities and pH-dependences of the endo- and exopeptidases activities
    • Koga H, Yamada H, Nishimura Y, Kato K, Imoto T. Multiple proteolytic action of rat liver cathepsin B: specificities and pH-dependences of the endo- and exopeptidases activities. J Biochem 1991; 110: 179-88.
    • (1991) J Biochem , vol.110 , pp. 179-188
    • Koga, H.1    Yamada, H.2    Nishimura, Y.3    Kato, K.4    Imoto, T.5
  • 84
    • 0032518496 scopus 로고    scopus 로고
    • Crystal structure of porcine cathepsin H determined at 2.1 A resolution: Location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function
    • Guncar G, Podobnik M, Pungercar J, Strukelj B, Turk V, Turk D. Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function. Structure 1998; 6: 51-61.
    • (1998) Structure , vol.6 , pp. 51-61
    • Guncar, G.1    Podobnik, M.2    Pungercar, J.3    Strukelj, B.4    Turk, V.5    Turk, D.6
  • 85
  • 86
    • 0032080113 scopus 로고    scopus 로고
    • Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix
    • Kafienah W, Brömme D, Buttle DJ, Croucher LJ, Hollander AP. Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix. Biochem J 1998; 331: 727-32.
    • (1998) Biochem J , vol.331 , pp. 727-732
    • Kafienah, W.1    Brömme, D.2    Buttle, D.J.3    Croucher, L.J.4    Hollander, A.P.5
  • 87
    • 0030026637 scopus 로고    scopus 로고
    • Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme
    • Brömme D, Okamoto K, Wang BB, Biroc S. Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme. J Biol Chem 1996; 271: 2126-32.
    • (1996) J Biol Chem , vol.271 , pp. 2126-2132
    • Brömme, D.1    Okamoto, K.2    Wang, B.B.3    Biroc, S.4
  • 88
    • 15844422855 scopus 로고    scopus 로고
    • Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts
    • Drake FH, Dodds RA, James IE, Connor JR, Debouck C, Richardson S et al. Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts. J Biol Chem 1996; 271: 12511-6.
    • (1996) J Biol Chem , vol.271 , pp. 12511-12516
    • Drake, F.H.1    Dodds, R.A.2    James, I.E.3    Connor, J.R.4    Debouck, C.5    Richardson, S.6
  • 89
    • 0029809357 scopus 로고    scopus 로고
    • Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency
    • Gelb BD, Shi GP, Chapman HA, Desnick RJ. Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency. Science 1996; 273: 1236-8.
    • (1996) Science , vol.273 , pp. 1236-1238
    • Gelb, B.D.1    Shi, G.P.2    Chapman, H.A.3    Desnick, R.J.4
  • 90
    • 0036226928 scopus 로고    scopus 로고
    • Acidic cysteine endoproteinase cathepsin K in the degeneration of the superficial articular hyaline cartilage in osteoarthritis
    • Konttinen YT, Mandelin J, Li TF, Salo J, Lassus J, Liljeström M et al. Acidic cysteine endoproteinase cathepsin K in the degeneration of the superficial articular hyaline cartilage in osteoarthritis. Arthritis Rhemu 2002; 46: 953-60.
    • (2002) Arthritis Rhemu , vol.46 , pp. 953-960
    • Konttinen, Y.T.1    Mandelin, J.2    Li, T.F.3    Salo, J.4    Lassus, J.5    Liljeström, M.6
  • 91
    • 2442699167 scopus 로고    scopus 로고
    • Up regulation of cathepsin K expression in articular chondrocytes in a transgenic mouse model for osteoarthritis
    • Morko JP, Söderström M, Säämänen AM, Salminen HJ, Vuorio EI. Up regulation of cathepsin K expression in articular chondrocytes in a transgenic mouse model for osteoarthritis. Ann Rheum Dis 2004; 63: 649-55.
    • (2004) Ann Rheum Dis , vol.63 , pp. 649-655
    • Morko, J.P.1    Söderström, M.2    Säämänen, A.M.3    Salminen, H.J.4    Vuorio, E.I.5
  • 92
    • 0032145836 scopus 로고    scopus 로고
    • Expression of elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells
    • Sukhova GK, Shi GP, Simon DI, Chapman HA, Libby P. Expression of elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells. J Clin Invest 1998; 102: 576-83.
    • (1998) J Clin Invest , vol.102 , pp. 576-583
    • Sukhova, G.K.1    Shi, G.P.2    Simon, D.I.3    Chapman, H.A.4    Libby, P.5
  • 93
    • 4544245056 scopus 로고    scopus 로고
    • Cysteine protease cathepsin F is expressed in human atherosclerotic lesions, is secreted by cultured macrophages, and modifies low density lipoprotein particles in vitro
    • Oörni K, Sneck M, Brömme D, Pentikäinen MO, Lindstedt KA, Mäyränpää M et al. Cysteine protease cathepsin F is expressed in human atherosclerotic lesions, is secreted by cultured macrophages, and modifies low density lipoprotein particles in vitro. J Biol Chem 2004; 279: 34776-84.
    • (2004) J Biol Chem , vol.279 , pp. 34776-34784
    • Oörni, K.1    Sneck, M.2    Brömme, D.3    Pentikäinen, M.O.4    Lindstedt, K.A.5    Mäyränpää, M.6
  • 94
    • 30044445997 scopus 로고    scopus 로고
    • Cathepsin L expression and regulation in human abdominal aortic aneurysm, atherosclerosis, and vascular cells
    • Liu J, Sukhova GK, Yang JT, Sun J, Ma L, Ren A et al. Cathepsin L expression and regulation in human abdominal aortic aneurysm, atherosclerosis, and vascular cells. Atherosclerosis 2006; 184: 302-11.
    • (2006) Atherosclerosis , vol.184 , pp. 302-311
    • Liu, J.1    Sukhova, G.K.2    Yang, J.T.3    Sun, J.4    Ma, L.5    Ren, A.6
  • 95
    • 4344670363 scopus 로고    scopus 로고
    • Yasuda Y, Li Z, Greenbaum D, Bogyo M, Weber E, Brömme D. Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. J Biol Chem 2004; 279: 36761-70.
    • Yasuda Y, Li Z, Greenbaum D, Bogyo M, Weber E, Brömme D. Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. J Biol Chem 2004; 279: 36761-70.
  • 96
    • 0037362831 scopus 로고    scopus 로고
    • Deficiency of cathepsin S reduces atherosclerosis in LDL receptor-deficient mice
    • Sukhova GK, Zhang Y, Pan JH, Wada Y, Yamamoto T, Naito M et al. Deficiency of cathepsin S reduces atherosclerosis in LDL receptor-deficient mice. J Clin Invest 2003; 111: 897-906.
    • (2003) J Clin Invest , vol.111 , pp. 897-906
    • Sukhova, G.K.1    Zhang, Y.2    Pan, J.H.3    Wada, Y.4    Yamamoto, T.5    Naito, M.6
  • 98
    • 33644865170 scopus 로고    scopus 로고
    • Disruption of the cathepsin K gene reduces atherosclerosis progression and induces plaque fibrosis but accelerates macrophage foam cell formation
    • Lutgens E, Lutgens SP, Faber BC, Heeneman S, Gijbels MM, de Winther MP et al. Disruption of the cathepsin K gene reduces atherosclerosis progression and induces plaque fibrosis but accelerates macrophage foam cell formation. Circulation 2006; 113: 98-107.
    • (2006) Circulation , vol.113 , pp. 98-107
    • Lutgens, E.1    Lutgens, S.P.2    Faber, B.C.3    Heeneman, S.4    Gijbels, M.M.5    de Winther, M.P.6
  • 99
    • 0033802292 scopus 로고    scopus 로고
    • Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-deficient human macrophages
    • Punturieri A, Filippov S, Allen E, Caras I, Murray R, Reddy V et al. Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-deficient human macrophages. J Exp Med 2000; 192: 789-99.
    • (2000) J Exp Med , vol.192 , pp. 789-799
    • Punturieri, A.1    Filippov, S.2    Allen, E.3    Caras, I.4    Murray, R.5    Reddy, V.6
  • 100
    • 0032790807 scopus 로고    scopus 로고
    • Distribution, activity and concentration of cathepsin B and cystatin C in the wall of aortic aneurysm
    • Gacko M, Chyczewski L, Chrostek L. Distribution, activity and concentration of cathepsin B and cystatin C in the wall of aortic aneurysm. Pol J Pathol 1999; 50: 83-6.
    • (1999) Pol J Pathol , vol.50 , pp. 83-86
    • Gacko, M.1    Chyczewski, L.2    Chrostek, L.3
  • 101
    • 0032559808 scopus 로고    scopus 로고
    • Activities of proteases in parietal thrombus of aortic aneurysm
    • Gacko M, Glowiński S. Activities of proteases in parietal thrombus of aortic aneurysm. Clin Chim Acta 1998; 271: 171-7.
    • (1998) Clin Chim Acta , vol.271 , pp. 171-177
    • Gacko, M.1    Glowiński, S.2
  • 102
    • 0037459360 scopus 로고    scopus 로고
    • Deficiency of the cysteine protease cathepsin S impairs microvessel growth
    • Shi GP, Sukhova GK, Kuzuya M, Ye Q, Du J, Zhang Y et al. Deficiency of the cysteine protease cathepsin S impairs microvessel growth. Circ Res 2003; 92: 493-500.
    • (2003) Circ Res , vol.92 , pp. 493-500
    • Shi, G.P.1    Sukhova, G.K.2    Kuzuya, M.3    Ye, Q.4    Du, J.5    Zhang, Y.6
  • 103
    • 0344043409 scopus 로고    scopus 로고
    • Cathepsin D and cathepsin L activities in aortic aneurysm wall and parietal thrombus
    • Gacko M, Glowiński S. Cathepsin D and cathepsin L activities in aortic aneurysm wall and parietal thrombus. Clin Chem Lab Med 1998; 36: 449-52.
    • (1998) Clin Chem Lab Med , vol.36 , pp. 449-452
    • Gacko, M.1    Glowiński, S.2
  • 104
    • 2442440597 scopus 로고    scopus 로고
    • Cathepsin S expression is up-regulated following balloon angioplasty in the hypercholesterolemic rabbit
    • Burns-Kurtis CL, Olzinski AR, Needle S, Fox JH, Capper EA, Kelly FM et al. Cathepsin S expression is up-regulated following balloon angioplasty in the hypercholesterolemic rabbit. Cardiovasc Res 2004; 62: 610-20.
    • (2004) Cardiovasc Res , vol.62 , pp. 610-620
    • Burns-Kurtis, C.L.1    Olzinski, A.R.2    Needle, S.3    Fox, J.H.4    Capper, E.A.5    Kelly, F.M.6
  • 105
    • 1542469612 scopus 로고    scopus 로고
    • Increased expression of elastolytic cysteine proteases, cathepsins S and K, in the neointima of balloon-injured rat carotid arteries
    • Cheng XW, Kuzuya M, Sasaki T, Arakawa K, Kanda S, Sumi D et al. Increased expression of elastolytic cysteine proteases, cathepsins S and K, in the neointima of balloon-injured rat carotid arteries. Am J Pathol 2004; 164: 243-51.
    • (2004) Am J Pathol , vol.164 , pp. 243-251
    • Cheng, X.W.1    Kuzuya, M.2    Sasaki, T.3    Arakawa, K.4    Kanda, S.5    Sumi, D.6
  • 107
    • 0037194598 scopus 로고    scopus 로고
    • Cathepsin-D affects multiple tumor progression steps in vivo: Proliferation, angiogenesis and apoptosis
    • Berchem G, Glondu M, Gleizes M, Brouillet JP, Vignon F, Garcia M et al. Cathepsin-D affects multiple tumor progression steps in vivo: proliferation, angiogenesis and apoptosis. Oncogene 2002; 21: 5951-5.
    • (2002) Oncogene , vol.21 , pp. 5951-5955
    • Berchem, G.1    Glondu, M.2    Gleizes, M.3    Brouillet, J.P.4    Vignon, F.5    Garcia, M.6
  • 108
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: Multifunctional enzymes in cancer
    • Mohamed MM, Sloane BF. Cysteine cathepsins: multifunctional enzymes in cancer. Nat Rev Cancer 2006; 6: 764-5.
    • (2006) Nat Rev Cancer , vol.6 , pp. 764-765
    • Mohamed, M.M.1    Sloane, B.F.2
  • 109
    • 33846643454 scopus 로고    scopus 로고
    • Cysteine cathepsins and the cutting edge of cancer invasion
    • Gocheva V, Joyce JA. Cysteine cathepsins and the cutting edge of cancer invasion. Cell Cycle 2007; 6: 60-4.
    • (2007) Cell Cycle , vol.6 , pp. 60-64
    • Gocheva, V.1    Joyce, J.A.2
  • 110
    • 37549070672 scopus 로고    scopus 로고
    • Cysteine cathepsin proteases as pharmacological targets in cancer
    • Palermo C, Joyce JA. Cysteine cathepsin proteases as pharmacological targets in cancer. Trends Pharmacol Sci 2008; 29: 22-8.
    • (2008) Trends Pharmacol Sci , vol.29 , pp. 22-28
    • Palermo, C.1    Joyce, J.A.2
  • 111
    • 38649084746 scopus 로고    scopus 로고
    • Dual contrasting roles of cysteine cathepsins in cancer progression: Apoptosis versus tumour invasion
    • Vasiljeva O, Turk B. Dual contrasting roles of cysteine cathepsins in cancer progression: apoptosis versus tumour invasion. Biochimie 2008; 90: 380-6.
    • (2008) Biochimie , vol.90 , pp. 380-386
    • Vasiljeva, O.1    Turk, B.2
  • 112
    • 0035202430 scopus 로고    scopus 로고
    • The six hyaluronidases-like genes in the human and mouse genomes
    • Csóka AB, Frost GI, Stern R. The six hyaluronidases-like genes in the human and mouse genomes. Matrix Biol 2001; 20: 499-508.
    • (2001) Matrix Biol , vol.20 , pp. 499-508
    • Csóka, A.B.1    Frost, G.I.2    Stern, R.3
  • 113
    • 44749085645 scopus 로고    scopus 로고
    • Stern R. Hyaluronidases in cancer biology. Semin Cancer Biol 2008; 18: 275-80.
    • Stern R. Hyaluronidases in cancer biology. Semin Cancer Biol 2008; 18: 275-80.
  • 114
    • 26444516484 scopus 로고    scopus 로고
    • Structures of vertebrate hyaluronidases and their unique enzymatic mechanism of hydrolysis
    • Jedrzejas MJ, Stern R. Structures of vertebrate hyaluronidases and their unique enzymatic mechanism of hydrolysis. Proteins 2005; 61: 227-38.
    • (2005) Proteins , vol.61 , pp. 227-238
    • Jedrzejas, M.J.1    Stern, R.2
  • 115
    • 34250205607 scopus 로고    scopus 로고
    • Structure of human hyaluronidase-1, a hyaluronan hydrolyzing enzyme involved in tumor growth and angiogenesis
    • Chao KL, Muthukumar L, Herzberg O. Structure of human hyaluronidase-1, a hyaluronan hydrolyzing enzyme involved in tumor growth and angiogenesis. Biochemistry 2007; 46: 6911-20.
    • (2007) Biochemistry , vol.46 , pp. 6911-6920
    • Chao, K.L.1    Muthukumar, L.2    Herzberg, O.3
  • 116
    • 0039261317 scopus 로고    scopus 로고
    • Purification and microsequencing of hyaluronidase isozymes from human urine
    • Csóka AB, Frost GI, Wong T, Stern R. Purification and microsequencing of hyaluronidase isozymes from human urine. FEBS Lett 1997; 417: 307-10.
    • (1997) FEBS Lett , vol.417 , pp. 307-310
    • Csóka, A.B.1    Frost, G.I.2    Wong, T.3    Stern, R.4
  • 117
    • 0344668719 scopus 로고    scopus 로고
    • Devising a pathway for hyaluronan catabolism: Are we there yet?
    • Stern R. Devising a pathway for hyaluronan catabolism: are we there yet? Glycobiology 2003; 12: 105R-15R.
    • (2003) Glycobiology , vol.12
    • Stern, R.1
  • 118
    • 0034677379 scopus 로고    scopus 로고
    • HYALLUCA-1, a candidate tumor suppressor gene on chromosome 3p21.3, is inactivated in head and neck squamous cell carcinomas by aberrant splicing of pre-mRNA
    • Frost GI, Mohapatra G, Wong TM, Csóka AB, Gray JW, Stern R. HYALLUCA-1, a candidate tumor suppressor gene on chromosome 3p21.3, is inactivated in head and neck squamous cell carcinomas by aberrant splicing of pre-mRNA. Oncogene 2000; 19: 870-7.
    • (2000) Oncogene , vol.19 , pp. 870-877
    • Frost, G.I.1    Mohapatra, G.2    Wong, T.M.3    Csóka, A.B.4    Gray, J.W.5    Stern, R.6
  • 120
    • 0642314338 scopus 로고    scopus 로고
    • Expression and regulation patters of hyaluronidases in small cell lung cancer and glioma lines
    • Junker N, Latini S, Petersen LN, Kristjansen PE. Expression and regulation patters of hyaluronidases in small cell lung cancer and glioma lines. Oncol Rep 2003; 10: 609-16.
    • (2003) Oncol Rep , vol.10 , pp. 609-616
    • Junker, N.1    Latini, S.2    Petersen, L.N.3    Kristjansen, P.E.4
  • 121
    • 34247119777 scopus 로고    scopus 로고
    • The magic glue hyaluronan and its eraser hyaluronidase: A biological overview
    • Girish KS, Kemparaju K. The magic glue hyaluronan and its eraser hyaluronidase: a biological overview. Life Sci 2007; 80: 1921-43.
    • (2007) Life Sci , vol.80 , pp. 1921-1943
    • Girish, K.S.1    Kemparaju, K.2
  • 122
    • 0032575479 scopus 로고    scopus 로고
    • HYAL2, a human gene expressed in many cells, encodes a lysosomal hyaluronidase with novel type specificity
    • Lepperdinger G, Strobl B, Kreil G. HYAL2, a human gene expressed in many cells, encodes a lysosomal hyaluronidase with novel type specificity. J Biol Chem 1998; 273: 22466-70.
    • (1998) J Biol Chem , vol.273 , pp. 22466-22470
    • Lepperdinger, G.1    Strobl, B.2    Kreil, G.3
  • 124
    • 0035202490 scopus 로고    scopus 로고
    • The dual functions of GPI-anchored PH-20: Hyaluronidase and intracellular signaling
    • Cherr GN, Yudin AI, Overstreet JW. The dual functions of GPI-anchored PH-20: hyaluronidase and intracellular signaling. Matrix Biol 2001; 20: 515-25.
    • (2001) Matrix Biol , vol.20 , pp. 515-525
    • Cherr, G.N.1    Yudin, A.I.2    Overstreet, J.W.3
  • 125
    • 0030059196 scopus 로고    scopus 로고
    • Association of elevated levels of hyaluronidase, a matrix-degrading enzyme, with prostate cancer progression
    • Lokeshwar VB, Lokeshwar BL, Pham HT, Block NL. Association of elevated levels of hyaluronidase, a matrix-degrading enzyme, with prostate cancer progression. Cancer Res 1996; 56: 651-7.
    • (1996) Cancer Res , vol.56 , pp. 651-657
    • Lokeshwar, V.B.1    Lokeshwar, B.L.2    Pham, H.T.3    Block, N.L.4
  • 126
    • 0033228245 scopus 로고    scopus 로고
    • Increased hyaluronidase expression in more aggressive prostate adenocarcinoma
    • Madan AK, Pang Y, Wilkiemeyer MB, Yu D, Beech DJ. Increased hyaluronidase expression in more aggressive prostate adenocarcinoma. Oncol Rep 1999; 6: 1431-3.
    • (1999) Oncol Rep , vol.6 , pp. 1431-1433
    • Madan, A.K.1    Pang, Y.2    Wilkiemeyer, M.B.3    Yu, D.4    Beech, D.J.5
  • 127
    • 33845877573 scopus 로고    scopus 로고
    • Hyaluronidase expression induces prostate tumor metastasis in an orthotopic mouse model
    • Kovar JL, Johnson MA, Volcheck WM, Chen J, Simpson MA. Hyaluronidase expression induces prostate tumor metastasis in an orthotopic mouse model. Am J Pathol 2006; 169: 1415-26.
    • (2006) Am J Pathol , vol.169 , pp. 1415-1426
    • Kovar, J.L.1    Johnson, M.A.2    Volcheck, W.M.3    Chen, J.4    Simpson, M.A.5
  • 128
    • 16844364920 scopus 로고    scopus 로고
    • HYAL1 hyaluronidase: A molecular determinant of bladder tumor growth and invasion
    • Lokeshwar VB, Cerwinka WH, Lokeshwar BL. HYAL1 hyaluronidase: a molecular determinant of bladder tumor growth and invasion. Cancer Res 2005; 65: 2243-50.
    • (2005) Cancer Res , vol.65 , pp. 2243-2250
    • Lokeshwar, V.B.1    Cerwinka, W.H.2    Lokeshwar, B.L.3
  • 130
    • 0036354170 scopus 로고    scopus 로고
    • Expression of PH-20 in normal and neoplastic breast tissue
    • Beech DJ, Madan AK, Deng N. Expression of PH-20 in normal and neoplastic breast tissue. J Surg Res 2002; 103: 203-7.
    • (2002) J Surg Res , vol.103 , pp. 203-207
    • Beech, D.J.1    Madan, A.K.2    Deng, N.3
  • 132
    • 0034623223 scopus 로고    scopus 로고
    • Differences in hyaluronic acidmediated functions and signaling in arterial, microvessel, and veinderived human endothelial cells
    • Lokeshwar VB, Selzer MG. Differences in hyaluronic acidmediated functions and signaling in arterial, microvessel, and veinderived human endothelial cells. J Biol Chem 2000; 275: 27641-9.
    • (2000) J Biol Chem , vol.275 , pp. 27641-27649
    • Lokeshwar, V.B.1    Selzer, M.G.2
  • 133
    • 21244464416 scopus 로고    scopus 로고
    • Hyaluronan fragments induce endothelial cell differentiation in a CD44- and CXCL1/GRO1-dependent manner
    • Takahashi Y, Li L, Kamiryo M, Asteriou T, Moustakas A, Yamashita H et al. Hyaluronan fragments induce endothelial cell differentiation in a CD44- and CXCL1/GRO1-dependent manner. J Biol Chem 2005; 280: 24195-204.
    • (2005) J Biol Chem , vol.280 , pp. 24195-24204
    • Takahashi, Y.1    Li, L.2    Kamiryo, M.3    Asteriou, T.4    Moustakas, A.5    Yamashita, H.6
  • 134
    • 0035853711 scopus 로고    scopus 로고
    • Stromal and epithelial expression of tumor markers hyaluronic acid and HYAL1 hyaluronidase in prostate cancer
    • Lokeshwar VB, Rubinowicz D, Schroeder GL, Forgacs E, Minna JD, Block NL et al. Stromal and epithelial expression of tumor markers hyaluronic acid and HYAL1 hyaluronidase in prostate cancer. J Biol Chem 2001; 276: 11922-32.
    • (2001) J Biol Chem , vol.276 , pp. 11922-11932
    • Lokeshwar, V.B.1    Rubinowicz, D.2    Schroeder, G.L.3    Forgacs, E.4    Minna, J.D.5    Block, N.L.6
  • 136
    • 1842417144 scopus 로고    scopus 로고
    • Tumorassociated hyaluronic acid: A new sensitive and specific urine marker for bladder cancer
    • Lokeshwar VB, Obek C, Soloway MS, Block NL. Tumorassociated hyaluronic acid: a new sensitive and specific urine marker for bladder cancer. Cancer Res 1997; 57: 773-7.
    • (1997) Cancer Res , vol.57 , pp. 773-777
    • Lokeshwar, V.B.1    Obek, C.2    Soloway, M.S.3    Block, N.L.4
  • 137
    • 24744443035 scopus 로고    scopus 로고
    • HYAL1 hyaluronidase in prostate cancer: A tumor promoter and suppressor
    • Lokeshwar VB, Cerwinka WH, Isoyama T, Lokeshwar BL. HYAL1 hyaluronidase in prostate cancer: a tumor promoter and suppressor. Cancer Res 2005; 65: 7782-9.
    • (2005) Cancer Res , vol.65 , pp. 7782-7789
    • Lokeshwar, V.B.1    Cerwinka, W.H.2    Isoyama, T.3    Lokeshwar, B.L.4
  • 138
    • 28444468878 scopus 로고    scopus 로고
    • Elevation of hyaluronidase-1 and soluble intercellular adhesion molecule-1 helps select bladder cancer patients at risk of invasion
    • Aboughalia AH. Elevation of hyaluronidase-1 and soluble intercellular adhesion molecule-1 helps select bladder cancer patients at risk of invasion. Arch Med Res 2006; 37: 109-16.
    • (2006) Arch Med Res , vol.37 , pp. 109-116
    • Aboughalia, A.H.1
  • 139
    • 0036466840 scopus 로고    scopus 로고
    • Hyaluronidase gene profiling and role of hyal-1 overexpression in an orthotopic model of prostate cancer
    • Patel S, Turner PR, Stubberfield C, Barry E, Rohlff CR, Stamps A et al. Hyaluronidase gene profiling and role of hyal-1 overexpression in an orthotopic model of prostate cancer. Int J Cancer 2002; 97: 416-24.
    • (2002) Int J Cancer , vol.97 , pp. 416-424
    • Patel, S.1    Turner, P.R.2    Stubberfield, C.3    Barry, E.4    Rohlff, C.R.5    Stamps, A.6
  • 140
    • 0041039937 scopus 로고    scopus 로고
    • The hyaluronidase gene HYAL1 maps to chromosome 3p21.2- p21.3 in human and 9F1-F2 in mouse, a conserved candidate tumor suppressor locus
    • Csóka AB, Frost GI, Heng HH, Scherer SW, Mohapatra G, Stern R. The hyaluronidase gene HYAL1 maps to chromosome 3p21.2- p21.3 in human and 9F1-F2 in mouse, a conserved candidate tumor suppressor locus. Genomics 1998; 48: 63-70.
    • (1998) Genomics , vol.48 , pp. 63-70
    • Csóka, A.B.1    Frost, G.I.2    Heng, H.H.3    Scherer, S.W.4    Mohapatra, G.5    Stern, R.6
  • 141
    • 0037063999 scopus 로고    scopus 로고
    • Hyaluronan oligosaccharides inhibit anchorage-independent growth of tumor cells by suppressing the phosphoinositide 3-kinase/Akt cell survival pathway
    • Ghatak S, Misra S, Toole BP. Hyaluronan oligosaccharides inhibit anchorage-independent growth of tumor cells by suppressing the phosphoinositide 3-kinase/Akt cell survival pathway. J Biol Chem 2002; 277: 38013-20.
    • (2002) J Biol Chem , vol.277 , pp. 38013-38020
    • Ghatak, S.1    Misra, S.2    Toole, B.P.3
  • 142
    • 0037145745 scopus 로고    scopus 로고
    • Expression of hyaluronan synthase 2 or hyaluronidase 1 differentially affect the growth rate of transplantable colon carcinoma cell tumors
    • Jacobson A, Rahmanian M, Rubin K, Heldin P. Expression of hyaluronan synthase 2 or hyaluronidase 1 differentially affect the growth rate of transplantable colon carcinoma cell tumors. Int J Cancer 2002; 102: 212-9.
    • (2002) Int J Cancer , vol.102 , pp. 212-219
    • Jacobson, A.1    Rahmanian, M.2    Rubin, K.3    Heldin, P.4
  • 143
    • 0037058318 scopus 로고    scopus 로고
    • Hyaluronidase reduces human breast cancer xenografts in SCID mice
    • Shuster S, Frost GI, Csoka AB, Formby B, Stern R. Hyaluronidase reduces human breast cancer xenografts in SCID mice. Int J Cancer 2002; 102: 192-7.
    • (2002) Int J Cancer , vol.102 , pp. 192-197
    • Shuster, S.1    Frost, G.I.2    Csoka, A.B.3    Formby, B.4    Stern, R.5
  • 144
    • 44749092220 scopus 로고    scopus 로고
    • Hyaluronidase: Both a tumor promoter and suppressor
    • Lokeshwar VB, Selzer MG. Hyaluronidase: both a tumor promoter and suppressor. Semin Cancer Biol 2008; 18: 281-7.
    • (2008) Semin Cancer Biol , vol.18 , pp. 281-287
    • Lokeshwar, V.B.1    Selzer, M.G.2
  • 146
    • 0034255845 scopus 로고    scopus 로고
    • Heparanase, a potential regulator of cell-matrix interactions
    • Dempsey LA, Brunn GJ, Platt JL. Heparanase, a potential regulator of cell-matrix interactions. Trends Biochem Sci 2000; 25: 349-51.
    • (2000) Trends Biochem Sci , vol.25 , pp. 349-351
    • Dempsey, L.A.1    Brunn, G.J.2    Platt, J.L.3
  • 147
    • 0035800803 scopus 로고    scopus 로고
    • Expression pattern sequence and secretion of human and chicken heparanase are determined by their signal peptide sequence
    • Goldshmidt O, Zcharia E, Aingorn H, Guatta-Rangini Z, Atzmon R, Michal I et al. Expression pattern sequence and secretion of human and chicken heparanase are determined by their signal peptide sequence. J Biol Chem 2001; 276: 29178-87.
    • (2001) J Biol Chem , vol.276 , pp. 29178-29187
    • Goldshmidt, O.1    Zcharia, E.2    Aingorn, H.3    Guatta-Rangini, Z.4    Atzmon, R.5    Michal, I.6
  • 148
    • 19944433489 scopus 로고    scopus 로고
    • Heparanase accelerates wound angiogenesis and wound healing in mouse and rat models
    • Zcharia E, Zilka R, Yaar A, Yacoby-Zeevi O, Zetser A, Metzger S et al. Heparanase accelerates wound angiogenesis and wound healing in mouse and rat models. FASEB J 2005; 19: 211-21.
    • (2005) FASEB J , vol.19 , pp. 211-221
    • Zcharia, E.1    Zilka, R.2    Yaar, A.3    Yacoby-Zeevi, O.4    Zetser, A.5    Metzger, S.6
  • 149
    • 0033057962 scopus 로고    scopus 로고
    • Mammalian heparanase: Gene cloning, expression and function in tumor progression and metastasis
    • Vlodavsky I, Friedmann Y, Elkin M, Aingorn H, Atzmon R, IshaiMichaeli R et al. Mammalian heparanase: gene cloning, expression and function in tumor progression and metastasis. Nat Med 1999; 5: 793-802.
    • (1999) Nat Med , vol.5 , pp. 793-802
    • Vlodavsky, I.1    Friedmann, Y.2    Elkin, M.3    Aingorn, H.4    Atzmon, R.5    IshaiMichaeli, R.6
  • 150
    • 0034904048 scopus 로고    scopus 로고
    • Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis
    • Vlodavsky I, Friedmann Y. Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis. J Clin Invest 2001; 108: 341-7.
    • (2001) J Clin Invest , vol.108 , pp. 341-347
    • Vlodavsky, I.1    Friedmann, Y.2
  • 152
    • 0033569922 scopus 로고    scopus 로고
    • Processing of the human heparanase precursor and evidence that the active enzyme is a heterodimer
    • Fairbanks MB, Mildner AM, Leone JW, Cavey GS, Mathews WR, Drong RF et al. Processing of the human heparanase precursor and evidence that the active enzyme is a heterodimer. J Biol Chem 1999; 274: 29587-90.
    • (1999) J Biol Chem , vol.274 , pp. 29587-29590
    • Fairbanks, M.B.1    Mildner, A.M.2    Leone, J.W.3    Cavey, G.S.4    Mathews, W.R.5    Drong, R.F.6
  • 154
    • 0042366191 scopus 로고    scopus 로고
    • Biochemical characterization of the active heterodimer form of human heparanase (Hpa1) protein expressed in insect cells
    • McKenzie E, Young K, Hircock M, Bennett J, Bhaman M, Felix R et al. Biochemical characterization of the active heterodimer form of human heparanase (Hpa1) protein expressed in insect cells. Biochem J 2003; 373: 423-35.
    • (2003) Biochem J , vol.373 , pp. 423-435
    • McKenzie, E.1    Young, K.2    Hircock, M.3    Bennett, J.4    Bhaman, M.5    Felix, R.6
  • 156
    • 49649094763 scopus 로고    scopus 로고
    • Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment
    • Abboud-Jarrous G, Atzmon R, Peretz T, Palermo C, Gadea BB, Joyce JA et al. Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment. J Biol Chem 2008; 283: 18167-76.
    • (2008) J Biol Chem , vol.283 , pp. 18167-18176
    • Abboud-Jarrous, G.1    Atzmon, R.2    Peretz, T.3    Palermo, C.4    Gadea, B.B.5    Joyce, J.A.6
  • 157
    • 0034719130 scopus 로고    scopus 로고
    • Identification of active-site residues of the pro-metastatic endoglycosidase heparanase
    • Hulett MD, Hornby JR, Ohms SJ, Zuegg J, Freeman C, Gready JE et al. Identification of active-site residues of the pro-metastatic endoglycosidase heparanase. Biochemistry 2000; 39: 15659-67.
    • (2000) Biochemistry , vol.39 , pp. 15659-15667
    • Hulett, M.D.1    Hornby, J.R.2    Ohms, S.J.3    Zuegg, J.4    Freeman, C.5    Gready, J.E.6
  • 158
    • 1542319836 scopus 로고    scopus 로고
    • Heparanase degrades syndecan-1 and perlecan heparan sulfate: Functional implications for tumor cell invasion
    • Reiland J, Sanderson RD, Waguespack M, Barker SA, Long R, Carson DD et al. Heparanase degrades syndecan-1 and perlecan heparan sulfate: functional implications for tumor cell invasion. J Biol Chem 2004; 279: 8047-55.
    • (2004) J Biol Chem , vol.279 , pp. 8047-8055
    • Reiland, J.1    Sanderson, R.D.2    Waguespack, M.3    Barker, S.A.4    Long, R.5    Carson, D.D.6
  • 159
    • 0028916622 scopus 로고
    • Molecular behavior adapts to context: Heparanase functions as an extracellular matrix-degrading enzyme or as a T cell adhesion molecule, depending on the local pH
    • Gilat D, Hershkoviz R, Goldkorn I, Cahalon L, Korner G, Vlodavsky I et al. Molecular behavior adapts to context: heparanase functions as an extracellular matrix-degrading enzyme or as a T cell adhesion molecule, depending on the local pH. J Exp Med 1995; 181: 1929-34.
    • (1995) J Exp Med , vol.181 , pp. 1929-1934
    • Gilat, D.1    Hershkoviz, R.2    Goldkorn, I.3    Cahalon, L.4    Korner, G.5    Vlodavsky, I.6
  • 160
    • 0037711133 scopus 로고    scopus 로고
    • Heparanase mediates cell adhesion independent of its enzymatic activity
    • Goldshmidt O, Zcharia E, Cohen M, Aingorn H, Cohen I, Nadav L et al. Heparanase mediates cell adhesion independent of its enzymatic activity. FASEB J 2003; 17: 1015-25.
    • (2003) FASEB J , vol.17 , pp. 1015-1025
    • Goldshmidt, O.1    Zcharia, E.2    Cohen, M.3    Aingorn, H.4    Cohen, I.5    Nadav, L.6
  • 161
    • 32944479184 scopus 로고    scopus 로고
    • Heparanase induces vascular endothelial growth factor expression: Correlation with p38 phosphorylation levels and Src activation
    • Zetser A, Bashenko Y, Edovitsky E, Levy-Adam F, Vlodavsky I, Ilan N. Heparanase induces vascular endothelial growth factor expression: correlation with p38 phosphorylation levels and Src activation. Cancer Res 2006; 66: 1455-63.
    • (2006) Cancer Res , vol.66 , pp. 1455-1463
    • Zetser, A.1    Bashenko, Y.2    Edovitsky, E.3    Levy-Adam, F.4    Vlodavsky, I.5    Ilan, N.6
  • 162
    • 33644863802 scopus 로고    scopus 로고
    • Heparanase promotes growth, angiogenesis and survival of primary breast tumors
    • Cohen I, Pappo O, Elkin M, San T, Bar-Shavit R, Hazan R et al. Heparanase promotes growth, angiogenesis and survival of primary breast tumors. Int J Cancer 2006; 118: 1609-17.
    • (2006) Int J Cancer , vol.118 , pp. 1609-1617
    • Cohen, I.1    Pappo, O.2    Elkin, M.3    San, T.4    Bar-Shavit, R.5    Hazan, R.6
  • 164
    • 33646341518 scopus 로고    scopus 로고
    • Novel heparanaseinhibiting antibody reduces neointima formation
    • Myler HA, Lipke EA, Rice EE, West JL. Novel heparanaseinhibiting antibody reduces neointima formation. J Biochem 2006; 139: 339-45.
    • (2006) J Biochem , vol.139 , pp. 339-345
    • Myler, H.A.1    Lipke, E.A.2    Rice, E.E.3    West, J.L.4
  • 166
  • 167
    • 34447287858 scopus 로고    scopus 로고
    • Heparanase: Structure, biological functions, and inhibition by heparin-derived mimetics of heparan sulfate
    • Vlodavsky I, Ilan N, Naggi A, Casu B. Heparanase: structure, biological functions, and inhibition by heparin-derived mimetics of heparan sulfate. Curr Pharm Des 2007; 13: 2057-73.
    • (2007) Curr Pharm Des , vol.13 , pp. 2057-2073
    • Vlodavsky, I.1    Ilan, N.2    Naggi, A.3    Casu, B.4
  • 168
    • 4143083982 scopus 로고    scopus 로고
    • Heparanase as a molecular target of cancer chemotherapy
    • Simizu S, Ishida K, Osada H. Heparanase as a molecular target of cancer chemotherapy. Cancer Sci 2004; 95: 553-8.
    • (2004) Cancer Sci , vol.95 , pp. 553-558
    • Simizu, S.1    Ishida, K.2    Osada, H.3
  • 169
    • 0036357939 scopus 로고    scopus 로고
    • Matrix metalloproteinases and cellular fibrinolytic activity
    • Lijnen HR. Matrix metalloproteinases and cellular fibrinolytic activity. Biochemistry (Mosc) 2002; 67: 92-8.
    • (2002) Biochemistry (Mosc) , vol.67 , pp. 92-98
    • Lijnen, H.R.1
  • 170
    • 33947321575 scopus 로고    scopus 로고
    • uPAR-uPA-PAI-1 interactions and signaling: A vascular biologist's view
    • Binder BR, Mihaly J, Prager GW. uPAR-uPA-PAI-1 interactions and signaling: a vascular biologist's view. Thromb Haemost 2007; 97: 336-42.
    • (2007) Thromb Haemost , vol.97 , pp. 336-342
    • Binder, B.R.1    Mihaly, J.2    Prager, G.W.3
  • 172
    • 0023153577 scopus 로고
    • Activation of plasminogen by single-chain urokinase or by two-chain urokinase: A demonstration that singlechain urokinase has a low catalytic activity (pro-urokinase)
    • Pannell R, Gurewich V. Activation of plasminogen by single-chain urokinase or by two-chain urokinase: a demonstration that singlechain urokinase has a low catalytic activity (pro-urokinase). Blood 1987; 69: 22-8.
    • (1987) Blood , vol.69 , pp. 22-28
    • Pannell, R.1    Gurewich, V.2
  • 173
    • 0023784931 scopus 로고
    • One-chain urokinase-type plasminogen activator from human sarcoma cells is a proenzyme with little or no intrinsic activity
    • Petersen LC, Lund LR, Nielsen LS, Dano K, Skriver L. One-chain urokinase-type plasminogen activator from human sarcoma cells is a proenzyme with little or no intrinsic activity. J Biol Chem 1988; 263: 11189-95.
    • (1988) J Biol Chem , vol.263 , pp. 11189-11195
    • Petersen, L.C.1    Lund, L.R.2    Nielsen, L.S.3    Dano, K.4    Skriver, L.5
  • 174
    • 0025917320 scopus 로고
    • Single-chain urokinase-type plasminogen activator does not possess measurable intrinsic amidolytic or plasminogen activator activities
    • Hussain SS. Single-chain urokinase-type plasminogen activator does not possess measurable intrinsic amidolytic or plasminogen activator activities. Biochemistry 1991; 30: 5707-15.
    • (1991) Biochemistry , vol.30 , pp. 5707-5715
    • Hussain, S.S.1
  • 175
    • 0023034961 scopus 로고
    • Binding of singlechain prourokinase to the urokinase receptor of human U937 cells
    • Cubellis MV, Nolli ML, Cassani G, Blasi F. Binding of singlechain prourokinase to the urokinase receptor of human U937 cells. J Biol Chem 1986; 261: 15189-22.
    • (1986) J Biol Chem , vol.261 , pp. 15189-15222
    • Cubellis, M.V.1    Nolli, M.L.2    Cassani, G.3    Blasi, F.4
  • 176
    • 0025845425 scopus 로고
    • Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinasetype plasminogen activator (Pro-uPA)
    • Kobayashi H, Schmitt M, Goretzki L, Chucholowski N, Calvete J, Kramer M et al. Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinasetype plasminogen activator (Pro-uPA). J Biol Chem 1991; 266: 5147-52.
    • (1991) J Biol Chem , vol.266 , pp. 5147-5152
    • Kobayashi, H.1    Schmitt, M.2    Goretzki, L.3    Chucholowski, N.4    Calvete, J.5    Kramer, M.6
  • 177
    • 0034711736 scopus 로고    scopus 로고
    • Plasminogen-independent initiation of the pro-urokinase activation cascade in vivo. Activation of pro-urokinase by glandular kallikrein (mGK-6) in plasminogen deficient mice
    • List K, Jensen ON, Bugge TH, Lund LR, Ploug M, Danø K et al. Plasminogen-independent initiation of the pro-urokinase activation cascade in vivo. Activation of pro-urokinase by glandular kallikrein (mGK-6) in plasminogen deficient mice. Biochemistry 2000; 39: 508-15.
    • (2000) Biochemistry , vol.39 , pp. 508-515
    • List, K.1    Jensen, O.N.2    Bugge, T.H.3    Lund, L.R.4    Ploug, M.5    Danø, K.6
  • 178
    • 0036369295 scopus 로고    scopus 로고
    • Urokinase as a multidomain protein and polyfunctional cell regulator
    • Stepanova VV, Tkachuck VA. Urokinase as a multidomain protein and polyfunctional cell regulator. Biochemistry (Mosc) 2002; 67: 109-18.
    • (2002) Biochemistry (Mosc) , vol.67 , pp. 109-118
    • Stepanova, V.V.1    Tkachuck, V.A.2
  • 179
    • 0023223148 scopus 로고
    • The receptor binding sequence of urokinase. A biological function for the growth-factor module of proteases
    • Appella E, Robinson EA, Ullrich SJ, Stoppelli MP, Corti A, Cassani G et al. The receptor binding sequence of urokinase. A biological function for the growth-factor module of proteases. J Biol Chem 1987; 262: 4437-40.
    • (1987) J Biol Chem , vol.262 , pp. 4437-4440
    • Appella, E.1    Robinson, E.A.2    Ullrich, S.J.3    Stoppelli, M.P.4    Corti, A.5    Cassani, G.6
  • 182
    • 56249141793 scopus 로고    scopus 로고
    • RNAimediated downregulation of urokinase plasminogen activator receptors inhibits proliferation, adhesion, migration and invasion in oral cancer cells
    • Epub ahead of print
    • Liang X, Yang X, Tang Y, Zhou H, Liu X, Xiao L et al. RNAimediated downregulation of urokinase plasminogen activator receptors inhibits proliferation, adhesion, migration and invasion in oral cancer cells. Oral Oncol 2008; (Epub ahead of print).
    • (2008) Oral Oncol
    • Liang, X.1    Yang, X.2    Tang, Y.3    Zhou, H.4    Liu, X.5    Xiao, L.6
  • 184
    • 23944450595 scopus 로고    scopus 로고
    • Matriptase-3 is a novel phylogenetically preserved membraneanchored serine protease with broad serpin reactivity
    • Szabo R, Netzel-Arnett S, Hobson JP, Antalis TM, Bugge TH. Matriptase-3 is a novel phylogenetically preserved membraneanchored serine protease with broad serpin reactivity. Biochem J 2005; 390: 231-42.
    • (2005) Biochem J , vol.390 , pp. 231-242
    • Szabo, R.1    Netzel-Arnett, S.2    Hobson, J.P.3    Antalis, T.M.4    Bugge, T.H.5
  • 185
    • 33746406076 scopus 로고    scopus 로고
    • Matriptase: Potent Proteolysis on the Cell Surface
    • List K, Bugge TH, Szabo R. Matriptase: Potent Proteolysis on the Cell Surface. Mol Med 2006; 12: 1-7.
    • (2006) Mol Med , vol.12 , pp. 1-7
    • List, K.1    Bugge, T.H.2    Szabo, R.3
  • 186
    • 48749092358 scopus 로고    scopus 로고
    • Genetic upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitro and in vivo and affects FAK and paxillin localization
    • Sanders AJ, Parr C, Martin TA, Lane J, Mason MD, Jiang WG. Genetic upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitro and in vivo and affects FAK and paxillin localization. J Cell Physiol 2008; 216: 780-9.
    • (2008) J Cell Physiol , vol.216 , pp. 780-789
    • Sanders, A.J.1    Parr, C.2    Martin, T.A.3    Lane, J.4    Mason, M.D.5    Jiang, W.G.6
  • 188
    • 0037020169 scopus 로고    scopus 로고
    • Matriptase- 2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins
    • Velasco G, Cal S, Quesada V, Sánchez LM, López-Otin C. Matriptase- 2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins. J Biol Chem 2002; 277: 37637-46.
    • (2002) J Biol Chem , vol.277 , pp. 37637-37646
    • Velasco, G.1    Cal, S.2    Quesada, V.3    Sánchez, L.M.4    López-Otin, C.5
  • 189
    • 33750315799 scopus 로고    scopus 로고
    • Matriptase activates stromelysin (MMP-3) and promotes tumor growth and angiogenesis
    • Jin X, Yagi M, Akiyama N, Hirosaki T, Higashi S, Lin CY et al. Matriptase activates stromelysin (MMP-3) and promotes tumor growth and angiogenesis. Cancer Sci 2006; 97: 1327-34.
    • (2006) Cancer Sci , vol.97 , pp. 1327-1334
    • Jin, X.1    Yagi, M.2    Akiyama, N.3    Hirosaki, T.4    Higashi, S.5    Lin, C.Y.6
  • 191
    • 34547684359 scopus 로고    scopus 로고
    • Matriptase-dependent cell surface proteolysis in epithelial development and pathogenesis
    • Bugge TH, List K, Szabo R. Matriptase-dependent cell surface proteolysis in epithelial development and pathogenesis. Front Biosci 2007; 12: 5060-70.
    • (2007) Front Biosci , vol.12 , pp. 5060-5070
    • Bugge, T.H.1    List, K.2    Szabo, R.3
  • 192
    • 34248192457 scopus 로고    scopus 로고
    • Human tissue kallikreins: A road under construction
    • Emami N, Diamandis EP. Human tissue kallikreins: a road under construction. Clin Chim Acta 2007; 381: 78-84.
    • (2007) Clin Chim Acta , vol.381 , pp. 78-84
    • Emami, N.1    Diamandis, E.P.2
  • 193
    • 47549096054 scopus 로고    scopus 로고
    • Debela M, Beaufort N, Magdolen V, Schechter NM, Craik CS, Schmitt M et al. Structures and specificity of the human kallikreinrelated peptidases KLK 4, 5, 6, and 7. Biol Chem 2008; 389: 623-32.
    • Debela M, Beaufort N, Magdolen V, Schechter NM, Craik CS, Schmitt M et al. Structures and specificity of the human kallikreinrelated peptidases KLK 4, 5, 6, and 7. Biol Chem 2008; 389: 623-32.
  • 194
    • 0035018273 scopus 로고    scopus 로고
    • The new human tissue kallikrein gene family: Structure, function, and association to disease
    • Yousef GM, Diamandis EP. The new human tissue kallikrein gene family: structure, function, and association to disease. Endor Rev 2001; 22: 184-204.
    • (2001) Endor Rev , vol.22 , pp. 184-204
    • Yousef, G.M.1    Diamandis, E.P.2
  • 195
    • 19344371357 scopus 로고    scopus 로고
    • Human tissue kallikrein gene family: Applications in cancer
    • Obiezu CV, Diamandis EP. Human tissue kallikrein gene family: applications in cancer. Cancer Lett 2005; 224: 1-22.
    • (2005) Cancer Lett , vol.224 , pp. 1-22
    • Obiezu, C.V.1    Diamandis, E.P.2
  • 196
    • 0036661263 scopus 로고    scopus 로고
    • Human tissue kallikreins: A new enzymatic cascade pathway?
    • Yousef GM, Diamandis EP. Human tissue kallikreins: a new enzymatic cascade pathway? Biol Chem 2002; 383: 1045-57.
    • (2002) Biol Chem , vol.383 , pp. 1045-1057
    • Yousef, G.M.1    Diamandis, E.P.2
  • 197
    • 28844506112 scopus 로고    scopus 로고
    • Biochemical characterization of human kallikrein 8 and its possible involvement in the degradation of extracellular matrix proteins
    • Rajapakse S, Ogiwara K, Takano N, Moriyama A, Takahashi T. Biochemical characterization of human kallikrein 8 and its possible involvement in the degradation of extracellular matrix proteins. FEBS Lett 2005; 579: 6879-84.
    • (2005) FEBS Lett , vol.579 , pp. 6879-6884
    • Rajapakse, S.1    Ogiwara, K.2    Takano, N.3    Moriyama, A.4    Takahashi, T.5
  • 199
    • 34047270915 scopus 로고    scopus 로고
    • Expression and functional characterization of the cancer-related serine protease, human tissue kallikrein 14
    • Borgono CA, Michael IP, Shaw JL, Luo LY, Ghosh MC, Soosaipillai A et al. Expression and functional characterization of the cancer-related serine protease, human tissue kallikrein 14. J Biol Chem 2007; 282: 2405-22.
    • (2007) J Biol Chem , vol.282 , pp. 2405-2422
    • Borgono, C.A.1    Michael, I.P.2    Shaw, J.L.3    Luo, L.Y.4    Ghosh, M.C.5    Soosaipillai, A.6
  • 200
    • 41149167016 scopus 로고    scopus 로고
    • The extracellular matrix protein fibronectin is a substrate for kallikrein 7
    • Ramani VC, Haun RS. The extracellular matrix protein fibronectin is a substrate for kallikrein 7. Biochem Biophys Res Commun 2008; 369: 1169-73.
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 1169-1173
    • Ramani, V.C.1    Haun, R.S.2
  • 201
    • 34247597726 scopus 로고    scopus 로고
    • Kallikrein 7 enhances pancreatice cancer cell invasion by shedding E-cadherin
    • Johnson SK, Ramani VC, Hennings L, Haun RS. Kallikrein 7 enhances pancreatice cancer cell invasion by shedding E-cadherin. Cancer 2007; 109: 1811-20.
    • (2007) Cancer , vol.109 , pp. 1811-1820
    • Johnson, S.K.1    Ramani, V.C.2    Hennings, L.3    Haun, R.S.4
  • 202
    • 33646136687 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors as prospective agents for the prevention and treatment of cardiovascular and neoplastic diseases
    • Review
    • Sang QX, Jin Y, Newcomer RG, Monroe SC, Fang X, Hurst DR, Lee S, Cao Q, Schwartz MA. Matrix metalloproteinase inhibitors as prospective agents for the prevention and treatment of cardiovascular and neoplastic diseases. Curr Top Med Chem. 2006; 6: 289-316. Review.
    • (2006) Curr Top Med Chem , vol.6 , pp. 289-316
    • Sang, Q.X.1    Jin, Y.2    Newcomer, R.G.3    Monroe, S.C.4    Fang, X.5    Hurst, D.R.6    Lee, S.7    Cao, Q.8    Schwartz, M.A.9


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