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Volumn 16, Issue 2, 2011, Pages 698-706

Cryptic activities of fibronectin fragments, particularly cryptic proteases

Author keywords

Cryptic activities; Fn proteinase; Mammalian fibronectins; Review; Small molecular mass inhibitors

Indexed keywords

ANIMALIA; BOVINAE; MAMMALIA; RATTUS;

EID: 79954989330     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3713     Document Type: Article
Times cited : (7)

References (48)
  • 1
    • 0002243057 scopus 로고
    • Primary structure of fibronectin
    • D. F Mosher, Ed Academic Press, New-York, London.
    • T.E. Petersen, K. Skorstengaard, and K. Vibe-Pedersen: Primary structure of fibronectin. In Fibronectin D. F Mosher, Ed, Academic Press, New-York, London. (1989)
    • (1989) Fibronectin
    • Petersen, T.E.1    Skorstengaard, K.2    Vibe-Pedersen, K.3
  • 3
    • 50249176028 scopus 로고    scopus 로고
    • New insights into form and function of fibronectin spliced variants
    • E.S. White, F.E. Baralle and A.F. Muro: New insights into form and function of fibronectin spliced variants. J. Pathol 216, 1-14, (2008)
    • (2008) J. Pathol , vol.216 , pp. 1-14
    • White, E.S.1    Baralle, F.E.2    Muro, A.F.3
  • 4
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis, a cell mediated matrix assembly process
    • Y.Mao and J. E. Schwarzbauer: Fibronectin fibrillogenesis, a cell mediated matrix assembly process. Matrix Biol. 24, 389-9, (2005)
    • (2005) Matrix Biol. , vol.24 , pp. 389-389
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 5
    • 77953566262 scopus 로고    scopus 로고
    • Zinc induces structural reorganization of the gelatin binding domain from human fibronectin and affects collagen binding
    • M. Graille, M. Pagano, T. Rose, M. Reboud Ravaux and H. van Tilbeurgh: Zinc induces structural reorganization of the gelatin binding domain from human fibronectin and affects collagen binding. Structure. I8, 710-8, (2010)
    • (2010) Structure. , vol.I8 , pp. 710-718
    • Graille, M.1    Pagano, M.2    Rose, T.3    Reboud Ravaux, M.4    Van Tilbeurgh, H.5
  • 6
    • 0026731793 scopus 로고
    • Fibronectin fragments cause chondrolysis of bovine articular cartilage slices in culture
    • G.A. Homandberg , R. Meyers, D.L. Xie: Fibronectin fragments cause chondrolysis of bovine articular cartilage slices in culture. J Biol Chem. 267, 3597-604, (1992)
    • (1992) J Biol Chem. , vol.267 , pp. 3597-3604
    • Homandberg, G.A.1    Meyers, R.2    Xie, D.L.3
  • 7
    • 0031822516 scopus 로고    scopus 로고
    • Fibronectin fragments modulate human retinal capillary cell proliferation and migration
    • DOI 10.2337/diabetes.47.8.1335
    • M.B. Grant, S. Caballero , D.M. Bush and P.E. Spoerri: Fibronectin fragments modulate human retinal capillary cell proliferation and migration. Diabetes. 47, 1335-40, (1998) (Pubitemid 28357013)
    • (1998) Diabetes , vol.47 , Issue.8 , pp. 1335-1340
    • Grant, M.B.1    Caballero, S.2    Bush, D.M.3    Spoerri, P.E.4
  • 8
    • 0029090299 scopus 로고
    • Release of biological activities from quiescent fibronectin by a conformational change and limited proteolysis by matrix metalloproteinases
    • F. Fukai , M.Ohtaki , N. Fujii , H. Yajima , T. Ishii , Y. Nishizawa , K. Miyazaki and T Katayama : Release of biological activities from quiescent fibronectin by a conformational change and limited proteolysis by matrix metalloproteinases: Biochemistry. 34, 11453-9, (1995)
    • (1995) Biochemistry. , vol.34 , pp. 11453-11459
    • Fukai, F.1    Ohtaki, M.2    Fujii, N.3    Yajima, H.4    Ishii, T.5    Nishizawa, Y.6    Miyazaki, K.7    Katayama, T.8
  • 9
    • 34249067404 scopus 로고    scopus 로고
    • Interdomain association in fibronectin: Insight into cryptic sites and fibrillogenesis
    • DOI 10.1038/sj.emboj.7601694, PII 7601694
    • I.Vakonakis , D. Staunton , L.M. Rooney and I.D. Campbell: Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis: EMBO J. 26, 2575-83, (2007) (Pubitemid 46788320)
    • (2007) EMBO Journal , vol.26 , Issue.10 , pp. 2575-2583
    • Vakonakis, I.1    Staunton, D.2    Rooney, L.M.3    Campbell, I.D.4
  • 11
    • 0025866527 scopus 로고
    • Collagen-binding domain of human plasma fibronectin contains a latent type-IV collagenase
    • S. Lambert-Vidmar, F. Lottspeich, I. Emod, J.M. Imhoff and V. Keil-Dlouha: Collagen-binding domain of human plasma fibronectin contains a latent type-IV collagenase: Eur. J. Biochem 201, 79-84, (1991)
    • (1991) Eur. J. Biochem , vol.201 , pp. 79-84
    • Lambert-Vidmar, S.1    Lottspeich, F.2    Emod, I.3    Imhoff, J.M.4    Keil-Dlouha, V.5
  • 12
    • 0032126695 scopus 로고    scopus 로고
    • Expression of collagenase/gelatinase activity from basement-membrane fibronectin. Isolation after limited proteolysis of a bovine lens capsule and molecular definition of this thiol-dependent zinc metalloproteinase
    • L. Boudjennah , V. Dalet-Fumeron and M. Pagano : Expression of collagenase/gelatinase activity from basement-membrane fibronectin:isolation after limited proteolysis of a bovine lens capsule and molecular definition of this thiol-dependent zinc metalloproteinase. Eur. J. Biochem. 255, 246-54, (1998) (Pubitemid 28316859)
    • (1998) European Journal of Biochemistry , vol.255 , Issue.1 , pp. 246-254
    • Boudjennah, L.1    Dalet-Fumeron, V.2    Pagano, M.3
  • 13
    • 0037446064 scopus 로고    scopus 로고
    • Vascular smooth muscle cells efficiently activate a new proteinase cascade involving plasminogen and fibronectin
    • X. Houard, C. Monnot, V. Dive, P. Corvol and M. Pagano: Vascular smooth muscle cells efficiently activate a new proteinase cascade involving plasminogen and fibronectin. J. Cell. Biochem. 88, 1188-2001, (2003)
    • (2003) J. Cell. Biochem. , vol.88 , pp. 1188-2001
    • Houard, X.1    Monnot, C.2    Dive, V.3    Corvol, P.4    Pagano, M.5
  • 14
    • 0027379724 scopus 로고
    • Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin
    • E.L. Georges, E.N. Georges-Labouesse, R.S. Patel-King, H. Rayburn and R.O. Hynes: Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development. 119, 1079-1091, (1993) (Pubitemid 23358578)
    • (1993) Development , vol.119 , Issue.4 , pp. 1079-1091
    • George, E.L.1    Georges-Labouesse, E.N.2    Patel-King, R.S.3    Rayburn, H.4    Hynes, R.O.5
  • 15
    • 0024344620 scopus 로고
    • Reappearance of an embryonic pattern of fibronectin splicing during wound healing in the adult rat
    • C. Ffrench-Constant, L. Van de Water, H.F. Dvorak and R.O Hynes: Reappearance of an embryonic pattern of fibronectin splicing during wound healing in the adult rat. J. Cell. Biol. 109, 903-914, (1989) (Pubitemid 19197047)
    • (1989) Journal of Cell Biology , vol.109 , Issue.2 , pp. 903-914
    • French-Constant, C.1    Van De Water, L.2    Dvorak, H.F.3    Hynes, R.O.4
  • 16
    • 0028952453 scopus 로고
    • Regulation of fibronectin expression in rat regenerating liver
    • M. Caputi, C.A. Melo and F.E. Baralle: Regulation of fibronectin expression in rat regenerating liver. Nucleic. Acids. Res. 23, 238-243, (1995)
    • (1995) Nucleic. Acids. Res. , vol.23 , pp. 238-243
    • Caputi, M.1    Melo, C.A.2    Baralle, F.E.3
  • 17
    • 0028596335 scopus 로고
    • Expression of variant fibronectin in wound healing: Cellular source and biological activities of the EIIIA segment in rat hepatic fibrogenesis
    • W.R. Jarnagin, D.C. Rakay, V.E. Kotesliansky, S.S. Wano and B.M. Bissell: Expression of variant fibronectin in wound healing: cellular source and biological activities of the EIIIA segment in rat hepatic fibrogenesis. J.Cell.Biol. 127, 2037-2048, (1994)
    • (1994) J.Cell.Biol. , vol.127 , pp. 2037-2048
    • Jarnagin, W.R.1    Rakay, D.C.2    Kotesliansky, V.E.3    Wano, S.S.4    Bissell, B.M.5
  • 18
    • 0031010393 scopus 로고    scopus 로고
    • HRS/SRp40-mediated inclusion of the fibronectin EIIIB exon, a possible cause of increased EIIIB expression in proliferating liver
    • K. Du, Y. Peng, L.E. Greenbaum, B.A. Haber and R.Taub: HRS/SRp40-mediated inclusion of the fibronectin EIIIB exon: a possible cause of increased EIIIB expression in proliferative liver. Mol. Cell. Biol. 17, 4096-4104, (1997) (Pubitemid 27281886)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.7 , pp. 4096-4104
    • Du, K.1    Peng, Y.2    Greenbaum, L.E.3    Haber, B.A.4    Taub, R.5
  • 19
    • 0004133195 scopus 로고
    • Academic Press, New-York, London.
    • D. F Mosher, Fibronectin, Academic Press, New-York, London. (1989)
    • (1989) Fibronectin
    • Mosher, D.F.1
  • 20
    • 33745271833 scopus 로고    scopus 로고
    • Role of fibronectin assembly in platelet thrombus formation
    • J. Cho, D.F. Mosher: Role of fibronectin assembly in platelet thrombus formation. J. Thromb. Haemost. 4, 1461-69, (2006)
    • (2006) J. Thromb. Haemost. , vol.4 , pp. 1461-1469
    • Cho, J.1    Mosher, D.F.2
  • 21
    • 0033838314 scopus 로고    scopus 로고
    • Persistence of platelet thrombus formation in arterioles of mice lacking both von Willebrand factor and fibrinogen
    • H.Ni, C.V. Denis, S. Subbarao, J.L. Dogen, T.N. Sato, R.O. Hynes and D.D. Wagner: Persistence of platelet thrombus formation in arterioles of mice lacking both won Willebrand factor and fibrinogen. J. Clin. Invest. 106, 385-392, (2000) (Pubitemid 30655638)
    • (2000) Journal of Clinical Investigation , vol.106 , Issue.3 , pp. 385-392
    • Ni, H.1    Denis, C.V.2    Subbarao, S.3    Degen, J.L.4    Sato, T.N.5    Hynes, R.O.6    Wagner, D.D.7
  • 23
    • 0024804591 scopus 로고
    • Selective secretion of alternatively spliced fibronectin variants
    • DOI 10.1083/jcb.109.6.3445
    • J.E. Schwarzbauer, C.S. Spencer and C.L. Wilson: Selective secretion of alternatively spliced fibronectin variants. J.Cell.Biol. 109, 3445-3453, (1989) (Pubitemid 20017994)
    • (1989) Journal of Cell Biology , vol.109 , Issue.6 , pp. 3445-3453
    • Schwarzbauer, J.E.1    Spencer, C.S.2    Wilson, C.L.3
  • 24
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • A.L. Main, T.S. Harvey, M. Baron, J. Boyd and I.D. Campbell: The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell. 71, 671-78, (1992)
    • (1992) Cell. , vol.71 , pp. 671-678
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 25
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • DOI 10.1242/jcs.00059
    • R. Pankov and K.M. Yamada: Fibronectin at a glance. J. Cell. Sci. 115, 3861-63. (2002) (Pubitemid 35256486)
    • (2002) Journal of Cell Science , vol.115 , Issue.20 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 26
    • 50949116784 scopus 로고    scopus 로고
    • The cartilage chondrolytic mechanism of fibronectin fragments involves MAP kinases: Comparison of three fragments and native fibronectin
    • L.Ding, D. Guo and G.A. Homandberg: The cartilage chondrolytic mechanism of fibronectin fragments involves MAP kinases: comparison of three fragments and native fibronectin. Osteoarthritis Cartilage. 16, 1253-62. (2008)
    • (2008) Osteoarthritis Cartilage. , vol.16 , pp. 1253-1262
    • Ding, L.1    Guo, D.2    Homandberg, G.A.3
  • 27
    • 0037093523 scopus 로고    scopus 로고
    • The 45 kDa collagen-binding fragment of fibronectin induces matrix metalloproteinase-13 synthesis by chondrocytes and aggrecan degradation by aggrecanases
    • H. Stanton , L. Ung , A.J. Fosang : The 45 kDa collagen-binding fragment of fibronectin induces matrix metalloproteinase-13 synthesis by chondrocytes and aggrecan degradation by aggrecanases. Biochem J. 364, 181-90. (2002) (Pubitemid 34538961)
    • (2002) Biochemical Journal , vol.364 , Issue.1 , pp. 181-190
    • Stanton, H.1    Ung, L.2    Fosang, A.J.3
  • 29
    • 0031036225 scopus 로고    scopus 로고
    • Cryptic self-association sites in type III modules of fibronectin
    • DOI 10.1074/jbc.272.3.1718
    • K.C. Ingham , S.A. Brew , S. Huff, and S.V. Litvinovich : Cryptic self-association sites in type III modules of fibronectin J Biol Chem. 272, 1718-24. (1997) (Pubitemid 27043258)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.3 , pp. 1718-1724
    • Ingham, K.C.1    Brew, S.A.2    Huff, S.3    Litvinovich, S.V.4
  • 30
    • 33745191852 scopus 로고    scopus 로고
    • The N-terminal 70-kDa fragment of fibronectin binds to cell surface fibronectin assembly sites in the absence of intact fibronectin
    • B.R. Tomasini-Johansson, D.S. Annis and D.F. Mosher: The N-terminal 70-kDa fragment of fibronectin binds to cell surface fibronectin assembly sites in the absence of intact fibronectin. Matrix. Biol. 25, 282-93, (2006)
    • (2006) Matrix. Biol. , vol.25 , pp. 282-293
    • Tomasini-Johansson, B.R.1    Annis, D.S.2    Mosher, D.F.3
  • 31
    • 0026686130 scopus 로고
    • Quantitative study of the binding of cysteine proteinases to basement membranes
    • N. Guinec, V. Dalet-Fumeron and M. Pagano : Quantitative study of the binding of cysteine proteinases to basement membranes. FEBS. Lett. 308, 305-308, (1992)
    • (1992) FEBS. Lett. , vol.308 , pp. 305-308
    • Guinec, N.1    Dalet-Fumeron, V.2    Pagano, M.3
  • 32
    • 0027329828 scopus 로고
    • In vitro study of basement membrane degradation by the cysteine proteinases, cathepsins B, B-like and L. Digestion of collagen IV, laminin, fibronectin, and release of gelatinase activities from basement membrane fibronectin
    • N. Guinec, V. Dalet-Fumeron and M Pagano : "In vitro" study of basement membrane degradation by the cysteine proteinases, cathepsins B, B-like and L. Digestion of collagen IV, laminin, fibronectin, and release of gelatinase activities from basement membrane fibronectin. Biol. Chem Hoppe Seyler. 374, 1135-46, (1993) (Pubitemid 2023819)
    • (1993) Biological Chemistry Hoppe-Seyler , vol.374 , Issue.12 , pp. 1135-1146
    • Guinec, N.1    Dalet-Fumeron, V.2    Pagano, M.3
  • 34
    • 0025616093 scopus 로고
    • Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties
    • Y. Okada, T. Morodoni, J.J. Enghild, K. Susuki, A. Yasui, I. Nakanishi, G. Salvesen, and H. Nagase: Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties. Eur. J. Biochem. 194, 721-730, (1990)
    • (1990) Eur. J. Biochem. , vol.194 , pp. 721-730
    • Okada, Y.1    Morodoni, T.2    Enghild, J.J.3    Susuki, K.4    Yasui, A.5    Nakanishi, I.6    Salvesen, G.7    Nagase, H.8
  • 35
    • 0029146477 scopus 로고
    • Neutrophil elastase processing of gelatinase A is mediated by extracellular matrix
    • A. Rice and M. J. Banda: Neutrophil elastase processing of gelatinase A is mediated by extracellular matrix. Biochemistry. 34, 9256-59, (1995)
    • (1995) Biochemistry. , vol.34 , pp. 9256-9259
    • Rice, A.1    Banda, M.J.2
  • 36
    • 0034467924 scopus 로고    scopus 로고
    • The proteolytic activity of the recombinant cryptic human fibronectin type IV collagenase from E. coli expression
    • DOI 10.1023/A:1007104420017
    • J. Schnepel and H Tschesche: The proteolytic activity of the recombinant cryptic human fibronectin type IV collagenase from E-coli expression J. Prot .Chem. 19, 685-692, (2000) (Pubitemid 32220986)
    • (2000) Journal of Protein Chemistry , vol.19 , Issue.8 , pp. 685-692
    • Schnepel, J.1    Tschesche, H.2
  • 37
    • 0032774325 scopus 로고    scopus 로고
    • The proteolytic activity and cleavage specificity of fibronectin- gelatinase and fibronectin-lamininase
    • DOI 10.1023/A:1020684508212
    • J.Unger and H. Tschesche: The proteolytic activity and cleavage specificity of fibronectin-gelatinase and fibronectin-lamininase J.Prot.Chem. 18, 403-411, (1999) (Pubitemid 29382094)
    • (1999) Journal of Protein Chemistry , vol.18 , Issue.4 , pp. 403-411
    • Unger, J.1    Tschesche, H.2
  • 38
    • 54249091078 scopus 로고    scopus 로고
    • Liberation of an Nterminal proline-rich peptide from the cryptic proteinase of fibonectin by auto-proteolysis
    • M. Pagano, G. Clotild, G. Bolbach, M. Michiel, S. Haddag and M. Reboud-Ravaux: Liberation of an Nterminal proline-rich peptide from the cryptic proteinase of fibonectin by auto-proteolysis. Arch.Biochem. Biophys. 479, 158-162, (2008)
    • (2008) Arch.Biochem. Biophys. , vol.479 , pp. 158-162
    • Pagano, M.1    Clotild, G.2    Bolbach, G.3    Michiel, M.4    Haddag, S.5    Reboud-Ravaux, M.6
  • 42
    • 38349014380 scopus 로고    scopus 로고
    • Src family kinases: Regulation of their activities, levels and identification of new pathways
    • E. Ingley: Src family kinases: regulation of their activities, levels and identification of new pathways. Biochim. Biophys. Acta, 1784, 56-65, (2008)
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 56-65
    • Ingley, E.1
  • 47
    • 0026505650 scopus 로고
    • A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteases
    • C. G. Knight, F. Willenbrock and G Murphy: A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteases, FEBS Lett. 296, 263-266, (1992)
    • (1992) FEBS Lett. , vol.296 , pp. 263-266
    • Knight, C.G.1    Willenbrock, F.2    Murphy, G.3


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