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Volumn 51, Issue 3, 2005, Pages 217-221

Differential effects of echistatin and thrombin on collagen production and prolidase activity in human dermal fibroblasts and their possible implication in β1-integrin-mediated signaling

Author keywords

1 integrins; Collagen; Echistatin; Fibroblasts; Prolidase; Thrombin

Indexed keywords

BETA1 INTEGRIN; ECHISTATIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROLINE DIPEPTIDASE; RAF PROTEIN; SOS PROTEIN; THROMBIN;

EID: 12344265557     PISSN: 10436618     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phrs.2004.08.004     Document Type: Article
Times cited : (37)

References (33)
  • 1
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphotylated in response to cell attachment to fibronectin
    • S.K. Hanks, M.B. Calalb, M.C. Harper, and S.K. Patel Focal adhesion protein-tyrosine kinase phosphotylated in response to cell attachment to fibronectin Proc Natl Acad Sci USA 89 1992 8487 8491
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 2
    • 0027682591 scopus 로고    scopus 로고
    • Adhesion molecules in cancer, the role of integrins
    • R.L. Juliano, and J.A. Varner Adhesion molecules in cancer, the role of integrins Curr Opin Cell Biol 5 1997 812 818
    • (1997) Curr Opin Cell Biol , vol.5 , pp. 812-818
    • Juliano, R.L.1    Varner, J.A.2
  • 4
    • 0035085628 scopus 로고    scopus 로고
    • Cell-matrix contact structures
    • J.C. Adams Cell-matrix contact structures Cell Mol Life Sci 58 2001 371 392
    • (2001) Cell Mol Life Sci , vol.58 , pp. 371-392
    • Adams, J.C.1
  • 5
    • 0025806141 scopus 로고
    • In vitro and in vivo consequences of VLA-2 expression on rhabdomyosarcoma cells
    • M. Bosco, C. Chan, N. Matsuura, Y. Tokada, B.R. Zetter, and M.E. Hemler In vitro and in vivo consequences of VLA-2 expression on rhabdomyosarcoma cells Science 25 1991 1600 1602
    • (1991) Science , vol.25 , pp. 1600-1602
    • Bosco, M.1    Chan, C.2    Matsuura, N.3    Tokada, Y.4    Zetter, B.R.5    Hemler, M.E.6
  • 6
    • 0033581478 scopus 로고    scopus 로고
    • Integrin alpha2beta1 mediates isoform-specific activation of p38 and up-regulation of collagen gene transcription by a mechanism involving the alpha2 cytoplasmic tail
    • J. Ivaska, H. Reunanen, J. Westermarck, L. Koivisto, V.M. Kahari, and J. Heino Integrin alpha2beta1 mediates isoform-specific activation of p38 and up-regulation of collagen gene transcription by a mechanism involving the alpha2 cytoplasmic tail J Cell Biol 147 1999 401 416
    • (1999) J Cell Biol , vol.147 , pp. 401-416
    • Ivaska, J.1    Reunanen, H.2    Westermarck, J.3    Koivisto, L.4    Kahari, V.M.5    Heino, J.6
  • 7
    • 0021338826 scopus 로고
    • Prolidase and prolidase deficiency
    • I. Myara, C. Charpentier, and A. Lemonnier Prolidase and prolidase deficiency Life Sci 34 1984 1985 1998
    • (1984) Life Sci , vol.34 , pp. 1985-1998
    • Myara, I.1    Charpentier, C.2    Lemonnier, A.3
  • 8
    • 0027439867 scopus 로고
    • Proline-dependent structural and biological properties of peptides and proteins
    • A. Yaron, and F. Naider Proline-dependent structural and biological properties of peptides and proteins Crit Rev Biochem Mol Biol 28 1993 31 81
    • (1993) Crit Rev Biochem Mol Biol , vol.28 , pp. 31-81
    • Yaron, A.1    Naider, F.2
  • 9
    • 0027276281 scopus 로고
    • Hydrolysis of proline dipeptides completely fulfills the proline requirement in a proline-auxotropic Chinese hamster ovary cell line
    • K.S. Emmerson, and J.M. Phang Hydrolysis of proline dipeptides completely fulfills the proline requirement in a proline-auxotropic Chinese hamster ovary cell line J Nutr 123 1993 909 914
    • (1993) J Nutr , vol.123 , pp. 909-914
    • Emmerson, K.S.1    Phang, J.M.2
  • 10
    • 0016591014 scopus 로고
    • Iminopeptiduria: A genetic defect in recycling of collagen; A method for determining prolidase in erytrocytes
    • S.H. Jackson, A.W. Dennis, and M. Greenberg Iminopeptiduria: a genetic defect in recycling of collagen; a method for determining prolidase in erytrocytes Can Med Assoc J 113 1975 759 763
    • (1975) Can Med Assoc J , vol.113 , pp. 759-763
    • Jackson, S.H.1    Dennis, A.W.2    Greenberg, M.3
  • 11
    • 0030930783 scopus 로고    scopus 로고
    • Prolidase activity in fibroblasts is regulated by interaction of extracellular matrix with cell surface integrin receptor
    • J. Pałka, and J. Phang Prolidase activity in fibroblasts is regulated by interaction of extracellular matrix with cell surface integrin receptor J Cell Biochem 67 1997 166 175
    • (1997) J Cell Biochem , vol.67 , pp. 166-175
    • Pałka, J.1    Phang, J.2
  • 12
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphotylated in response to cell attachment to fibronectin
    • S.K. Hanks, M.B. Calalb, M.C. Harper, and S.K. Patel Focal adhesion protein-tyrosine kinase phosphotylated in response to cell attachment to fibronectin Proc Natl Acad Sci USA 89 1992 8487 8491
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 13
    • 0030297728 scopus 로고    scopus 로고
    • Cooperation between soluble factors and integrin-mediated cell anchorage in the control of cell growth and differentiation
    • R. Juliano Cooperation between soluble factors and integrin-mediated cell anchorage in the control of cell growth and differentiation Bioessays 18 1996 911 917
    • (1996) Bioessays , vol.18 , pp. 911-917
    • Juliano, R.1
  • 14
    • 0029011218 scopus 로고
    • The MAPK signaling cascade
    • R. Seger, and E.G. Krebs The MAPK signaling cascade FASEB J 9 1995 726 735
    • (1995) FASEB J , vol.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 15
    • 0033655316 scopus 로고    scopus 로고
    • Interaction between cells and extracellular matrix: Signaling by integrins and the elastin-laminin receptor
    • J. Labat-Robert, and L. Robert Interaction between cells and extracellular matrix: signaling by integrins and the elastin-laminin receptor Prog Mol Subcell Biol 25 2000 57 70
    • (2000) Prog Mol Subcell Biol , vol.25 , pp. 57-70
    • Labat-Robert, J.1    Robert, L.2
  • 16
    • 0026782355 scopus 로고
    • The disulfide bridge pattern of snake venom disintegrins, flavoridin and echistatin
    • J.J. Calvete, Y. Wang, K. Mann, W. Schafer, S. Niewiarowski, and G.J. Stewart The disulfide bridge pattern of snake venom disintegrins, flavoridin and echistatin FEBS Lett 309 1992 316 320
    • (1992) FEBS Lett , vol.309 , pp. 316-320
    • Calvete, J.J.1    Wang, Y.2    Mann, K.3    Schafer, W.4    Niewiarowski, S.5    Stewart, G.J.6
  • 17
    • 0034678129 scopus 로고    scopus 로고
    • Signal-transducing mechanisms involved in activation of the platelet collagen receptor integrin alpha(2)beta(1)
    • S.M. Jung, and M. Moroi Signal-transducing mechanisms involved in activation of the platelet collagen receptor integrin alpha(2)beta(1) J Biol Chem 275 2000 8016 8026
    • (2000) J Biol Chem , vol.275 , pp. 8016-8026
    • Jung, S.M.1    Moroi, M.2
  • 18
    • 0019904296 scopus 로고
    • Optimal conditions for prolidase assay by proline colorimetric determination: Application to imidodipeptiduria
    • I. Myara, C. Charpentier, and A. Lemonnier Optimal conditions for prolidase assay by proline colorimetric determination: application to imidodipeptiduria Clin Chim Acta 125 1982 193 205
    • (1982) Clin Chim Acta , vol.125 , pp. 193-205
    • Myara, I.1    Charpentier, C.2    Lemonnier, A.3
  • 20
    • 0025060724 scopus 로고
    • Scorbutic and fasted guinea pig sera contain an insulin-like growth factor-I reversible inhibitor of proteoglycan and collagen synthesis in chick embryo chondrocytes and adult human skin fibroblasts
    • I. Oyamada, J. Pałka, E.M. Schalk, K. Takeda, and B. Peterkofsky Scorbutic and fasted guinea pig sera contain an insulin-like growth factor-I reversible inhibitor of proteoglycan and collagen synthesis in chick embryo chondrocytes and adult human skin fibroblasts Arch Biochem Biophys 276 1990 85 93
    • (1990) Arch Biochem Biophys , vol.276 , pp. 85-93
    • Oyamada, I.1    Pałka, J.2    Schalk, E.M.3    Takeda, K.4    Peterkofsky, B.5
  • 21
    • 0025878450 scopus 로고
    • Elevated activity of low molecular weight insulin-like growth factor-binding proteins in sera of vitamin C-deficient and fasted guinea pigs
    • B. Peterkofsky, J. Pałka, S. Wilson, K. Takeda, and V. Shah Elevated activity of low molecular weight insulin-like growth factor-binding proteins in sera of vitamin C-deficient and fasted guinea pigs Endocrinology 128 1991 1769 1779
    • (1991) Endocrinology , vol.128 , pp. 1769-1779
    • Peterkofsky, B.1    Pałka, J.2    Wilson, S.3    Takeda, K.4    Shah, V.5
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 2642570379 scopus 로고
    • Prolidase activity is regulated by cell surface extracellular matrix interaction in normal fibroblast and MCF-7 cells
    • J.A. Pałka, and J.M. Phang Prolidase activity is regulated by cell surface extracellular matrix interaction in normal fibroblast and MCF-7 cells Proc Am Assoc Cancer Res 35 1994 531
    • (1994) Proc Am Assoc Cancer Res , vol.35 , pp. 531
    • Pałka, J.A.1    Phang, J.M.2
  • 25
    • 0025978352 scopus 로고
    • Control of growth and differentiation of vascular cells by extracellular matrix
    • D.J. Carey Control of growth and differentiation of vascular cells by extracellular matrix Ann Rev Physiol 53 1991 161 177
    • (1991) Ann Rev Physiol , vol.53 , pp. 161-177
    • Carey, D.J.1
  • 26
    • 0026903388 scopus 로고
    • Control of cell motility and tumor invasion by extracellular matrix interaction
    • E. Ruoslahti Control of cell motility and tumor invasion by extracellular matrix interaction Br J Cancer 66 1992 239 242
    • (1992) Br J Cancer , vol.66 , pp. 239-242
    • Ruoslahti, E.1
  • 27
    • 0032721665 scopus 로고    scopus 로고
    • Role of integrins in cancer: Survey of expression patterns
    • G.J. Mizejewski Role of integrins in cancer: survey of expression patterns Proc Soc Exp Biol Med 222 1999 124 138
    • (1999) Proc Soc Exp Biol Med , vol.222 , pp. 124-138
    • Mizejewski, G.J.1
  • 28
    • 0033980343 scopus 로고    scopus 로고
    • Snake venom modulators of platelet adhesion receptors and their ligands
    • R.K. Andrews, and M.C. Berndt Snake venom modulators of platelet adhesion receptors and their ligands Toxicon 38 2000 775 791
    • (2000) Toxicon , vol.38 , pp. 775-791
    • Andrews, R.K.1    Berndt, M.C.2
  • 29
    • 0031897532 scopus 로고    scopus 로고
    • Contortrostatin, a homodimeric snake venom disintegrin, is a potent inhibitor of osteoclast attachment
    • B. Mercer, F. Markland, and C. Minkin Contortrostatin, a homodimeric snake venom disintegrin, is a potent inhibitor of osteoclast attachment J Bone Miner Res 13 1998 409 414
    • (1998) J Bone Miner Res , vol.13 , pp. 409-414
    • Mercer, B.1    Markland, F.2    Minkin, C.3
  • 33
    • 0023684353 scopus 로고
    • Regulation of thrombin generation and functions
    • J.W. Fenton II Regulation of thrombin generation and functions Semin Thromb Hemost 14 1988 234 240
    • (1988) Semin Thromb Hemost , vol.14 , pp. 234-240
    • Fenton II, J.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.