메뉴 건너뛰기




Volumn 163, Issue 3, 2003, Pages 1045-1056

Vascular smooth muscle cells orchestrate the assembly of type I collagen via α2β1 integrin, RhoA, and fibronectin polymerization

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA5 INTEGRIN; BETA1 INTEGRIN; COLLAGEN TYPE 1; COMPLEMENTARY DNA; FIBRONECTIN; LYSOPHOSPHATIDIC ACID; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 0041924762     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0002-9440(10)63464-5     Document Type: Article
Times cited : (142)

References (42)
  • 1
    • 0020691997 scopus 로고
    • Germline integration of Moloney murine leukemia virus at the Mov13 locus leads to recessive lethal mutation and early embryonic death
    • Jaenisch R, Harbers K, Schnieke A, Lohler J, Chumakov I, Jahner D, Grotkopp D, Hoffmann E: Germline integration of Moloney murine leukemia virus at the Mov13 locus leads to recessive lethal mutation and early embryonic death. Cell 1983, 32:209-216
    • (1983) Cell , vol.32 , pp. 209-216
    • Jaenisch, R.1    Harbers, K.2    Schnieke, A.3    Lohler, J.4    Chumakov, I.5    Jahner, D.6    Grotkopp, D.7    Hoffmann, E.8
  • 2
    • 0021752455 scopus 로고
    • Retrovirus-induced lethal mutation in collagen I gene of mice is associated with an altered chromatin structure
    • Breindl M, Harbers K, Jaenisch R: Retrovirus-induced lethal mutation in collagen I gene of mice is associated with an altered chromatin structure Cell 1984, 38:9-16
    • (1984) Cell , vol.38 , pp. 9-16
    • Breindl, M.1    Harbers, K.2    Jaenisch, R.3
  • 5
    • 0001472055 scopus 로고
    • Heat precipitation of collagen from neutral salt solutions: Some rate regulating factors
    • Gross J, Kirk D: Heat precipitation of collagen from neutral salt solutions: some rate regulating factors. J Biol Chem 1958, 233:355-360
    • (1958) J Biol Chem , vol.233 , pp. 355-360
    • Gross, J.1    Kirk, D.2
  • 6
    • 0013771738 scopus 로고
    • The precipitation of collagen fibers from solution
    • Wood GC: The precipitation of collagen fibers from solution. Int Rev Connect Tissue Res 1964, 2:1-31
    • (1964) Int Rev Connect Tissue Res , vol.2 , pp. 1-31
    • Wood, G.C.1
  • 7
    • 0018079235 scopus 로고
    • Collagen fibril formation. Optimal in vitro conditions and preliminary kinetic results
    • Williams BR, Gelman RA, Poppke DC, Piez KA: Collagen fibril formation. Optimal in vitro conditions and preliminary kinetic results. J Biol Chem 1978, 253:6578-6585
    • (1978) J Biol Chem , vol.253 , pp. 6578-6585
    • Williams, B.R.1    Gelman, R.A.2    Poppke, D.C.3    Piez, K.A.4
  • 8
    • 0020402498 scopus 로고
    • Formation of collagen fibrils in vitro by cleavage of procollagen with procollagen proteinases
    • Miyahara M, Njieha FK, Prockop DJ: Formation of collagen fibrils in vitro by cleavage of procollagen with procollagen proteinases. J Biol Chem 1982, 257:8442-8448
    • (1982) J Biol Chem , vol.257 , pp. 8442-8448
    • Miyahara, M.1    Njieha, F.K.2    Prockop, D.J.3
  • 9
    • 0023656926 scopus 로고
    • Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen Cproteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process
    • Kadler KE, Hojima Y, Prockop DJ: Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen Cproteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process. J Biol Chem 1987, 262:15696-15701
    • (1987) J Biol Chem , vol.262 , pp. 15696-15701
    • Kadler, K.E.1    Hojima, Y.2    Prockop, D.J.3
  • 10
    • 0028158454 scopus 로고
    • Vertebrate (chick) collagen fibrils formed in vivo can exhibit a reversal in molecular polarity
    • Holmes DF, Lowe MP, Chapman JA: Vertebrate (chick) collagen fibrils formed in vivo can exhibit a reversal in molecular polarity. J Mol Biol 1994, 235:80-83
    • (1994) J Mol Biol , vol.235 , pp. 80-83
    • Holmes, D.F.1    Lowe, M.P.2    Chapman, J.A.3
  • 11
    • 0032546947 scopus 로고    scopus 로고
    • Inhibition of the self-assembly of collagen I into fibrils with synthetic peptides Demonstration that assembly is driven by specific binding sites on the monomers
    • Prockop DJ, Fertala A: Inhibition of the self-assembly of collagen I into fibrils with synthetic peptides Demonstration that assembly is driven by specific binding sites on the monomers. J Biol Chem 1998, 273: 15598-15604
    • (1998) J Biol Chem , vol.273 , pp. 15598-15604
    • Prockop, D.J.1    Fertala, A.2
  • 12
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • Danielson KG, Baribault H, Holmes DF, Graham H, Kadler KE, Iozzo RV: Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J Cell Biol 1997, 136:729-743
    • (1997) J Cell Biol , vol.136 , pp. 729-743
    • Danielson, K.G.1    Baribault, H.2    Holmes, D.F.3    Graham, H.4    Kadler, K.E.5    Iozzo, R.V.6
  • 13
    • 0032101311 scopus 로고    scopus 로고
    • Lumican regulates collagen fibril assembly: Skin fragility and corneal opacity in the absence of lumican
    • Chakravarti S, Magnuson T, Lass JH, Jepsen KJ, LaMantia C, Carroll H: Lumican regulates collagen fibril assembly: skin fragility and corneal opacity in the absence of lumican. J Cell Biol 1998, 141:1277-1286
    • (1998) J Cell Biol , vol.141 , pp. 1277-1286
    • Chakravarti, S.1    Magnuson, T.2    Lass, J.H.3    Jepsen, K.J.4    LaMantia, C.5    Carroll, H.6
  • 14
    • 0040436000 scopus 로고    scopus 로고
    • Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon
    • Svensson L, Aszodi A, Reinholt FP, Fassler R, Heinegard D, Oldberg A: Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon. J Biol Chem 1999, 274:9636-9647
    • (1999) J Biol Chem , vol.274 , pp. 9636-9647
    • Svensson, L.1    Aszodi, A.2    Reinholt, F.P.3    Fassler, R.4    Heinegard, D.5    Oldberg, A.6
  • 15
    • 0036796746 scopus 로고    scopus 로고
    • Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions
    • Sottile J, Hocking DC: Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions. Mol Biol Cell 2002, 13:3546-3559
    • (2002) Mol Biol Cell , vol.13 , pp. 3546-3559
    • Sottile, J.1    Hocking, D.C.2
  • 16
    • 0028786294 scopus 로고
    • Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix
    • Wu C, Keivens VM, O'Toole TE, McDonald J, Ginsberg MH: Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix. Cell 1995, 83:715-724
    • (1995) Cell , vol.83 , pp. 715-724
    • Wu, C.1    Keivens, V.M.2    O'Toole, T.E.3    McDonald, J.4    Ginsberg, M.H.5
  • 17
    • 0032869760 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis: A paradigm for extracellular matrix assembly
    • Schwarzbauer JE, Sechler JL: Fibronectin fibrillogenesis: a paradigm for extracellular matrix assembly. Curr Opin Cell Biol 1999, 11:622-627
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 622-627
    • Schwarzbauer, J.E.1    Sechler, J.L.2
  • 18
    • 0028955624 scopus 로고
    • Integrin-mediated collagen matrix reorganization by cultured human vascular smooth muscle cells
    • Lee RT, Berditchevski F, Cheng GC, Hemler ME: Integrin-mediated collagen matrix reorganization by cultured human vascular smooth muscle cells. Circ Res 1995, 76:209-214
    • (1995) Circ Res , vol.76 , pp. 209-214
    • Lee, R.T.1    Berditchevski, F.2    Cheng, G.C.3    Hemler, M.E.4
  • 19
    • 0027476105 scopus 로고
    • Prevention of smooth muscle cell outgrowth from human atherosclerotic plaque by a recombinant fusion protein specific for the epidermal growth factor receptor
    • Pickering JG, Bacha P, Weir L, Jekanowski J, Nichols JC, Isner JM: Prevention of smooth muscle cell outgrowth from human atherosclerotic plaque by a recombinant fusion protein specific for the epidermal growth factor receptor. J Clin Invest 1993, 91:724-729
    • (1993) J Clin Invest , vol.91 , pp. 724-729
    • Pickering, J.G.1    Bacha, P.2    Weir, L.3    Jekanowski, J.4    Nichols, J.C.5    Isner, J.M.6
  • 20
    • 0001297636 scopus 로고
    • Production of a tissue-like structure by contraction of collagen lattices by human fibroblasts of different proliferative potential in vitro
    • Bell E, Ivarsson B, Merrill C: Production of a tissue-like structure by contraction of collagen lattices by human fibroblasts of different proliferative potential in vitro. Proc Natl Acad Sci USA 1979, 76:1274-1278
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 1274-1278
    • Bell, E.1    Ivarsson, B.2    Merrill, C.3
  • 22
    • 0030772436 scopus 로고    scopus 로고
    • Modulation of in vivo migratory function of alpha 2 beta 1 integrin in mouse liver
    • Ho WC, Heinemann C, Hangan D, Uniyal S, Morris VL, Chan BM: Modulation of in vivo migratory function of alpha 2 beta 1 integrin in mouse liver. Mol Biol Cell 1997, 8:1863-1875
    • (1997) Mol Biol Cell , vol.8 , pp. 1863-1875
    • Ho, W.C.1    Heinemann, C.2    Hangan, D.3    Uniyal, S.4    Morris, V.L.5    Chan, B.M.6
  • 23
    • 0033621952 scopus 로고    scopus 로고
    • α5β1 integrin expression and luminal edge fibronectin matrix assembly by smooth muscle cells after arterial injury
    • Pickering JG, Chow LH, Li S, Rogers KA, Rocnik EF, Zhong R, Chan BM: α5β1 integrin expression and luminal edge fibronectin matrix assembly by smooth muscle cells after arterial injury. Am J Pathol 2000, 156:453-465
    • (2000) Am J Pathol , vol.156 , pp. 453-465
    • Pickering, J.G.1    Chow, L.H.2    Li, S.3    Rogers, K.A.4    Rocnik, E.F.5    Zhong, R.6    Chan, B.M.7
  • 24
    • 0028820587 scopus 로고
    • Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pakl
    • Zhang S, Han J, Sells MA, Chernoff J, Knaus UG, Ulevitch RJ, Bokoch GM: Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pakl. J Biol Chem 1995, 270:23934-23936
    • (1995) J Biol Chem , vol.270 , pp. 23934-23936
    • Zhang, S.1    Han, J.2    Sells, M.A.3    Chernoff, J.4    Knaus, U.G.5    Ulevitch, R.J.6    Bokoch, G.M.7
  • 25
    • 0027236954 scopus 로고
    • Production of high-titer helper-free retroviruses by transient transfection
    • Pear WS, Nolan GP, Scott ML, Baltimore D: Production of high-titer helper-free retroviruses by transient transfection. Proc Natl Acad Sci USA 1993, 90:8392-8396
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8392-8396
    • Pear, W.S.1    Nolan, G.P.2    Scott, M.L.3    Baltimore, D.4
  • 26
    • 0031834932 scopus 로고    scopus 로고
    • Fibrous long spacing collagen ultrastructure elucidated by atomic force microscopy
    • Paige MF, Rainey JK, Goh MC: Fibrous long spacing collagen ultrastructure elucidated by atomic force microscopy. Biophys J 1998, 74:3211-3216
    • (1998) Biophys J , vol.74 , pp. 3211-3216
    • Paige, M.F.1    Rainey, J.K.2    Goh, M.C.3
  • 27
    • 0030994656 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 potentiates vascular smooth muscle cell migration to platelet-derived growth factor: Upregulation of α2β1 integrin and disassembly of actin filaments
    • Pickering JG, Uniyal S, Ford C, Chau T, Laurin MA, Chow LH, Ellis CG, Fish J. Chan BMC: Fibroblast growth factor-2 potentiates vascular smooth muscle cell migration to platelet-derived growth factor: upregulation of α2β1 integrin and disassembly of actin filaments. Circ Res 1997, 80:627-637
    • (1997) Circ Res , vol.80 , pp. 627-637
    • Pickering, J.G.1    Uniyal, S.2    Ford, C.3    Chau, T.4    Laurin, M.A.5    Chow, L.H.6    Ellis, C.G.7    Fish, J.8    Chan, B.M.C.9
  • 28
    • 0019215417 scopus 로고
    • Fibronectin presence in native collagen fibrils of human fibroblasts: Immunoperoxidase and immunoferritin localization
    • Furcht LT, Smith D, Wendelschafer-Crabb G, Mosher DF, Foidart JM: Fibronectin presence in native collagen fibrils of human fibroblasts: immunoperoxidase and immunoferritin localization. J Histochem Cytochem 1980, 28:1319-1333
    • (1980) J Histochem Cytochem , vol.28 , pp. 1319-1333
    • Furcht, L.T.1    Smith, D.2    Wendelschafer-Crabb, G.3    Mosher, D.F.4    Foidart, J.M.5
  • 29
    • 0027422170 scopus 로고
    • The alpha 5 beta 1 integrin fibronectin receptor, but not the alpha 5 cytoplasmic domain, functions in an early and essential step in fibronectin matrix assembly
    • Wu C, Bauer JS, Juliano RL, McDonald JA: The alpha 5 beta 1 integrin fibronectin receptor, but not the alpha 5 cytoplasmic domain, functions in an early and essential step in fibronectin matrix assembly. J Biol Chem 1993, 268:21883-21888
    • (1993) J Biol Chem , vol.268 , pp. 21883-21888
    • Wu, C.1    Bauer, J.S.2    Juliano, R.L.3    McDonald, J.A.4
  • 30
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A: Rho GTPases and the actin cytoskeleton. Science 1998, 279:509-514
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 31
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley AJ, Hall A: The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 1992, 70:389-399
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 32
    • 0031309902 scopus 로고    scopus 로고
    • The discoiding domain receptor tyrosine kinases are activated by collagen
    • Vogel W, Gisg GD, Alves F, Pawson T: The discoiding domain receptor tyrosine kinases are activated by collagen. Mol Cell 1997, 1:13-23
    • (1997) Mol Cell , vol.1 , pp. 13-23
    • Vogel, W.1    Gisg, G.D.2    Alves, F.3    Pawson, T.4
  • 33
    • 0022470549 scopus 로고
    • Extracellular compartments in tendon morphogenesis: Collagen fibril, bundle, and macroaggregate formation
    • Birk DE, Trelstad RL: Extracellular compartments in tendon morphogenesis: collagen fibril, bundle, and macroaggregate formation. J Cell Biol 1986, 103:231-240
    • (1986) J Cell Biol , vol.103 , pp. 231-240
    • Birk, D.E.1    Trelstad, R.L.2
  • 34
    • 0029585289 scopus 로고
    • Collagen and collagenase gene expression in three-dimensional collagen lattices are differentially regulated by α1β1 and α2β1 integrins
    • Langholz O, Rockel D, Mauch C, Kozlowska E, Bank I, Krieg T: Collagen and collagenase gene expression in three-dimensional collagen lattices are differentially regulated by α1β1 and α2β1 integrins. J Cell Biol 1995, 131:1903-1915
    • (1995) J Cell Biol , vol.131 , pp. 1903-1915
    • Langholz, O.1    Rockel, D.2    Mauch, C.3    Kozlowska, E.4    Bank, I.5    Krieg, T.6
  • 35
    • 0025880917 scopus 로고
    • Integrin α2β1 is upregulated in fibroblasts and highly aggressive melanoma cells in three-dimensional collagen lattices and mediates the reorganization of collagen I fibrils
    • Klein CE, Dressel D, Steinmayer T, Mauch C, Eckes B, Krieg T, Bankert RB, Weber L: Integrin α2β1 is upregulated in fibroblasts and highly aggressive melanoma cells in three-dimensional collagen lattices and mediates the reorganization of collagen I fibrils. J Cell Biol 1991, 115:1427-1436
    • (1991) J Cell Biol , vol.115 , pp. 1427-1436
    • Klein, C.E.1    Dressel, D.2    Steinmayer, T.3    Mauch, C.4    Eckes, B.5    Krieg, T.6    Bankert, R.B.7    Weber, L.8
  • 36
    • 0037020239 scopus 로고    scopus 로고
    • Polymerization of type I and III collagens is dependent on fibronectin and enhanced by integrins a11,β1 and α2,β1
    • Velling T, Risteli J, Krister W, Mosher DF, Johansson S: Polymerization of type I and III collagens is dependent on fibronectin and enhanced by integrins a11,β1 and α2,β1. J Biol Chem 2002, 277:37377-37381
    • (2002) J Biol Chem , vol.277 , pp. 37377-37381
    • Velling, T.1    Risteli, J.2    Krister, W.3    Mosher, D.F.4    Johansson, S.5
  • 37
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong C, Chrzanowska-Wodnicka M, Brown J, Shaub A, Belkin AM, Burridge K: Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J Cell Biol 1998, 141:539-551
    • (1998) J Cell Biol , vol.141 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.M.5    Burridge, K.6
  • 38
    • 0030928057 scopus 로고    scopus 로고
    • Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through Rho-dependent actin stress fiber formation and cell contraction
    • Zhang Q, Magnusson MK, Mosher DF: Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through Rho-dependent actin stress fiber formation and cell contraction. Mol Biol Cell 1997, 8:1415-1425
    • (1997) Mol Biol Cell , vol.8 , pp. 1415-1425
    • Zhang, Q.1    Magnusson, M.K.2    Mosher, D.F.3
  • 40
    • 0030587234 scopus 로고    scopus 로고
    • Evidence for rapid accumulation and persistently disordered architecture of fibrillar collagen in human coronary restenosis lesions
    • Pickering JG, Ford CM, Chow LH: Evidence for rapid accumulation and persistently disordered architecture of fibrillar collagen in human coronary restenosis lesions. Am J Cardiol 1996, 78:633-637
    • (1996) Am J Cardiol , vol.78 , pp. 633-637
    • Pickering, J.G.1    Ford, C.M.2    Chow, L.H.3
  • 42
    • 0029054734 scopus 로고
    • Molecular basis of acute coronary syndromes
    • Libby P: Molecular basis of acute coronary syndromes. Circulation 1995, 91:2844-2850
    • (1995) Circulation , vol.91 , pp. 2844-2850
    • Libby, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.