메뉴 건너뛰기




Volumn 285, Issue 6 54-6, 2003, Pages

Fibroblast fiber contraction: Role of C and Rho kinase in activation by thromboxane A2

Author keywords

Collagen matrix; Signal transduction; Wound repair

Indexed keywords

1 [N,O BIS(5 ISOQUINOLINESULFONYL) N METHYLTYROSYL] 4 PHENYLPIPERAZINE; 12 (2 CYANOETHYL) 6,7,12,13 TETRAHYDRO 13 METHYL 5 OXOINDOLO[2,3 A]PYRROLO[3,4 C]CARBAZOLE; 15 HYDROXY 11ALPHA,9ALPHA EPOXYMETHANOPROSTA 5,13 DIENOIC ACID; 4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; 7 [3 [(4 PHENYLSEMICARBAZIDO)METHYL] 7 OXABICYCLO[2.2.1]HEPT 2 YL] 5 HEPTENOIC ACID; CALCIUM ION; CALPHOSTIN C; CYCLOPIAZONIC ACID; CYTOCHALASIN D; GROWTH FACTOR; N (6 AMINOHEXYL) 5 CHLORO 1 NAPHTHALENESULFONAMIDE; NEUROTRANSMITTER; PHOSPHOLIPID; PROTEIN KINASE C; RHO KINASE; RHO KINASE INHIBITOR; THROMBOXANE A2; THROMBOXANE A2 DERIVATIVE; THROMBOXANE A2 RECEPTOR BLOCKING AGENT; UNCLASSIFIED DRUG;

EID: 0242510041     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.00067.2003     Document Type: Article
Times cited : (4)

References (34)
  • 1
    • 0030460491 scopus 로고    scopus 로고
    • Platelet prostanoid receptors
    • Armstrong RA. Platelet prostanoid receptors. Pharmacol Ther 72: 171-191, 1996.
    • (1996) Pharmacol Ther , vol.72 , pp. 171-191
    • Armstrong, R.A.1
  • 3
    • 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, and 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 76: 1274-1278, 1979.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 1274-1278
    • Bell, E.1    Ivarsson, B.2    Merrill, C.3
  • 4
    • 0026496905 scopus 로고
    • Dissociation of the contractile and hypertrophic effects of vasoconstrictor prostanoids in vascular smooth muscle
    • Dorn GW, Becker MW, and Davis MG. Dissociation of the contractile and hypertrophic effects of vasoconstrictor prostanoids in vascular smooth muscle. J Biol Chem 267: 24897-24905, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 24897-24905
    • Dorn, G.W.1    Becker, M.W.2    Davis, M.G.3
  • 5
    • 0033773756 scopus 로고    scopus 로고
    • Differences in the mechanism for high- versus moderate-density fibroblast-populated collagen lattice contraction
    • Ehrlich HP and Rittenberg T. Differences in the mechanism for high- versus moderate-density fibroblast-populated collagen lattice contraction. J Cell Physiol 185: 432-439, 2000.
    • (2000) J Cell Physiol , vol.185 , pp. 432-439
    • Ehrlich, H.P.1    Rittenberg, T.2
  • 6
    • 0034285081 scopus 로고    scopus 로고
    • Fibroblast-collagen-matrix contraction: Growth-factor signalling and mechanical loading
    • Grinnell F. Fibroblast-collagen-matrix contraction: growth-factor signalling and mechanical loading. Trends Cell Biol 10: 362-365, 2000.
    • (2000) Trends Cell Biol , vol.10 , pp. 362-365
    • Grinnell, F.1
  • 7
    • 0033534684 scopus 로고    scopus 로고
    • Differences in the regulation of fibroblast contraction of floating versus stressed collagen matrices
    • Grinnell F, Ho CH, Lin YC, and Skuta G. Differences in the regulation of fibroblast contraction of floating versus stressed collagen matrices. J Biol Chem 274: 918-923, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 918-923
    • Grinnell, F.1    Ho, C.H.2    Lin, Y.C.3    Skuta, G.4
  • 8
    • 0021895138 scopus 로고
    • 2+ indicators with greatly improved fluorescence properties
    • 2+ indicators with greatly improved fluorescence properties. J Biol Chem 260: 3440-3450, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 9
    • 0028012779 scopus 로고
    • Elongation factor-2 kinase: Effective inhibition by the novel protein kinase inhibitor rottlerin and relative insensitivity towards staurosporine
    • Gschwendt M, Kittstein W, and Marks F. Elongation factor-2 kinase: effective inhibition by the novel protein kinase inhibitor rottlerin and relative insensitivity towards staurosporine. FEBS Lett 338: 85-88, 1994.
    • (1994) FEBS Lett , vol.338 , pp. 85-88
    • Gschwendt, M.1    Kittstein, W.2    Marks, F.3
  • 10
    • 0016748441 scopus 로고
    • Thromboxanes: A new group of biologically active compounds derived from prostaglandin endoperoxides
    • Hamberg M, Svensson J, and Samuelsson B. Thromboxanes: a new group of biologically active compounds derived from prostaglandin endoperoxides. Proc Natl Acad Sci USA 72: 2994-2998, 1975.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 2994-2998
    • Hamberg, M.1    Svensson, J.2    Samuelsson, B.3
  • 11
    • 0024550448 scopus 로고
    • Calphostin C (UCN-1028C), a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C
    • Kobayashi E, Nakano H, Morimoto M, and Tamaoki T. Calphostin C (UCN-1028C), a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C. Biochem Biophys Res Commun 159: 548-553, 1989.
    • (1989) Biochem Biophys Res Commun , vol.159 , pp. 548-553
    • Kobayashi, E.1    Nakano, H.2    Morimoto, M.3    Tamaoki, T.4
  • 12
    • 0027435246 scopus 로고
    • Correlation of myosin light chain phosphorylation with isometric contraction of fibroblasts
    • Kolodney MS and Elson EL. Correlation of myosin light chain phosphorylation with isometric contraction of fibroblasts. J Biol Chem 268: 23850-23855, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 23850-23855
    • Kolodney, M.S.1    Elson, E.L.2
  • 13
    • 0026519128 scopus 로고
    • Isometric contraction by fibroblasts and endothelial cells in tissue culture: A quantitative study
    • Kolodney MS and Wysolmerski RB. Isometric contraction by fibroblasts and endothelial cells in tissue culture: a quantitative study. J Cell Biol 117: 73-82, 1992.
    • (1992) J Cell Biol , vol.117 , pp. 73-82
    • Kolodney, M.S.1    Wysolmerski, R.B.2
  • 14
    • 0030934532 scopus 로고    scopus 로고
    • Wound healing-aiming for perfect skin regeneration
    • Martin P. Wound healing-aiming for perfect skin regeneration. Science 276: 75-81, 1997.
    • (1997) Science , vol.276 , pp. 75-81
    • Martin, P.1
  • 17
    • 0024043131 scopus 로고
    • Transforming growth factor-β stimulates collagen-matrix contraction by fibroblasts: Implications for wound healing
    • Montesano R and Orci L. Transforming growth factor-β stimulates collagen-matrix contraction by fibroblasts: implications for wound healing. Proc Natl Acad Sci USA 85: 4894-4897, 1988.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4894-4897
    • Montesano, R.1    Orci, L.2
  • 18
    • 0032823306 scopus 로고    scopus 로고
    • Prostanoid receptors: Structures, properties, and functions
    • Narumiya S, Sugimoto Y, and Ushikubi F. Prostanoid receptors: structures, properties, and functions. Physiol Rev 79: 1193-1226, 1999.
    • (1999) Physiol Rev , vol.79 , pp. 1193-1226
    • Narumiya, S.1    Sugimoto, Y.2    Ushikubi, F.3
  • 20
    • 0034671202 scopus 로고    scopus 로고
    • 2+ stores in regulation of isometric force in NIH 3T3 fibroblast fibres
    • 2+ stores in regulation of isometric force in NIH 3T3 fibroblast fibres. J Physiol 529: 669-679, 2000.
    • (2000) J Physiol , vol.529 , pp. 669-679
    • Nobe, K.1    Nobe, H.2    Obara, K.3    Paul, R.J.4
  • 21
    • 0029099125 scopus 로고
    • Fibroblast contractility without an increase in basal myosin light chain phosphorylation in wild-type cells and cells expressing the catalytic domain of myosin light chain kinase
    • Obara K, Nikcevic G, Pestic L, Nowak G, Lorimer DD, Guerriero V Jr, Elson EL, Paul RJ, and de Lanerolle P. Fibroblast contractility without an increase in basal myosin light chain phosphorylation in wild-type cells and cells expressing the catalytic domain of myosin light chain kinase. J Biol Chem 270: 18734-18737, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 18734-18737
    • Obara, K.1    Nikcevic, G.2    Pestic, L.3    Nowak, G.4    Lorimer, D.D.5    Guerriero Jr., V.6    Elson, E.L.7    Paul, R.J.8    De Lanerolle, P.9
  • 23
    • 0034141607 scopus 로고    scopus 로고
    • Regulation of LPA-promoted myofibroblast contraction: Role of Rho, myosin light chain kinase, and myosin light chain phosphatase
    • Parizi M, Howard EW, and Tomasek JJ. Regulation of LPA-promoted myofibroblast contraction: role of Rho, myosin light chain kinase, and myosin light chain phosphatase. Exp Cell Res 254: 210-220, 2000.
    • (2000) Exp Cell Res , vol.254 , pp. 210-220
    • Parizi, M.1    Howard, E.W.2    Tomasek, J.J.3
  • 24
    • 0023604648 scopus 로고
    • Calcium in the regulation of aldosterone secretion and vascular smooth muscle contraction
    • Rasmussen H, Barrett P, Takuwa Y, and Apfeldorf W. Calcium in the regulation of aldosterone secretion and vascular smooth muscle contraction. Hypertension 10: 123-126, 1987.
    • (1987) Hypertension , vol.10 , pp. 123-126
    • Rasmussen, H.1    Barrett, P.2    Takuwa, Y.3    Apfeldorf, W.4
  • 25
    • 0028321785 scopus 로고
    • Signal transduction pathways regulating Rho-mediated stress fibre formation: Requirement for a tyrosine kinase
    • Ridley AJ and Hall A. Signal transduction pathways regulating Rho-mediated stress fibre formation: requirement for a tyrosine kinase. EMBO J 13: 2600-2610, 1994.
    • (1994) EMBO J , vol.13 , pp. 2600-2610
    • Ridley, A.J.1    Hall, A.2
  • 26
    • 0023644877 scopus 로고
    • Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase
    • Saitoh M, Ishikawa T, Matsushima S, Naka M, and Hidaka H. Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase. J Biol Chem 262: 7796-7801, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 7796-7801
    • Saitoh, M.1    Ishikawa, T.2    Matsushima, S.3    Naka, M.4    Hidaka, H.5
  • 28
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • Somlyo AP and Somlyo AV. Signal transduction and regulation in smooth muscle. Nature 372: 231-236, 1994. [Corrigenda. Nature 372: December 1994, p. 812]
    • (1994) Nature , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 29
    • 0028043535 scopus 로고
    • Corrigenda
    • December
    • Somlyo AP and Somlyo AV. Signal transduction and regulation in smooth muscle. Nature 372: 231-236, 1994. [Corrigenda. Nature 372: December 1994, p. 812]
    • (1994) Nature , vol.372 , pp. 812
  • 30
    • 0035834439 scopus 로고    scopus 로고
    • Effects of lactoferrin on collagen gel contractile activity and myosin light chain phosphorylation in human fibroblasts
    • Takayama Y and Mizumachi K. Effects of lactoferrin on collagen gel contractile activity and myosin light chain phosphorylation in human fibroblasts. FEBS Lett 508: 111-116, 2001.
    • (2001) FEBS Lett , vol.508 , pp. 111-116
    • Takayama, Y.1    Mizumachi, K.2
  • 31
    • 0019940315 scopus 로고
    • Two types of calcium-dependent protein phosphorylations modulated by calmodulin antagonists. Naphthalenesulfonamide derivatives
    • Tanaka T, Ohmura T, Yamakado T, and Hidaka H. Two types of calcium-dependent protein phosphorylations modulated by calmodulin antagonists. Naphthalenesulfonamide derivatives. Mol Pharmacol 22: 408-412, 1982.
    • (1982) Mol Pharmacol , vol.22 , pp. 408-412
    • Tanaka, T.1    Ohmura, T.2    Yamakado, T.3    Hidaka, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.