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Volumn 23, Issue 2, 2003, Pages 238-243

Mast cell chymase induces smooth muscle cell apoptosis by a mechanism involving fibronectin degradation and disruption of focal adhesions

Author keywords

Apoptosis; Chymase; Focal adhesion kinase; Mast cell; Smooth muscle cell

Indexed keywords

CATHEPSIN G; CHYMASE; CHYMOTRYPSIN A; COMPOUND 48-80; ELASTASE; FIBRONECTIN; FOCAL ADHESION KINASE; INTEGRIN; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; SCLEROPROTEIN; TRYPSIN; VANADATE SODIUM;

EID: 0037324287     PISSN: 10795642     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.ATV.0000051405.68811.4D     Document Type: Article
Times cited : (106)

References (46)
  • 2
    • 0028903234 scopus 로고
    • Apoptosis of human vascular smooth muscle cells derived from normal vessels and coronary atherosclerotic plaques
    • Bennett MR, Evan GI, Schwartz SM. Apoptosis of human vascular smooth muscle cells derived from normal vessels and coronary atherosclerotic plaques. J Clin Invest. 1995;95:2266-2274.
    • (1995) J Clin Invest , vol.95 , pp. 2266-2274
    • Bennett, M.R.1    Evan, G.I.2    Schwartz, S.M.3
  • 3
  • 5
    • 0032537609 scopus 로고    scopus 로고
    • Apoptosis and related proteins in different stages of human atherosclerotic plaques
    • Kockx MM, De Meyer GRY, Muhring J, Jacob W, Bult H, Herman AG. Apoptosis and related proteins in different stages of human atherosclerotic plaques. Circulation. 1998;97:2307-2315.
    • (1998) Circulation , vol.97 , pp. 2307-2315
    • Kockx, M.M.1    De Meyer, G.R.Y.2    Muhring, J.3    Jacob, W.4    Bult, H.5    Herman, A.G.6
  • 6
    • 0030055903 scopus 로고    scopus 로고
    • Apoptosis is abundant in human atherosclerotic lesions, especially in inflammatory cells (macrophages and T cells), and may contribute to the accumulation of gruel and plaque instability
    • Björkerud S, Björkerud B. Apoptosis is abundant in human atherosclerotic lesions, especially in inflammatory cells (macrophages and T cells), and may contribute to the accumulation of gruel and plaque instability. Am J Pathol. 1996;149:367-380.
    • (1996) Am J Pathol , vol.149 , pp. 367-380
    • Björkerud, S.1    Björkerud, B.2
  • 7
    • 0028117853 scopus 로고
    • Accumulation of activated mast cells in the shoulder region of human coronary atheroma, the predilection site of atheromatous rupture
    • Kaartinen M, Penttilä A, Kovanen PT. Accumulation of activated mast cells in the shoulder region of human coronary atheroma, the predilection site of atheromatous rupture. Circulation. 1994;90:1669-1678.
    • (1994) Circulation , vol.90 , pp. 1669-1678
    • Kaartinen, M.1    Penttilä, A.2    Kovanen, P.T.3
  • 8
    • 0029165365 scopus 로고
    • Infiltrates of activated mast cells at the site of coronary atheromatous erosion of rupture in myocardial infarction
    • Kovanen PT, Kaartinen M, Paavonen T. Infiltrates of activated mast cells at the site of coronary atheromatous erosion of rupture in myocardial infarction. Circulation. 1995;92:1084-1088.
    • (1995) Circulation , vol.92 , pp. 1084-1088
    • Kovanen, P.T.1    Kaartinen, M.2    Paavonen, T.3
  • 11
    • 0031773610 scopus 로고    scopus 로고
    • Activation of matrix-degrading metalloproteinases by mast cell proteases in atherosclerotic plaques
    • Johnson JL, Jackson CL, Angelini GD, George SJ. Activation of matrix-degrading metalloproteinases by mast cell proteases in atherosclerotic plaques. Arterioscler Thromb Vasc Biol. 1998;18:1707-1715.
    • (1998) Arterioscler Thromb Vasc Biol , vol.18 , pp. 1707-1715
    • Johnson, J.L.1    Jackson, C.L.2    Angelini, G.D.3    George, S.J.4
  • 13
    • 0030971415 scopus 로고    scopus 로고
    • Regulation of local angiotensin II formation in the human heart in the presence of interstitial fluid. Inhibition of chymase by protease inhibitors of interstitial fluid and of angiotensin converting enzyme by Ang-(1-9) formed by heart carboxypeptidase A-like activity
    • Kokkonen JO, Saarinen J, Kovanen PT. Regulation of local angiotensin II formation in the human heart in the presence of interstitial fluid. Inhibition of chymase by protease inhibitors of interstitial fluid and of angiotensin converting enzyme by Ang-(1-9) formed by heart carboxypeptidase A-like activity. Circulation. 1997;95:1455-1463.
    • (1997) Circulation , vol.95 , pp. 1455-1463
    • Kokkonen, J.O.1    Saarinen, J.2    Kovanen, P.T.3
  • 14
    • 0029889948 scopus 로고    scopus 로고
    • Chymase in exocytosed rat mast cell granules effectively proteolyzes apolipoprotein A1-containing lipoproteins, so reducing the cholesterol efflux-inducing ability of serum and aortic intimal fluid
    • Lindstedt L, Lee M, Castro GR, Fruchart J, Kovanen PT. Chymase in exocytosed rat mast cell granules effectively proteolyzes apolipoprotein A1-containing lipoproteins, so reducing the cholesterol efflux-inducing ability of serum and aortic intimal fluid. J Clin Invest. 1996;97:2174-2182.
    • (1996) J Clin Invest , vol.97 , pp. 2174-2182
    • Lindstedt, L.1    Lee, M.2    Castro, G.R.3    Fruchart, J.4    Kovanen, P.T.5
  • 15
    • 0019876460 scopus 로고
    • Susceptibility of soluble and matrix fibronectins to degradation by tissue proteinases, mast cell chymase and cathepsin G
    • Vartio T, Seppa H, Vaheri A. Susceptibility of soluble and matrix fibronectins to degradation by tissue proteinases, mast cell chymase and cathepsin G. J Biol Chem. 1981;256:471-477.
    • (1981) J Biol Chem , vol.256 , pp. 471-477
    • Vartio, T.1    Seppa, H.2    Vaheri, A.3
  • 16
    • 0027082390 scopus 로고
    • The effect of mast cell chymase on extracellular matrix: Studies in autoimmune thyroiditis and in cultured thyroid cells
    • Banovac K, De Forteza R. The effect of mast cell chymase on extracellular matrix: studies in autoimmune thyroiditis and in cultured thyroid cells. Int Arch Allergy Immunol. 1992;99:141-149.
    • (1992) Int Arch Allergy Immunol , vol.99 , pp. 141-149
    • Banovac, K.1    De Forteza, R.2
  • 17
    • 0032547796 scopus 로고    scopus 로고
    • Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53-mediated apoptosis
    • Ilic D, Almeida EA, Schlaepfer DD, Dazin Aizawa S, Damsky CH. Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53-mediated apoptosis. J Cell Biol. 1998;143:547-560.
    • (1998) J Cell Biol , vol.143 , pp. 547-560
    • Ilic, D.1    Almeida, E.A.2    Schlaepfer, D.D.3    Dazin Aizawa, S.4    Damsky, C.H.5
  • 18
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch SM, Vuori K, Ruoslahti E, Chan-Hui PY. Control of adhesion-dependent cell survival by focal adhesion kinase. J Cell Biol. 1996;134: 793-799.
    • (1996) J Cell Biol , vol.134 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan-Hui, P.Y.4
  • 19
    • 0033594105 scopus 로고    scopus 로고
    • Extracellular matrix regulates apoptosis in mammary epithelium through a control on insulin signaling
    • Farrelly N, Lee YJ, Oliver J, Dive C, Streuli CH. Extracellular matrix regulates apoptosis in mammary epithelium through a control on insulin signaling. J Cell Biol. 1999;144:1337-1348.
    • (1999) J Cell Biol , vol.144 , pp. 1337-1348
    • Farrelly, N.1    Lee, Y.J.2    Oliver, J.3    Dive, C.4    Streuli, C.H.5
  • 21
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch SM, Francis H. Disruption of epithelial cell-matrix interactions induces apoptosis. J Cell Biol. 1994;124:619-626.
    • (1994) J Cell Biol , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 22
    • 0033593622 scopus 로고    scopus 로고
    • Heparin proteoglycans released from rat serosal mast cells inhibit proliferation of rat aortic smooth muscle cells in culture
    • Wang Y, Kovanen PT. Heparin proteoglycans released from rat serosal mast cells inhibit proliferation of rat aortic smooth muscle cells in culture. Circ Res. 1999;84:74-83.
    • (1999) Circ Res , vol.84 , pp. 74-83
    • Wang, Y.1    Kovanen, P.T.2
  • 23
    • 0024830821 scopus 로고
    • Heparin selectively inhibits a protein kinase C-dependent mechanism of cell cycle progression in calf aortic smooth muscle cells
    • Castellot JJ Jr, Pukac LA, Caleb BL, Wright TC Jr, Karnovsky MJ. Heparin selectively inhibits a protein kinase C-dependent mechanism of cell cycle progression in calf aortic smooth muscle cells. J Cell Biol. 1989;109: 3147-3155.
    • (1989) J Cell Biol , vol.109 , pp. 3147-3155
    • Castellot J.J., Jr.1    Pukac, L.A.2    Caleb, B.L.3    Wright T.C., Jr.4    Karnovsky, M.J.5
  • 24
    • 0022343901 scopus 로고
    • Low density lipoprotein degradation by rat mast cells: Demonstration of extracellular proteolysis caused by mast cell granules
    • Kokkonen JO, Kovanen PT. Low density lipoprotein degradation by rat mast cells: demonstration of extracellular proteolysis caused by mast cell granules. J Biol Chem. 1985;260:14756-14763.
    • (1985) J Biol Chem , vol.260 , pp. 14756-14763
    • Kokkonen, J.O.1    Kovanen, P.T.2
  • 25
    • 0034995590 scopus 로고    scopus 로고
    • Activation of paracrine TGF-beta1 signaling upon stimulation and degranulation of rat serosal mast cells: A novel function for chymase
    • Lindstedt KA, Wang Y, Shiota N, Saarinen J, Hyytiainen M, Kokkonen JO, Keski-Oja J, Kovanen PT. Activation of paracrine TGF-beta1 signaling upon stimulation and degranulation of rat serosal mast cells: a novel function for chymase. FASEB J. 2001;15:1377-1388.
    • (2001) FASEB J , vol.15 , pp. 1377-1388
    • Lindstedt, K.A.1    Wang, Y.2    Shiota, N.3    Saarinen, J.4    Hyytiainen, M.5    Kokkonen, J.O.6    Keski-Oja, J.7    Kovanen, P.T.8
  • 27
    • 0030795851 scopus 로고    scopus 로고
    • Disruption of integrin alpha 5 beta 1 signaling does not impair PDGF-BB-mediated stimulation of the extracellular signal-regulated kinase pathway in smooth muscle cells
    • Hedin UL, Daum G, Clowes AW. Disruption of integrin alpha 5 beta 1 signaling does not impair PDGF-BB-mediated stimulation of the extracellular signal-regulated kinase pathway in smooth muscle cells. J Cell Physiol. 1997;172:109-116.
    • (1997) J Cell Physiol , vol.172 , pp. 109-116
    • Hedin, U.L.1    Daum, G.2    Clowes, A.W.3
  • 29
    • 0029984473 scopus 로고    scopus 로고
    • Expression of the integrin alpha 5 subunit in HT29 colon carcinoma cells suppresses apoptosis triggered by serum deprivation
    • O'Brien V, Frisch SM, Juliano RL. Expression of the integrin alpha 5 subunit in HT29 colon carcinoma cells suppresses apoptosis triggered by serum deprivation. Exp Cell Res. 1996;224:208-213.
    • (1996) Exp Cell Res , vol.224 , pp. 208-213
    • O'Brien, V.1    Frisch, S.M.2    Juliano, R.L.3
  • 30
    • 0031596988 scopus 로고    scopus 로고
    • The alpha5beta1 integrin mediates elimination of amyloid-beta peptide and protects against apoptosis
    • Matter ML, Zhang Z, Nordstedt C, Ruoslahti E. The alpha5beta1 integrin mediates elimination of amyloid-beta peptide and protects against apoptosis. J Cell Biol. 1998;141:1019-1030.
    • (1998) J Cell Biol , vol.141 , pp. 1019-1030
    • Matter, M.L.1    Zhang, Z.2    Nordstedt, C.3    Ruoslahti, E.4
  • 32
    • 0035958902 scopus 로고    scopus 로고
    • A signaling pathway from the alpha5beta1 and alpha(v)beta3 integrins that elevates bcl-2 transcription
    • Matter ML, Ruoslahti E. A signaling pathway from the alpha5beta1 and alpha(v)beta3 integrins that elevates bcl-2 transcription. J Biol Chem. 2001; 276:27757-27763.
    • (2001) J Biol Chem , vol.276 , pp. 27757-27763
    • Matter, M.L.1    Ruoslahti, E.2
  • 33
    • 0031845562 scopus 로고    scopus 로고
    • Modulation of apoptotic cell death by extracellular matrix proteins and a fibronectin-derived antiadhesive peptide
    • Fukai F, Mashimo M, Akiyama K, Goto T, Tanuma S, Katayama K. Modulation of apoptotic cell death by extracellular matrix proteins and a fibronectin-derived antiadhesive peptide. Exp J Cell Res. 1998;242:92-99.
    • (1998) Exp J Cell Res , vol.242 , pp. 92-99
    • Fukai, F.1    Mashimo, M.2    Akiyama, K.3    Goto, T.4    Tanuma, S.5    Katayama, K.6
  • 36
    • 0034122838 scopus 로고    scopus 로고
    • Fibronectin fragments induce MMP activity in mouse mammary epithelial cells: Evidence for a role in mammary tissue remodeling
    • Schedin P, Strange R, Mitrenga T, Wolfe P, Kaeck M. Fibronectin fragments induce MMP activity in mouse mammary epithelial cells: evidence for a role in mammary tissue remodeling. J Cell Sci. 2000;113:795-806.
    • (2000) J Cell Sci , vol.113 , pp. 795-806
    • Schedin, P.1    Strange, R.2    Mitrenga, T.3    Wolfe, P.4    Kaeck, M.5
  • 37
    • 0035830852 scopus 로고    scopus 로고
    • Altered processing of fibronectin in mice lacking heparin. A role for heparin-dependent mast cell chymase in fibronectin degradation
    • Tchougounova E, Forsberg E, Angelborg G, Kjellen L, Pejler G. Altered processing of fibronectin in mice lacking heparin. a role for heparin-dependent mast cell chymase in fibronectin degradation. J Biol Chem. 2001; 276:3772-3777.
    • (2001) J Biol Chem , vol.276 , pp. 3772-3777
    • Tchougounova, E.1    Forsberg, E.2    Angelborg, G.3    Kjellen, L.4    Pejler, G.5
  • 38
    • 0028987190 scopus 로고
    • Cooperative signaling by alpha 5 beta 1 and alpha 4 beta 1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin
    • Huhtala P, Humphries MJ, McCarthy JB, Tremble PM, Werb Z, Damsky CH. Cooperative signaling by alpha 5 beta 1 and alpha 4 beta 1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin. J Cell Biol. 1995;129:867-879.
    • (1995) J Cell Biol , vol.129 , pp. 867-879
    • Huhtala, P.1    Humphries, M.J.2    McCarthy, J.B.3    Tremble, P.M.4    Werb, Z.5    Damsky, C.H.6
  • 39
    • 0033975217 scopus 로고    scopus 로고
    • Involvement of matrix metalloproteinases 2 and 9, tissue inhibitor of metalloproteinases and apoptosis in tissue remodelling in the sheep placenta
    • Riley SC, Webb CJ, Leask R, McCaig FM, Howe DC. Involvement of matrix metalloproteinases 2 and 9, tissue inhibitor of metalloproteinases and apoptosis in tissue remodelling in the sheep placenta. J Reprod Fertil. 2000;118: 19-27.
    • (2000) J Reprod Fertil , vol.118 , pp. 19-27
    • Riley, S.C.1    Webb, C.J.2    Leask, R.3    McCaig, F.M.4    Howe, D.C.5
  • 41
    • 0033229742 scopus 로고    scopus 로고
    • Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlates with cleavage of pp125(FAK), paxillin, and talin
    • Carragher NO, Levkau B, Ross R, Raines EW. Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlates with cleavage of pp125(FAK), paxillin, and talin. J Cell Biol. 1999;147:619-630.
    • (1999) J Cell Biol , vol.147 , pp. 619-630
    • Carragher, N.O.1    Levkau, B.2    Ross, R.3    Raines, E.W.4
  • 42
    • 0034610067 scopus 로고    scopus 로고
    • Nuclear localization and apoptotic regulation of an amino-terminal domain focal adhesion kinase fragment in endothelial cells
    • Lobo M, Zachary I. Nuclear localization and apoptotic regulation of an amino-terminal domain focal adhesion kinase fragment in endothelial cells. Biochem Biophys Res Commun. 2000;276:1068-1074.
    • (2000) Biochem Biophys Res Commun , vol.276 , pp. 1068-1074
    • Lobo, M.1    Zachary, I.2
  • 43
    • 0035392952 scopus 로고    scopus 로고
    • Loss of focal adhesion kinase (FAK) inhibits epidermal growth factor receptor-dependent migration and induces aggregation of nh(2)-terminal FAK in the nuclei of apoptotic glioblastoma cells
    • Jones G, Machado J Jr, Merlo A. Loss of focal adhesion kinase (FAK) inhibits epidermal growth factor receptor-dependent migration and induces aggregation of nh(2)-terminal FAK in the nuclei of apoptotic glioblastoma cells. Cancer Res. 2001;61:4978-4981.
    • (2001) Cancer Res , vol.61 , pp. 4978-4981
    • Jones, G.1    Machado J., Jr.2    Merlo, A.3
  • 44
    • 0035118748 scopus 로고    scopus 로고
    • Chymase bound to heparin is resistant to its natural inhibitors and capable of proteolyzing high density lipoproteins in aortic intimal fluid
    • Lindstedt L, Lee M, Kovanen PT. Chymase bound to heparin is resistant to its natural inhibitors and capable of proteolyzing high density lipoproteins in aortic intimal fluid. Atherosclerosis. 2001;155:87-97.
    • (2001) Atherosclerosis , vol.155 , pp. 87-97
    • Lindstedt, L.1    Lee, M.2    Kovanen, P.T.3


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