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Volumn 1593, Issue 2-3, 2003, Pages 249-258

Cytochalasin D disruption of actin filaments in 3T3 cells produces an anti-apoptotic response by activating gelatinase A extracellularly and initiating intracellular survival signals

Author keywords

Cell survival; Integrin V 3; Signal transduction

Indexed keywords

BETA3 INTEGRIN; CYTOCHALASIN D; GELATINASE A; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; PROTEIN BAD; STRESS ACTIVATED PROTEIN KINASE;

EID: 0037441563     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4889(02)00395-6     Document Type: Article
Times cited : (34)

References (41)
  • 1
    • 0034507907 scopus 로고    scopus 로고
    • Role of ECM remodeling in thyroid hormone-dependent apoptosis during anuran metamorphosis
    • Damjanovski S., Amano T., Li Q., Ueda S., Shi Y.-B., Ishizuka-Oka A. Role of ECM remodeling in thyroid hormone-dependent apoptosis during anuran metamorphosis. Ann. N.Y. Acad. Sci. 926:2000;180-191.
    • (2000) Ann. N.Y. Acad. Sci. , vol.926 , pp. 180-191
    • Damjanovski, S.1    Amano, T.2    Li, Q.3    Ueda, S.4    Shi, Y.-B.5    Ishizuka-Oka, A.6
  • 2
    • 15844379355 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 (gelatinase A) regulates glomerular mesangial cell proliferation and differentiation
    • Turck J., Pollock A.S., Le L.K., Marti H.-P., Lovett D.H. Matrix metalloproteinase 2 (gelatinase A) regulates glomerular mesangial cell proliferation and differentiation. J. Biol. Chem. 271:1996;15074-15083.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15074-15083
    • Turck, J.1    Pollock, A.S.2    Le, L.K.3    Marti, H.-P.4    Lovett, D.H.5
  • 3
    • 0033612184 scopus 로고    scopus 로고
    • Regression of hypertrophied rat pulmonary arteries in organ culture is associated with suppression of proteolytic activity, inhibition of tenascin-C, and smooth muscle cell apoptosis
    • Cowan K.N., Jones P.L., Rabinovitch M. Regression of hypertrophied rat pulmonary arteries in organ culture is associated with suppression of proteolytic activity, inhibition of tenascin-C, and smooth muscle cell apoptosis. Circ. Res. 84:1999;1223-1233.
    • (1999) Circ. Res. , vol.84 , pp. 1223-1233
    • Cowan, K.N.1    Jones, P.L.2    Rabinovitch, M.3
  • 4
    • 0030860609 scopus 로고    scopus 로고
    • Regulation of tenascin-C, a vascular smooth muscle cell survival factor that interact with αVβ3 integrin to promote epidermal growth factor receptor phosphorylation and growth
    • Jones P.L., Crack J., Rabinovitch M. Regulation of tenascin-C, a vascular smooth muscle cell survival factor that interact with αVβ3 integrin to promote epidermal growth factor receptor phosphorylation and growth. J. Biol. Chem. 139:1997;279-293.
    • (1997) J. Biol. Chem. , vol.139 , pp. 279-293
    • Jones, P.L.1    Crack, J.2    Rabinovitch, M.3
  • 5
    • 0033989282 scopus 로고    scopus 로고
    • Elastase and matrix metalloproteinase inhibitors induce regression, and tenascin-C antisense prevents progression, of vascular disease
    • Jones P.L., Crack J., Rabinovitch M. Elastase and matrix metalloproteinase inhibitors induce regression, and tenascin-C antisense prevents progression, of vascular disease. J. Clin. Invest. 105:2000;21-34.
    • (2000) J. Clin. Invest. , vol.105 , pp. 21-34
    • Jones, P.L.1    Crack, J.2    Rabinovitch, M.3
  • 6
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes R.O. Integrins: versatility, modulation, and signaling in cell adhesion. Cell. 69:1992;11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 7
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer D.D., Hanks S.K., Hunter T., Van der Geer P. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature. 372:1994;786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van der Geer, P.4
  • 9
    • 0033962672 scopus 로고    scopus 로고
    • Focal adhesions - The cytoskeletal connection
    • Critchly D.R. Focal adhesions - the cytoskeletal connection. Curr. Opin. Cell Biol. 12:2000;133-139.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 133-139
    • Critchly, D.R.1
  • 10
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch S.M., Hfrancis H. Disruption of epithelial cell-matrix interactions induces apoptosis. J. Cell Biol. 124:1994;619-626.
    • (1994) J. Cell Biol. , vol.124 , pp. 619-626
    • Frisch, S.M.1    Hfrancis, H.2
  • 11
    • 0028306464 scopus 로고
    • Lypophosphatidic acid stimulates tyrosine phosphorylation of focal adhesion kinase, Paxillin, and p130
    • Seufferlein T., Rozengurt E. Lypophosphatidic acid stimulates tyrosine phosphorylation of focal adhesion kinase, Paxillin, and p130. J. Biol. Chem. 269:1994;9345-9351.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9345-9351
    • Seufferlein, T.1    Rozengurt, E.2
  • 12
  • 14
    • 0013044914 scopus 로고
    • Actin filaments: Structure and assembly
    • New York: Garland Publishing
    • Bray D. Actin filaments: structure and assembly. Cell Movement. 1992;75-92 Garland Publishing, New York.
    • (1992) Cell Movement , pp. 75-92
    • Bray, D.1
  • 15
    • 0025885254 scopus 로고
    • Secretion of latent type IV procollagenase and active type IV collagenase by testicular cells in culture
    • Ailenberg M., Stetler-Stevenson W.G., Fritz I.B. Secretion of latent type IV procollagenase and active type IV collagenase by testicular cells in culture. Biochem. J. 279:1991;75-80.
    • (1991) Biochem. J. , vol.279 , pp. 75-80
    • Ailenberg, M.1    Stetler-Stevenson, W.G.2    Fritz, I.B.3
  • 16
    • 0028412703 scopus 로고
    • Activation of procollagenase IV by cytochalasin D and concanavalin A in cultured rat mesangial cells: Linkage to cytoskeletal reorganization
    • Ailenberg M., Weinstein T., Li I., Silverman M. Activation of procollagenase IV by cytochalasin D and concanavalin A in cultured rat mesangial cells: linkage to cytoskeletal reorganization. J. Am. Soc. Nephrol. 4:1994;1760-1770.
    • (1994) J. Am. Soc. Nephrol. , vol.4 , pp. 1760-1770
    • Ailenberg, M.1    Weinstein, T.2    Li, I.3    Silverman, M.4
  • 17
    • 0030044503 scopus 로고    scopus 로고
    • Cellular activation of mesangial gelatinase A by cytochalasin D is accompanied by enhanced mRNA expression by both gelatinase A and its membrane associated gelatinase A activator (MT-MMP)
    • Ailenberg M., Silverman M. Cellular activation of mesangial gelatinase A by cytochalasin D is accompanied by enhanced mRNA expression by both gelatinase A and its membrane associated gelatinase A activator (MT-MMP). Biochem. J. 313:1996;879-884.
    • (1996) Biochem. J. , vol.313 , pp. 879-884
    • Ailenberg, M.1    Silverman, M.2
  • 19
    • 0026027556 scopus 로고
    • Cancer, metastasis and angiogenesis: An imbalance of positive and negative regulation
    • Liotta L.A., Steeg P.S., Stetler-Stevenson W.G. Cancer, metastasis and angiogenesis: an imbalance of positive and negative regulation. Cell. 64:1991;327-336.
    • (1991) Cell , vol.64 , pp. 327-336
    • Liotta, L.A.1    Steeg, P.S.2    Stetler-Stevenson, W.G.3
  • 20
    • 0032714845 scopus 로고    scopus 로고
    • Extracellular matrix deposition and cell proliferation in a model of chronic glomerulonephritis in the rat
    • Haredza S., Schneider A., Helmchen U., Stahl R. Extracellular matrix deposition and cell proliferation in a model of chronic glomerulonephritis in the rat. Nephrol. Dial. Transplant. 14:1999;2873-2879.
    • (1999) Nephrol. Dial. Transplant. , vol.14 , pp. 2873-2879
    • Haredza, S.1    Schneider, A.2    Helmchen, U.3    Stahl, R.4
  • 21
    • 0035896502 scopus 로고    scopus 로고
    • Activation of MAPKs by angiotensin II in vascular smooth muscle cells
    • Eguchi S., Dempsey P.J., Frank G.D., Motley D., Inagami T. Activation of MAPKs by angiotensin II in vascular smooth muscle cells. J. Biol. Chem. 276:2001;7957-7962.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7957-7962
    • Eguchi, S.1    Dempsey, P.J.2    Frank, G.D.3    Motley, D.4    Inagami, T.5
  • 23
    • 0035793037 scopus 로고    scopus 로고
    • Disruption of matrix metalloproteinase 2 binding to integrin αVβ3 by an organic molecule inhibits angiogenesis and tumor growth in vivo
    • Silletti S., Kessler T., Goldberg J., Boger D.L., Cheresh D.A. Disruption of matrix metalloproteinase 2 binding to integrin αVβ3 by an organic molecule inhibits angiogenesis and tumor growth in vivo. Proc. Natl. Acad. Sci. 98:2000;119-124.
    • (2000) Proc. Natl. Acad. Sci. , vol.98 , pp. 119-124
    • Silletti, S.1    Kessler, T.2    Goldberg, J.3    Boger, D.L.4    Cheresh, D.A.5
  • 24
    • 0038668000 scopus 로고    scopus 로고
    • Escaping cell death: Survival proteins in cancer
    • Jaattela M. Escaping cell death: survival proteins in cancer. Exp. Cell Res. 248:1999;30-43.
    • (1999) Exp. Cell Res. , vol.248 , pp. 30-43
    • Jaattela, M.1
  • 25
    • 0029050683 scopus 로고
    • Requirement of the NPXY motif in the integrin beta 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo
    • Filardo E.J., Brooks P.C., Deming S.L., Damsky C., Cheresh D.A. Requirement of the NPXY motif in the integrin beta 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo. J. Cell Biol. 130:1995;441-450.
    • (1995) J. Cell Biol. , vol.130 , pp. 441-450
    • Filardo, E.J.1    Brooks, P.C.2    Deming, S.L.3    Damsky, C.4    Cheresh, D.A.5
  • 26
    • 0027156853 scopus 로고
    • 5-Bromo-2-deoxyuridine regulates invasiveness and expression of integrins and matrix-degrading proteinases in a differentiated hamster melanoma cell
    • Thomas L., Chan P.D., Damsky C. 5-Bromo-2-deoxyuridine regulates invasiveness and expression of integrins and matrix-degrading proteinases in a differentiated hamster melanoma cell. J. Cell Sci. 105:1993;191-201.
    • (1993) J. Cell Sci. , vol.105 , pp. 191-201
    • Thomas, L.1    Chan, P.D.2    Damsky, C.3
  • 27
    • 0030890939 scopus 로고    scopus 로고
    • Site-directed mutagenesis using PCR-based staggered re-annealing method without restriction enzymes
    • Ailenberg M., Silverman M. Site-directed mutagenesis using PCR-based staggered re-annealing method without restriction enzymes. BioTechniques. 22:1997;624-629.
    • (1997) BioTechniques , vol.22 , pp. 624-629
    • Ailenberg, M.1    Silverman, M.2
  • 28
    • 0031921675 scopus 로고    scopus 로고
    • Construct for assessment of transfected secretory proteins using an independently secreted reporter gene
    • Ailenberg M., Silverman M. Construct for assessment of transfected secretory proteins using an independently secreted reporter gene. BioTechniques. 24:1998;710-712.
    • (1998) BioTechniques , vol.24 , pp. 710-712
    • Ailenberg, M.1    Silverman, M.2
  • 29
    • 0028899134 scopus 로고
    • Puromycin aminonucleoside inhibits mesangial cell-induced contraction of collagen gels by stimulating production of reactive oxygen species
    • Zent R., Ailenberg M., Waddel T.K., Downey G.P., Silverman M. Puromycin aminonucleoside inhibits mesangial cell-induced contraction of collagen gels by stimulating production of reactive oxygen species. Kidney Int. 47:1995;811-817.
    • (1995) Kidney Int. , vol.47 , pp. 811-817
    • Zent, R.1    Ailenberg, M.2    Waddel, T.K.3    Downey, G.P.4    Silverman, M.5
  • 30
    • 0034692498 scopus 로고    scopus 로고
    • Rapid activation of matrix metalloproteinase-2 by glioma cells occurs through a posttranslational MT1-MMP-dependent mechanism
    • Gingras D., Page M., Annabi B., Beliveau R. Rapid activation of matrix metalloproteinase-2 by glioma cells occurs through a posttranslational MT1-MMP-dependent mechanism. Biochim. Biophys. Acta. 1497:2000;341-350.
    • (2000) Biochim. Biophys. Acta , vol.1497 , pp. 341-350
    • Gingras, D.1    Page, M.2    Annabi, B.3    Beliveau, R.4
  • 31
    • 0029738086 scopus 로고    scopus 로고
    • Induction of neural apoptosis by camptothecin, an inhibitor of DNA topoisomerase-I: Evidence for cell cycle-dependent toxicity
    • Morris E.J., Geller H.M. Induction of neural apoptosis by camptothecin, an inhibitor of DNA topoisomerase-I: evidence for cell cycle-dependent toxicity. J. Biol. Chem. 134:1996;757-770.
    • (1996) J. Biol. Chem. , vol.134 , pp. 757-770
    • Morris, E.J.1    Geller, H.M.2
  • 32
    • 0029807603 scopus 로고    scopus 로고
    • Selective induction of apoptosis in Hep 3B cells by topoisomerase I inhibitors: Evidence for protease-dependent pathway that does not activate cysteine protease p32
    • Adjei P.N., Kaufmann S.H., Leung W.-Y., Mao F., Gores G.J. Selective induction of apoptosis in Hep 3B cells by topoisomerase I inhibitors: evidence for protease-dependent pathway that does not activate cysteine protease p32. J. Clin. Invest. 98:1996;2588-2596.
    • (1996) J. Clin. Invest. , vol.98 , pp. 2588-2596
    • Adjei, P.N.1    Kaufmann, S.H.2    Leung, W.-Y.3    Mao, F.4    Gores, G.J.5
  • 33
    • 0031467657 scopus 로고    scopus 로고
    • Inhibitory effects of oleic and decosahexaenoic acids on lung metastasis by colon-carcinoma-26 cells are associated with reduced matrix metalloproteinase-2 and 9 activities
    • Suzuki I., Iigo M., Ishikawa C., Kuhara T., Asamoto M., Kunimoto T., Moore M.A., Yazawa K., Araki E., Tsuda H. Inhibitory effects of oleic and decosahexaenoic acids on lung metastasis by colon-carcinoma-26 cells are associated with reduced matrix metalloproteinase-2 and 9 activities. Int. J. Cancer. 73:1997;607-612.
    • (1997) Int. J. Cancer , vol.73 , pp. 607-612
    • Suzuki, I.1    Iigo, M.2    Ishikawa, C.3    Kuhara, T.4    Asamoto, M.5    Kunimoto, T.6    Moore, M.A.7    Yazawa, K.8    Araki, E.9    Tsuda, H.10
  • 34
    • 0032943079 scopus 로고    scopus 로고
    • Influence of oleic acid on the expression, activation and activity of gelatinase A produced by oncogene-transformed human bronchial epithelial cells
    • Polette M., Huet E., Birembaut P., Maquart F.-X., Hornebeck W., Emonard H. Influence of oleic acid on the expression, activation and activity of gelatinase A produced by oncogene-transformed human bronchial epithelial cells. Int. J. Cancer. 80:1999;751-755.
    • (1999) Int. J. Cancer , vol.80 , pp. 751-755
    • Polette, M.1    Huet, E.2    Birembaut, P.3    Maquart, F.-X.4    Hornebeck, W.5    Emonard, H.6
  • 36
    • 85031247825 scopus 로고    scopus 로고
    • Differential plasma membrane binding of active and latent gelatinase A
    • Ailenberg M., Silverman M. Differential plasma membrane binding of active and latent gelatinase A. Mol. Biol. Cell. 8(Suppl.):1998;74a.
    • (1998) Mol. Biol. Cell , vol.8 , Issue.SUPPL.
    • Ailenberg, M.1    Silverman, M.2
  • 37
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta S.R., Dubek H., Tao X., Masters S., Fu H., Gotoh Y., Greenberg M.E. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell. 91:1997;231-241.
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dubek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 38
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through protein kinase Akt
    • del Peso L., Gonzales-Garcia M., Page C., Herrera R., Nunez G. Interleukin-3-induced phosphorylation of BAD through protein kinase Akt. Science. 278:1997;687-689.
    • (1997) Science , vol.278 , pp. 687-689
    • Del Peso, L.1    Gonzales-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 39
    • 0032698075 scopus 로고    scopus 로고
    • Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanism
    • Bonni A., Brunet A., West A., Datta S.R., Takasu M.A., Greenberg M.E. Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanism. Science. 286:1999;1358-1362.
    • (1999) Science , vol.286 , pp. 1358-1362
    • Bonni, A.1    Brunet, A.2    West, A.3    Datta, S.R.4    Takasu, M.A.5    Greenberg, M.E.6
  • 40
    • 0033520937 scopus 로고    scopus 로고
    • RSK blocks Bad-mediated cell death via a protein kinase C-dependent pathway
    • RSK blocks Bad-mediated cell death via a protein kinase C-dependent pathway. J. Biol. Chem. 274:1999;34859-34867.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34859-34867
    • Tan, Y.1    Ruan, H.2    Demeter, M.R.3    Comb, M.J.4
  • 41
    • 0033497124 scopus 로고    scopus 로고
    • A link between integrins and MMPs in angiogenesis
    • Silletti D., Cheresh D.A. A link between integrins and MMPs in angiogenesis. Fibrinolysis Proteolysis. 13:1999;226-238.
    • (1999) Fibrinolysis Proteolysis , vol.13 , pp. 226-238
    • Silletti, D.1    Cheresh, D.A.2


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