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Volumn 26, Issue 4, 1999, Pages 274-285

Altered actin cytoskeleton and inhibition of matrix metalloproteinase expression by vanadate and phenylarsine oxide, inhibitors of phosphotyrosine phosphatases: Modulation of migration and invasion of human malignant glioma cells

Author keywords

Focal adhesion kinase; Matrix metalloproteinase 9; Phosphotyrosine phosphatase; Protease

Indexed keywords

ARSENOSOBENZENE; FOCAL ADHESION KINASE; GELATINASE B; MATRIX METALLOPROTEINASE; PROTEIN TYROSINE PHOSPHATASE; VANADIC ACID;

EID: 0032712605     PISSN: 08991987     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1098-2744(199912)26:4<274::AID-MC6>3.0.CO;2-1     Document Type: Article
Times cited : (19)

References (38)
  • 1
    • 0020369710 scopus 로고
    • Dedifferentiated chondrocytes reexpress the differentiated collagen phenotype when cultured in agarose gels
    • Benya PD, Schaffer JD. Dedifferentiated chondrocytes reexpress the differentiated collagen phenotype when cultured in agarose gels. Cell 1982;30:215-224.
    • (1982) Cell , vol.30 , pp. 215-224
    • Benya, P.D.1    Schaffer, J.D.2
  • 2
    • 0024335963 scopus 로고
    • Signal transduction through the fibronectin receptor induces collagenases and stromelysin gene expression
    • Werb Z, Tremble PM, Behrendtsen O, Crowley E, Damsky CH. Signal transduction through the fibronectin receptor induces collagenases and stromelysin gene expression. J Cell Biol 1989;109:877-899.
    • (1989) J Cell Biol , vol.109 , pp. 877-899
    • Werb, Z.1    Tremble, P.M.2    Behrendtsen, O.3    Crowley, E.4    Damsky, C.H.5
  • 3
    • 0022977704 scopus 로고
    • Reorganization of polymerized actin: A possible trigger for induction of procollgenase in fibroblasts cultured in and on collagen
    • Unemori EN, Werb Z. Reorganization of polymerized actin: A possible trigger for induction of procollgenase in fibroblasts cultured in and on collagen. J Cell Biol 1986;103: 1021-1031.
    • (1986) J Cell Biol , vol.103 , pp. 1021-1031
    • Unemori, E.N.1    Werb, Z.2
  • 4
    • 0032577493 scopus 로고    scopus 로고
    • Induction of matrix metalloproteinase-9 requires a polymerized actin cytoskeleton in human glioma cells
    • Chintala SK, Sawaya R, Aggarwal BB, et al. Induction of matrix metalloproteinase-9 requires a polymerized actin cytoskeleton in human glioma cells. J Biol Chem 1998;273: 13545-13551.
    • (1998) J Biol Chem , vol.273 , pp. 13545-13551
    • Chintala, S.K.1    Sawaya, R.2    Aggarwal, B.B.3
  • 5
    • 0025285474 scopus 로고
    • Inverse correlation between tyrosine phosphorylation and collegenase production in chondrocytes
    • Cruz TF, Mills G, Pritzker KP, Kandel RA. Inverse correlation between tyrosine phosphorylation and collegenase production in chondrocytes. Biochem J 1990;269:717-721.
    • (1990) Biochem J , vol.269 , pp. 717-721
    • Cruz, T.F.1    Mills, G.2    Pritzker, K.P.3    Kandel, R.A.4
  • 6
    • 0029842723 scopus 로고    scopus 로고
    • Regulation of cytoskeleton organization and paxillin dephosphorylation by cAMP. Studies on rnurine Y1 adrenal cells
    • Han JD, Rubin CJ. Regulation of cytoskeleton organization and paxillin dephosphorylation by cAMP. Studies on rnurine Y1 adrenal cells. J Biol Chem 1996;271:29211-29215.
    • (1996) J Biol Chem , vol.271 , pp. 29211-29215
    • Han, J.D.1    Rubin, C.J.2
  • 8
    • 0026806366 scopus 로고
    • Activation of signal transduction in platelets by the tyrosine phosphatase inhibitor pervanadate (vanadyl hydroperoxide)
    • Pumiglia KM, Lau LF, Huang CK, Burroughs S, Feinstein MB. Activation of signal transduction in platelets by the tyrosine phosphatase inhibitor pervanadate (vanadyl hydroperoxide). Biochem J 1992;286:441-449.
    • (1992) Biochem J , vol.286 , pp. 441-449
    • Pumiglia, K.M.1    Lau, L.F.2    Huang, C.K.3    Burroughs, S.4    Feinstein, M.B.5
  • 9
    • 0025197060 scopus 로고
    • 2 and vanadate concomitantly stimulates protein tyrosine phosphorylation and polyphosphoinositide breakdown in different cell lines
    • 2 and vanadate concomitantly stimulates protein tyrosine phosphorylation and polyphosphoinositide breakdown in different cell lines. Biochemistry 1990;29:10240-10245.
    • (1990) Biochemistry , vol.29 , pp. 10240-10245
    • Zick, Y.1    Sagi-Eisenberg, R.2
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0027433279 scopus 로고
    • Determination of phosphotyrosine phosphatase (PTPase) activity in normal and transformed cells
    • Kremerskothen J, Barnekow A. Determination of phosphotyrosine phosphatase (PTPase) activity in normal and transformed cells. Mol Cell Biochem 1993;125:1-9.
    • (1993) Mol Cell Biochem , vol.125 , pp. 1-9
    • Kremerskothen, J.1    Barnekow, A.2
  • 12
    • 0031425359 scopus 로고    scopus 로고
    • Altered in vitro spreading and cytoskeletal organization in human glioma cells by downregulation of urokinase receptor
    • Chintala SK, Mohanam S, Go Y, et al. Altered in vitro spreading and cytoskeletal organization in human glioma cells by downregulation of urokinase receptor. Mol Carcinog 1997;20:355-365.
    • (1997) Mol Carcinog , vol.20 , pp. 355-365
    • Chintala, S.K.1    Mohanam, S.2    Go, Y.3
  • 13
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells
    • Schreiber E, Matthias P, Muller MM, Schaffner W. Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells. Nucleic Acids Res 1989;17:6419.
    • (1989) Nucleic Acids Res , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 14
    • 0023176085 scopus 로고
    • An inducible transcription factor activates expression of human immunodeficiency virus in T cells
    • Nabel G, Baltimore D. An inducible transcription factor activates expression of human immunodeficiency virus in T cells. Nature 1987;326:711-713.
    • (1987) Nature , vol.326 , pp. 711-713
    • Nabel, G.1    Baltimore, D.2
  • 15
    • 0025260779 scopus 로고
    • Regulation of tumor necrosis factor alpha transcription in macrophages: Involvement of four kappa B-like motifs and of constitutive and inducible forms of NF-kappa B
    • Collart MA, Baeuerle P, Vassalli P. Regulation of tumor necrosis factor alpha transcription in macrophages: Involvement of four kappa B-like motifs and of constitutive and inducible forms of NF-kappa B. Mol Cell Biol 1990;10: 1489-1506.
    • (1990) Mol Cell Biol , vol.10 , pp. 1489-1506
    • Collart, M.A.1    Baeuerle, P.2    Vassalli, P.3
  • 16
    • 0024284826 scopus 로고
    • Molecular cloning of an enhancer binding protein: Isolation by screening of an expression library with a recognition site DNA
    • Singh H, LeBowitz JH, Baldwin ASJ, Sharp PA. Molecular cloning of an enhancer binding protein: Isolation by screening of an expression library with a recognition site DNA. Cell 1988;52:415-423.
    • (1988) Cell , vol.52 , pp. 415-423
    • Singh, H.1    LeBowitz, J.H.2    Baldwin, A.S.J.3    Sharp, P.A.4
  • 17
    • 0027438302 scopus 로고
    • v-Src activates the expression of 92-kDa type IV collagenase gene through the AP-1 site and the GT box homologous to retinoblastoma control elements. A mechanism regulating gene expression independent of that by inflammatory cytokines
    • Sato H, Kita M, Seiki M. v-Src activates the expression of 92-kDa type IV collagenase gene through the AP-1 site and the GT box homologous to retinoblastoma control elements. A mechanism regulating gene expression independent of that by inflammatory cytokines. J Biol Chem 1993;268: 23460-23468.
    • (1993) J Biol Chem , vol.268 , pp. 23460-23468
    • Sato, H.1    Kita, M.2    Seiki, M.3
  • 18
    • 0031013736 scopus 로고    scopus 로고
    • Protein kinase mediators of integrin signal transduction
    • Hannigan GE, Dedhar S. Protein kinase mediators of integrin signal transduction. J Mol Med 1997;75:35-44.
    • (1997) J Mol Med , vol.75 , pp. 35-44
    • Hannigan, G.E.1    Dedhar, S.2
  • 19
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge K, Fath K, Kelly T, Nuckolls G, Turner C. Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton. Ann Rev Cell Dev Biol 1988;4:487-525.
    • (1988) Ann Rev Cell Dev Biol , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 20
    • 0021627104 scopus 로고
    • Spreading of non-transformed and transformed cells
    • Vasiliev JM. Spreading of non-transformed and transformed cells. Biochim Biophys Acta 1985;780:21-65.
    • (1985) Biochim Biophys Acta , vol.780 , pp. 21-65
    • Vasiliev, J.M.1
  • 21
    • 0027242121 scopus 로고
    • Tyrosine phosphorylation and cytoskeletal reorganization in platelets are triggered by interaction of integrin receptors with their immobilized ligands
    • Haimovich B, Lipfert L, Brugge JS, Shattil SJ. Tyrosine phosphorylation and cytoskeletal reorganization in platelets are triggered by interaction of integrin receptors with their immobilized ligands. J Biol Chem 1993;268:15868-15877.
    • (1993) J Biol Chem , vol.268 , pp. 15868-15877
    • Haimovich, B.1    Lipfert, L.2    Brugge, J.S.3    Shattil, S.J.4
  • 22
    • 0027459771 scopus 로고
    • Signal transduction from the extracellular matrix
    • Juliano RL, Haskill SJ. Signal transduction from the extracellular matrix. J Cell Biol 1993;120:577-585.
    • (1993) J Cell Biol , vol.120 , pp. 577-585
    • Juliano, R.L.1    Haskill, S.J.2
  • 23
    • 0025946283 scopus 로고
    • Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by clustering of beta 1 integrins
    • Kornberg LJ, Earp HS, Turner CE, Prockop C, Juliano RL. Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by clustering of beta 1 integrins. Proc Natl Acad Sci USA 1991;88:8392-8396.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8392-8396
    • Kornberg, L.J.1    Earp, H.S.2    Turner, C.E.3    Prockop, C.4    Juliano, R.L.5
  • 24
    • 0026445719 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge K, Turner CE, Romer LH. Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton. J Cell Biol 1992;119:893-903.
    • (1992) J Cell Biol , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 25
    • 0028149381 scopus 로고
    • The coordinated action of protein tyrosine phosphatases and kinases in cell signaling
    • Sun H, Tonks NK. The coordinated action of protein tyrosine phosphatases and kinases in cell signaling. Trends Biochem Sci 1994;19:480-485.
    • (1994) Trends Biochem Sci , vol.19 , pp. 480-485
    • Sun, H.1    Tonks, N.K.2
  • 26
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter T. Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling. Cell 1995; 80:225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 27
    • 0030936323 scopus 로고    scopus 로고
    • PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer
    • Li J, Yen C, Liaw D, et al. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science 1997;275:1943-1947.
    • (1997) Science , vol.275 , pp. 1943-1947
    • Li, J.1    Yen, C.2    Liaw, D.3
  • 28
    • 0028792065 scopus 로고
    • p125FAK tyrosine phosphorylation and focal adhesion assembly: Studies with phosphotyrosine phosphatase inhibitors
    • Defilippi P, Retta SF, Olivo C, et al. p125FAK tyrosine phosphorylation and focal adhesion assembly: Studies with phosphotyrosine phosphatase inhibitors. Exp Cell Res 1995; 221:141-152.
    • (1995) Exp Cell Res , vol.221 , pp. 141-152
    • Defilippi, P.1    Retta, S.F.2    Olivo, C.3
  • 30
    • 0028361090 scopus 로고
    • Thyroid cell spreading and focal adhesion formation depend upon protein tyrosine phosphorylation and actin microfilaments
    • Yap AS, Keast JR, Manley SW. Thyroid cell spreading and focal adhesion formation depend upon protein tyrosine phosphorylation and actin microfilaments. Exp Cell Res 1994;210:306-314.
    • (1994) Exp Cell Res , vol.210 , pp. 306-314
    • Yap, A.S.1    Keast, J.R.2    Manley, S.W.3
  • 31
    • 0030470250 scopus 로고    scopus 로고
    • Suppression of metastatic potential of high-metastatic Lewis lung carcinoma cells by vanadate, an inhibitor of tyrosine phosphatase, through inhibiting cell-substrate adhesion
    • Takenaga K. Suppression of metastatic potential of high-metastatic Lewis lung carcinoma cells by vanadate, an inhibitor of tyrosine phosphatase, through inhibiting cell-substrate adhesion. Invasion Metastasis 1996;16: 97-106.
    • (1996) Invasion Metastasis , vol.16 , pp. 97-106
    • Takenaga, K.1
  • 32
    • 0026529501 scopus 로고
    • The effect of tyrosine-specific protein phosphorylation on the assembly of adherens-type junctions
    • Volberg T, Zick Y, Dror R, et al. The effect of tyrosine-specific protein phosphorylation on the assembly of adherens-type junctions. EMBO J 1992;11:1733-1742.
    • (1992) EMBO J , vol.11 , pp. 1733-1742
    • Volberg, T.1    Zick, Y.2    Dror, R.3
  • 33
    • 0028853550 scopus 로고
    • Differential role of protein tyrosine phosphorylation/dephosphorylation in affinity regulation of beta 1 and beta 3 integrin in human fibroblasts
    • Takagi J, Saito Y. Differential role of protein tyrosine phosphorylation/dephosphorylation in affinity regulation of beta 1 and beta 3 integrin in human fibroblasts. Cell Struct Funct 1995;20:403-413.
    • (1995) Cell Struct Funct , vol.20 , pp. 403-413
    • Takagi, J.1    Saito, Y.2
  • 34
    • 0027483931 scopus 로고
    • Activation of phosphotyrosine phosphatase activity by reduction of cell-substrate adhesion
    • Maher PA. Activation of phosphotyrosine phosphatase activity by reduction of cell-substrate adhesion. Proc Natl Acad Sci USA 1993;90:11177-11181.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11177-11181
    • Maher, P.A.1
  • 35
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark EA, Brugge JS. Integrins and signal transduction pathways: The road taken. Science 1995;268:233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 36
    • 0030005705 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in signaling
    • Streuli M. Protein tyrosine phosphatases in signaling. Curr Opin Cell Biol 1996;8:182-188.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 182-188
    • Streuli, M.1
  • 37
    • 0031128376 scopus 로고    scopus 로고
    • Modulation of protein tyrosine phosphorylation by the extracellular matrix
    • Corbett SA, Schwarzbauer JE. Modulation of protein tyrosine phosphorylation by the extracellular matrix. J Surg Res 1997;69:220-225.
    • (1997) J Surg Res , vol.69 , pp. 220-225
    • Corbett, S.A.1    Schwarzbauer, J.E.2
  • 38
    • 0029035974 scopus 로고
    • Differential regulation of protein-tyrosine phosphatases by integrin alpha lib beta 3 through cytoskeletal reorganization and tyrosine phosphorylation in human platelets
    • Ezumi Y, Takayama H, Okuma M. Differential regulation of protein-tyrosine phosphatases by integrin alpha lib beta 3 through cytoskeletal reorganization and tyrosine phosphorylation in human platelets. J Biol Chem 1995;270: 11927-11934.
    • (1995) J Biol Chem , vol.270 , pp. 11927-11934
    • Ezumi, Y.1    Takayama, H.2    Okuma, M.3


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