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Volumn 176, Issue 2, 1998, Pages 293-302

Cell shape-dependent pathway of plasminogen activator inhibitor type-1 gene expression requires cytoskeletal reorganization

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALPHOSTIN C; CYCLOHEXIMIDE; CYTOCHALASIN D; GENISTEIN; HERBIMYCIN A; PLASMINOGEN ACTIVATOR INHIBITOR 1; PUROMYCIN; TYRPHOSTIN;

EID: 0031873602     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4652(199808)176:2<293::AID-JCP7>3.0.CO;2-J     Document Type: Article
Times cited : (13)

References (58)
  • 1
    • 0021274363 scopus 로고
    • Changes in cell shape correlate with collagenase gene expression in rabbit synovial fibroblasts
    • Aggeler, J., Frisch, S.M., and Werb, Z. (1984) Changes in cell shape correlate with collagenase gene expression in rabbit synovial fibroblasts. J. Cell Biol., 98:1662-1671.
    • (1984) J. Cell Biol. , vol.98 , pp. 1662-1671
    • Aggeler, J.1    Frisch, S.M.2    Werb, Z.3
  • 2
    • 0030589664 scopus 로고    scopus 로고
    • The extracellular matrix in epithelial biology: Shared molecules and common themes in distant phyla
    • Ashkenas, J., Muschler, J., and Bissell, M.J. (1996) The extracellular matrix in epithelial biology: Shared molecules and common themes in distant phyla. Dev. Biol., 180:533-444.
    • (1996) Dev. Biol. , vol.180 , pp. 533-1444
    • Ashkenas, J.1    Muschler, J.2    Bissell, M.J.3
  • 3
    • 0031022256 scopus 로고    scopus 로고
    • Anchorage-dependent cell cycle progression
    • Assoian, R.K. (1997) Anchorage-dependent cell cycle progression. J. Cell Biol., 136:1-4.
    • (1997) J. Cell Biol. , vol.136 , pp. 1-4
    • Assoian, R.K.1
  • 4
    • 0029332186 scopus 로고
    • Mechanoreception at the cellular level: The detection, interpretation, and diversity of responses to mechanical signals
    • Banes, A.J., Tsuzaki, M., Yamamoto, J., Fischer, T., Brigman, B., Brown, T., and Miller, L. (1995) Mechanoreception at the cellular level: the detection, interpretation, and diversity of responses to mechanical signals. Biochem. Cell Biol., 73:349-365.
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 349-365
    • Banes, A.J.1    Tsuzaki, M.2    Yamamoto, J.3    Fischer, T.4    Brigman, B.5    Brown, T.6    Miller, L.7
  • 5
    • 0028868384 scopus 로고
    • Expression of the human gene encoding urokinase plasminogen activator receptor is activated by disruption of the cytoskeleton
    • Bayraktutan, U., and Jones, P. (1995) Expression of the human gene encoding urokinase plasminogen activator receptor is activated by disruption of the cytoskeleton. Exp. Cell Res., 221:486-495.
    • (1995) Exp. Cell Res. , vol.221 , pp. 486-495
    • Bayraktutan, U.1    Jones, P.2
  • 6
    • 0025190019 scopus 로고
    • Plasminogen activator gene expression is induced by the src oncogene product and tumor promoters
    • Bell, S.M., Brackenbury, R.W., Leslie, N.D., and Degen, J.L. (1990) Plasminogen activator gene expression is induced by the src oncogene product and tumor promoters. J. Biol. Chem., 265:1333-1338.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1333-1338
    • Bell, S.M.1    Brackenbury, R.W.2    Leslie, N.D.3    Degen, J.L.4
  • 7
    • 0017812339 scopus 로고
    • The control of mRNA production, translation, and turnover in suspended and reattached anchorage-dependent fibroblasts
    • Benecke, B., Ben-Ze'ev, A., and Penman, S. (1978) The control of mRNA production, translation, and turnover in suspended and reattached anchorage-dependent fibroblasts. Cell, 14:931-939.
    • (1978) Cell , vol.14 , pp. 931-939
    • Benecke, B.1    Ben-Ze'ev, A.2    Penman, S.3
  • 8
    • 0018942383 scopus 로고
    • Protein synthesis requires cell-surface contact while nuclear events respond to cell shape in anchorage-dependent fibroblasts
    • Ben-Ze'ev, A., Farmer, S.R., and Penman, S. (1980) Protein synthesis requires cell-surface contact while nuclear events respond to cell shape in anchorage-dependent fibroblasts. Cell, 21:365-372.
    • (1980) Cell , vol.21 , pp. 365-372
    • Ben-Ze'ev, A.1    Farmer, S.R.2    Penman, S.3
  • 9
    • 0024121578 scopus 로고
    • Cell-cell and cell-matrix interactions differentially regulate the expression of hepatic and cytoskeletal genes in primary cultures of rat hepatocytes
    • Ben-Ze'ev, A., Robinson, G.S., Bucher, N.L.R., and Farmer, S.R. (1988) Cell-cell and cell-matrix interactions differentially regulate the expression of hepatic and cytoskeletal genes in primary cultures of rat hepatocytes. Proc. Natl. Acad. Sci. USA, 85:2161-2165.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2161-2165
    • Ben-Ze'ev, A.1    Robinson, G.S.2    Bucher, N.L.R.3    Farmer, S.R.4
  • 10
    • 0022646342 scopus 로고
    • Cytochalasin B slows but does not prevent monomer addition at the barbed end of the actin filament
    • Bonder, E.M., and Mooseker, M.S. (1986) Cytochalasin B slows but does not prevent monomer addition at the barbed end of the actin filament. J. Cell Biol., 102:282-288.
    • (1986) J. Cell Biol. , vol.102 , pp. 282-288
    • Bonder, E.M.1    Mooseker, M.S.2
  • 11
    • 0025374009 scopus 로고
    • Disruption of cytoskeletal structures results in the induction of the urokinase-type plasminogen activator gene expression
    • Botteri, F.M., Ballmer-Hofer, K., Rajput, B., and Nagamine, Y. (1990) Disruption of cytoskeletal structures results in the induction of the urokinase-type plasminogen activator gene expression. J. Biol. Chem., 265:13327-13334.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13327-13334
    • Botteri, F.M.1    Ballmer-Hofer, K.2    Rajput, B.3    Nagamine, Y.4
  • 12
    • 0019404945 scopus 로고
    • Mechanism of actin of cytoachalasin: Evidence that it binds to actin filaments
    • Brown, S.S., and Spudich, J.A. (1981) Mechanism of actin of cytoachalasin: Evidence that it binds to actin filaments. J. Cell Biol., 88:487-491.
    • (1981) J. Cell Biol. , vol.88 , pp. 487-491
    • Brown, S.S.1    Spudich, J.A.2
  • 14
    • 0019829488 scopus 로고
    • Cytochalasin D inhibits actin polymerization and induces depolymerization of actin filaments formed during platelet shape change
    • Casella, J.F., Flanagan, M.D., and Shin, L. (1981) Cytochalasin D inhibits actin polymerization and induces depolymerization of actin filaments formed during platelet shape change. Nature, 293:302-305.
    • (1981) Nature , vol.293 , pp. 302-305
    • Casella, J.F.1    Flanagan, M.D.2    Shin, L.3
  • 16
    • 0019892036 scopus 로고
    • Stimulation of plasminogen activator expression and induction of DNA synthesis by microtubule disruptive drugs
    • Chou, I.N., Zeiger, J., Solomon, J.A., and Black, P.H. (1982) Stimulation of plasminogen activator expression and induction of DNA synthesis by microtubule disruptive drugs. Biochem. Biophys. Res. Comm., 101:1266-1273.
    • (1982) Biochem. Biophys. Res. Comm. , vol.101 , pp. 1266-1273
    • Chou, I.N.1    Zeiger, J.2    Solomon, J.A.3    Black, P.H.4
  • 17
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper, J.A. (1987) Effects of cytochalasin and phalloidin on actin. J. Cell Biol., 105:1473-1478.
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 18
    • 0019377692 scopus 로고
    • Evidence that microtubule depolymerization early in the cell cycle is sufficient to initiate DNA synthesis
    • Crossin, K.L., and Carney, D.H. (1981) Evidence that microtubule depolymerization early in the cell cycle is sufficient to initiate DNA synthesis. Cell, 23:61-71.
    • (1981) Cell , vol.23 , pp. 61-71
    • Crossin, K.L.1    Carney, D.H.2
  • 19
    • 0026938957 scopus 로고
    • Signal transduction by integrin receptors for extracellular matrix: Cooperative processing of extracellular information
    • Damsky, C.H., and Werb, Z. (1992) Signal transduction by integrin receptors for extracellular matrix: Cooperative processing of extracellular information. Curr. Opin. Cell Biol., 4:772-781.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 772-781
    • Damsky, C.H.1    Werb, Z.2
  • 20
    • 0018140371 scopus 로고
    • Role of cell shape in growth control
    • Folkman, J., and Moscona, A. (1978) Role of cell shape in growth control. Nature, 273:345-349.
    • (1978) Nature , vol.273 , pp. 345-349
    • Folkman, J.1    Moscona, A.2
  • 22
    • 0023465678 scopus 로고
    • Cell motility and the problem of anatomical homeostasis
    • Harris, A.K. (1987) Cell motility and the problem of anatomical homeostasis. J. Cell Sci., 8(Suppl.):121-140.
    • (1987) J. Cell Sci. , vol.8 , Issue.SUPPL. , pp. 121-140
    • Harris, A.K.1
  • 23
    • 0025772967 scopus 로고
    • SPARC induces the expression of type 1 plasminogen activator inhibitor in cultured bovine aortic endothelial cells
    • Hasselaar, P., Loskutoff, D.J., Sawdey, M., and Sage, E.H. (1991) SPARC induces the expression of type 1 plasminogen activator inhibitor in cultured bovine aortic endothelial cells. J. Biol. Chem., 266:13178-13184.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13178-13184
    • Hasselaar, P.1    Loskutoff, D.J.2    Sawdey, M.3    Sage, E.H.4
  • 24
    • 0004545956 scopus 로고
    • Extracellular matrix interaction with the cytoskeleton
    • W.D. Stein and F. Bronner, eds. Academic Press, New York
    • Hay, E.D., and Svoboda, K.K. (1989) Extracellular matrix interaction with the cytoskeleton. In: Cell Shape: Determinants, Regulation, and Regulatory Role. W.D. Stein and F. Bronner, eds. Academic Press, New York, pp. 147-172.
    • (1989) Cell Shape: Determinants, Regulation, and Regulatory Role , pp. 147-172
    • Hay, E.D.1    Svoboda, K.K.2
  • 25
    • 0345558258 scopus 로고
    • Induced expression of p52(PAI-1) in the cellular response to hyperoxia: Common changes in gene expression elicited by growth factors and hyperoxic stress
    • A. Johnson and T.J. Ferro, eds. Marcel Dekker, New York
    • Higgins, P.J. (1992) Induced expression of p52(PAI-1) in the cellular response to hyperoxia: common changes in gene expression elicited by growth factors and hyperoxic stress. In: Lung Vascular Injury: Molecular and Cellular Response. A. Johnson and T.J. Ferro, eds. Marcel Dekker, New York, pp. 175-189.
    • (1992) Lung Vascular Injury: Molecular and Cellular Response , pp. 175-189
    • Higgins, P.J.1
  • 26
    • 0344264260 scopus 로고
    • p52(PAI-1) mRNA transcripts partition to the cytoskeletal framework during shape-dependent induction of p52(PAI-1) gene expression in normal rat kidney cells
    • Higgins, P.J. (1994) p52(PAI-1) mRNA transcripts partition to the cytoskeletal framework during shape-dependent induction of p52(PAI-1) gene expression in normal rat kidney cells. Allergy Immunol, 13:1-8.
    • (1994) Allergy Immunol , vol.13 , pp. 1-8
    • Higgins, P.J.1
  • 27
    • 0025308417 scopus 로고
    • p52 induction by cytochalasin D in rat kidney fibroblasts: Homologies between p52 and plasminogen activator inhibitor type-1
    • Higgins, P.J., Ryan, M.P., Zeheb, R., Gelehrter, T.D., and Chaudhari, P. (1990) p52 induction by cytochalasin D in rat kidney fibroblasts: Homologies between p52 and plasminogen activator inhibitor type-1. J. Cell Physiol., 143:321-329.
    • (1990) J. Cell Physiol. , vol.143 , pp. 321-329
    • Higgins, P.J.1    Ryan, M.P.2    Zeheb, R.3    Gelehrter, T.D.4    Chaudhari, P.5
  • 28
    • 0027103885 scopus 로고
    • Cell shape-associated transcriptional activation of the p52(PAI-1) gene in rat kidney cells
    • Higgins, P.J., Ryan, M.P., and Ahmed, A. (1992) Cell shape-associated transcriptional activation of the p52(PAI-1) gene in rat kidney cells. Biochem. J., 288:1017-1024.
    • (1992) Biochem. J. , vol.288 , pp. 1017-1024
    • Higgins, P.J.1    Ryan, M.P.2    Ahmed, A.3
  • 29
    • 0028145018 scopus 로고
    • Induced expression of p52(PAI-1) in normal rat kidney cells by the microfilament-disrupting agent cytochalasin D
    • Higgins, P.J., Ryan, M.P. and Providence, K.P. (1994) Induced expression of p52(PAI-1) in normal rat kidney cells by the microfilament-disrupting agent cytochalasin D. J. Cell Physiol., 159:187-195.
    • (1994) J. Cell Physiol. , vol.159 , pp. 187-195
    • Higgins, P.J.1    Ryan, M.P.2    Providence, K.P.3
  • 30
    • 0026245524 scopus 로고
    • Integrins as mechanochemical transducers
    • Ingber, D. (1991) Integrins as mechanochemical transducers. Curr. Opin. Cell Biol., 3:841-848.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 841-848
    • Ingber, D.1
  • 31
    • 0027221483 scopus 로고
    • Cellular tensegrity: Denning new rules of biological design that govern the cytoskeleton
    • Ingber, D.R. (1993) Cellular tensegrity: Denning new rules of biological design that govern the cytoskeleton. J. Cell Sci., 104:613-627.
    • (1993) J. Cell Sci. , vol.104 , pp. 613-627
    • Ingber, D.R.1
  • 32
    • 0002332210 scopus 로고
    • Tension and compression as basic determinants of form and function: Utilization of a cellular tensegrity mechanism
    • W. Stein and F. Bronner, eds. Academic Press, San Diego
    • Ingber, D.E., and Folkman, J. (1989) Tension and compression as basic determinants of form and function: Utilization of a cellular tensegrity mechanism. In: Cell Shape: Determinants, Regulation, and Regulatory Role. W. Stein and F. Bronner, eds. Academic Press, San Diego, pp. 3-31.
    • (1989) Cell Shape: Determinants, Regulation, and Regulatory Role , pp. 3-31
    • Ingber, D.E.1    Folkman, J.2
  • 33
    • 0028860191 scopus 로고
    • Effects of cytochalasin D on shape and fluid pinocytosis in human neutrophils as related to cytoskeletal changes
    • Keller, H., and Niggli, V. (1995) Effects of cytochalasin D on shape and fluid pinocytosis in human neutrophils as related to cytoskeletal changes. Eur. J. Cell Biol., 66:157-164.
    • (1995) Eur. J. Cell Biol. , vol.66 , pp. 157-164
    • Keller, H.1    Niggli, V.2
  • 34
    • 0020123666 scopus 로고
    • Actin polymerization and its regulation by proteins from non-muscle cells
    • Korn, E.D. (1982) Actin polymerization and its regulation by proteins from non-muscle cells. Physiol. Rev., 62:672-737.
    • (1982) Physiol. Rev. , vol.62 , pp. 672-737
    • Korn, E.D.1
  • 36
    • 0024309860 scopus 로고
    • Growth factors in the regulation of pericellular proteolysis: A review
    • Laiho, M., and Keski-Oja, J. (1989) Growth factors in the regulation of pericellular proteolysis: a review. Cancer Res., 49:2533-2553.
    • (1989) Cancer Res. , vol.49 , pp. 2533-2553
    • Laiho, M.1    Keski-Oja, J.2
  • 37
    • 0029122355 scopus 로고
    • Cytochalasin D induces changes in cell shape and promotes in vitro chondrogenesis: A morphological study
    • Loty, S., Forest, N., Boulekbache, H., and Sautier, J.M. (1995) Cytochalasin D induces changes in cell shape and promotes in vitro chondrogenesis: a morphological study. Biol. Cell, 83:149-161.
    • (1995) Biol. Cell , vol.83 , pp. 149-161
    • Loty, S.1    Forest, N.2    Boulekbache, H.3    Sautier, J.M.4
  • 38
    • 0020170017 scopus 로고
    • Dihydrocytochalasin B disorganizes actin cytoarchitecture and inhibits initiation of DNA synthesis in 3T3 cells
    • Maness, P.F., and Walsh, R.C. (1982) Dihydrocytochalasin B disorganizes actin cytoarchitecture and inhibits initiation of DNA synthesis in 3T3 cells. Cell, 30:253-262.
    • (1982) Cell , vol.30 , pp. 253-262
    • Maness, P.F.1    Walsh, R.C.2
  • 39
    • 0015792646 scopus 로고
    • Growth of fibroblasts on linear and planar anchorages of limiting dimensions
    • Maroudas, N.G. (1973) Growth of fibroblasts on linear and planar anchorages of limiting dimensions. Exp. Cell Res., 81:104-110.
    • (1973) Exp. Cell Res. , vol.81 , pp. 104-110
    • Maroudas, N.G.1
  • 40
    • 0016366562 scopus 로고
    • Action of cytochalasin D on cells of established lines. I. Early events
    • Miranda, A.F., Godman, G.C. Deitch, A.D., and Tanenbaum, S.W. (1974a) Action of cytochalasin D on cells of established lines. I. Early events. J. Cell Biol., 61:481-500.
    • (1974) J. Cell Biol. , vol.61 , pp. 481-500
    • Miranda, A.F.1    Godman, G.C.2    Deitch, A.D.3    Tanenbaum, S.W.4
  • 41
    • 0016234522 scopus 로고
    • Actin of cytochalasin D on cells of established lines. II. Cortex and microfilaments
    • Miranda, A.F., Godman, G.C., and Tanenbaum, S.W. (1974b) Actin of cytochalasin D on cells of established lines. II. Cortex and microfilaments. J. Cell Biol., 62:406-423.
    • (1974) J. Cell Biol. , vol.62 , pp. 406-423
    • Miranda, A.F.1    Godman, G.C.2    Tanenbaum, S.W.3
  • 42
    • 0020440480 scopus 로고
    • Nucleated polymerization of actin from membrane associated ends of microvillar filaments in the intestinal brush border
    • Mooseker, M.S., Pollard, T.D., and Whaton, K.A. (1982) Nucleated polymerization of actin from membrane associated ends of microvillar filaments in the intestinal brush border. J. Cell Biol., 95:223-233.
    • (1982) J. Cell Biol. , vol.95 , pp. 223-233
    • Mooseker, M.S.1    Pollard, T.D.2    Whaton, K.A.3
  • 43
    • 0026321941 scopus 로고
    • Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin
    • Murphy-Ullrich, J.E., Lightner, V.A., Aukhil, I., Yan, Y.Z., Erickson, H.P., and Hook, M. (1991) Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin. J. Cell Biol., 115:1127-1136.
    • (1991) J. Cell Biol. , vol.115 , pp. 1127-1136
    • Murphy-Ullrich, J.E.1    Lightner, V.A.2    Aukhil, I.3    Yan, Y.Z.4    Erickson, H.P.5    Hook, M.6
  • 44
    • 0027231432 scopus 로고
    • Platelet-derived growth factor B chain promoter contains a cis-acting fluid sheer-stress-responsive element
    • Resnick, N., Collins, T., Atkinson, W., Bonthron, D.T., Dewey, C.F., and Gimbrone, M.A. (1993) Platelet-derived growth factor B chain promoter contains a cis-acting fluid sheer-stress-responsive element. Proc. Natl. Acad. Sci. USA, 90:4591-4595.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4591-4595
    • Resnick, N.1    Collins, T.2    Atkinson, W.3    Bonthron, D.T.4    Dewey, C.F.5    Gimbrone, M.A.6
  • 45
    • 0028964437 scopus 로고
    • Cytoskeletal control of gene expression: Depolymerization of microtubules activates NF-κB
    • Rosetti, C., and Karin, M. (1995) Cytoskeletal control of gene expression: Depolymerization of microtubules activates NF-κB. J. Cell Biol., 128:1111-1119.
    • (1995) J. Cell Biol. , vol.128 , pp. 1111-1119
    • Rosetti, C.1    Karin, M.2
  • 46
    • 0023753748 scopus 로고
    • Cytoarchitecture of Kirsten sarcoma virus-transformed rat kidney fibroblasts: Butyrate-induced reorganization within the actin microfilament network
    • Ryan, M.P., and Higgins, P.J. (1988) Cytoarchitecture of Kirsten sarcoma virus-transformed rat kidney fibroblasts: Butyrate-induced reorganization within the actin microfilament network. J. Cell. Physiol., 137:25-34.
    • (1988) J. Cell. Physiol. , vol.137 , pp. 25-34
    • Ryan, M.P.1    Higgins, P.J.2
  • 47
    • 0027294923 scopus 로고
    • Growth state-regulated expression of p52(PAI-1) in normal rat kidney cells
    • Ryan, M.P., and Higgins, P.J. (1993) Growth state-regulated expression of p52(PAI-1) in normal rat kidney cells. J. Cell. Physiol., 155:376-384.
    • (1993) J. Cell. Physiol. , vol.155 , pp. 376-384
    • Ryan, M.P.1    Higgins, P.J.2
  • 48
    • 0029918347 scopus 로고    scopus 로고
    • Complex regulation of plasminogen activator inhibitor type-1 (PAI-1) gene expression by serum and substrate adhesion
    • Ryan, M.P., Kutz, S.M., and Higgins, P.J. (1996) Complex regulation of plasminogen activator inhibitor type-1 (PAI-1) gene expression by serum and substrate adhesion. Biochem. J., 314:1041-1046.
    • (1996) Biochem. J. , vol.314 , pp. 1041-1046
    • Ryan, M.P.1    Kutz, S.M.2    Higgins, P.J.3
  • 49
    • 0028122650 scopus 로고
    • Focal adhesion kinase and associated proteins
    • Schaller, J., and Parsons, J.T. (1994) Focal adhesion kinase and associated proteins. Curr. Opin. Cell Biol., 6:705-710.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 705-710
    • Schaller, J.1    Parsons, J.T.2
  • 50
    • 0020044056 scopus 로고
    • Actin of cytochalasin D on cytoskeletal networks
    • Schliwa, M. (1982) Actin of cytochalasin D on cytoskeletal networks. J. Cell Biol., 92:89-91.
    • (1982) J. Cell Biol. , vol.92 , pp. 89-91
    • Schliwa, M.1
  • 51
    • 0026651718 scopus 로고
    • Stimulation by proinsulin of expression of plasminogen activator inhibitor type-L in endothelial cells
    • Schneider, D.J., Nordt, T.K., and Sobel, B.E. (1992) Stimulation by proinsulin of expression of plasminogen activator inhibitor type-L in endothelial cells. Diabetes, 41:890-895.
    • (1992) Diabetes , vol.41 , pp. 890-895
    • Schneider, D.J.1    Nordt, T.K.2    Sobel, B.E.3
  • 52
    • 2642682442 scopus 로고    scopus 로고
    • Regulation of PAI-1 gene expression in renal cells by distal 5′ flanking elements
    • submitted
    • Slack, J.K., and Higgins, P.J. (1998) Regulation of PAI-1 gene expression in renal cells by distal 5′ flanking elements. Biochem. J. (submitted).
    • (1998) Biochem. J.
    • Slack, J.K.1    Higgins, P.J.2
  • 53
    • 0022447353 scopus 로고
    • Cytochalasin D alters the rate of synthesis of some Hep-2 cytoskeletal proteins. Examination by two-dimensional gel electrophoresis
    • Tannenbaum, J. (1986) Cytochalasin D alters the rate of synthesis of some Hep-2 cytoskeletal proteins. Examination by two-dimensional gel electrophoresis. Eur. J. Biochem., 155:533-542.
    • (1986) Eur. J. Biochem. , vol.155 , pp. 533-542
    • Tannenbaum, J.1
  • 54
    • 0022977704 scopus 로고
    • Reorganization of polymerized actin: A possible trigger for induction of procollagenase in fibroblasts culture in and on collagen gels
    • Unemori, E.N., and Werb, Z. (1986) Reorganization of polymerized actin: A possible trigger for induction of procollagenase in fibroblasts culture in and on collagen gels. J. Cell Biol., 103:1021-1031.
    • (1986) J. Cell Biol. , vol.103 , pp. 1021-1031
    • Unemori, E.N.1    Werb, Z.2
  • 55
    • 0028109926 scopus 로고
    • Genistein reduces tumor necrosis factor α-induced plasminogen activator inhibitor-1 transcription but not urokinase expression in human endothelial cells
    • van Hinsberg, V.W.M., Vermeer, M., Koolwijk, P., Grimbergen, J., and Kooistra, T. (1994) Genistein reduces tumor necrosis factor α-induced plasminogen activator inhibitor-1 transcription but not urokinase expression in human endothelial cells. Blood, 84:2984-2991.
    • (1994) Blood , vol.84 , pp. 2984-2991
    • Van Hinsberg, V.W.M.1    Vermeer, M.2    Koolwijk, P.3    Grimbergen, J.4    Kooistra, T.5
  • 56
    • 0022539752 scopus 로고
    • Commitment to expression of the metalloendopeptidases, collagenase and stromelysin: Relationship of inducing events to changes in cytoskeletal architecture
    • Werb, Z., Hembry, R.M., Murphy, G., and Aggeler, J. (1986) Commitment to expression of the metalloendopeptidases, collagenase and stromelysin: Relationship of inducing events to changes in cytoskeletal architecture. J. Cell Biol., 102:697-702.
    • (1986) J. Cell Biol. , vol.102 , pp. 697-702
    • Werb, Z.1    Hembry, R.M.2    Murphy, G.3    Aggeler, J.4
  • 57
    • 0026033696 scopus 로고
    • Disruption of the cytoskeleton with cytochalasin D induces c-fos gene expression
    • Zambetti, G., Ramsey-Ewing, A., Bortell, R., Stein, G., and Stein, J. (1992) Disruption of the cytoskeleton with cytochalasin D induces c-fos gene expression. Exp. Cell Res., 192:93-101.
    • (1992) Exp. Cell Res. , vol.192 , pp. 93-101
    • Zambetti, G.1    Ramsey-Ewing, A.2    Bortell, R.3    Stein, G.4    Stein, J.5
  • 58
    • 0021254046 scopus 로고
    • Induction of chondrogenesis in limb mesenchymal cultures by disruption of the actin cytoskeleton
    • Zanetti, N.C., and Solursh, M. (1984) Induction of chondrogenesis in limb mesenchymal cultures by disruption of the actin cytoskeleton. J. Cell Biol., 99:115-123.
    • (1984) J. Cell Biol. , vol.99 , pp. 115-123
    • Zanetti, N.C.1    Solursh, M.2


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