메뉴 건너뛰기




Volumn 109, Issue 10, 1996, Pages 2499-2508

Cyclic GMP-dependent protein kinase is required for thrombospondin and tenascin mediated focal adhesion disassembly

Author keywords

Focal adhesion; PKG; SPARC; Tenascin; Thrombospondin

Indexed keywords

CYCLIC GMP DEPENDENT PROTEIN KINASE; MATRIX PROTEIN; TENASCIN; THROMBOSPONDIN;

EID: 0029909499     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (54)

References (84)
  • 1
    • 0000399393 scopus 로고
    • The thrombospondin family
    • Adams, J. and Lawler, J. (1993). The thrombospondin family. Curr. Biol. 3, 188-190.
    • (1993) Curr. Biol. , vol.3 , pp. 188-190
    • Adams, J.1    Lawler, J.2
  • 2
    • 0028339074 scopus 로고
    • Cell-type specific adhesive interactions of skeletal myoblasts with thrombospondin-1
    • Adams, J. C. and Lawler, J. (1994). Cell-type specific adhesive interactions of skeletal myoblasts with thrombospondin-1. Mol. Biol. Cell 5, 423-437.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 423-437
    • Adams, J.C.1    Lawler, J.2
  • 3
    • 0029015719 scopus 로고
    • Formation of stable microspikes containing actin and the 55 kDa actin bundling protein, fascin, is a consequence of cell adhesion to thrombospondin 1: Implications for the anti-adhesive activities of thrombospondin-1
    • Adams, J. C. (1995). Formation of stable microspikes containing actin and the 55 kDa actin bundling protein, fascin, is a consequence of cell adhesion to thrombospondin 1: implications for the anti-adhesive activities of thrombospondin-1. J. Cell Sci. 108, 1977-1990.
    • (1995) J. Cell Sci. , vol.108 , pp. 1977-1990
    • Adams, J.C.1
  • 4
    • 0028297116 scopus 로고
    • Expression of the catalytic domain of cyclic GMP-dependent protein kinase in a baculovirus system
    • Boerth, N. J. and Lincoln, T. M. (1994). Expression of the catalytic domain of cyclic GMP-dependent protein kinase in a baculovirus system. FEBS Lett. 342, 255-260.
    • (1994) FEBS Lett. , vol.342 , pp. 255-260
    • Boerth, N.J.1    Lincoln, T.M.2
  • 6
    • 0026445719 scopus 로고
    • FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
    • FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J. Cell Biol. 119, 893-903.
    • (1992) J. Cell Biol. , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 7
    • 0025250329 scopus 로고
    • Inhibition of cGMP-dependent protein kinase by (Rp)-guanosine 3′,5′-monophosphorothioates
    • Butte, E., Van Bemmelen, M., Fischer, L., Walter, U. and Jastorff, B. (1990). Inhibition of cGMP-dependent protein kinase by (Rp)-guanosine 3′,5′-monophosphorothioates. FEBS Lett. 263, 47-50.
    • (1990) FEBS Lett. , vol.263 , pp. 47-50
    • Butte, E.1    Van Bemmelen, M.2    Fischer, L.3    Walter, U.4    Jastorff, B.5
  • 8
    • 0027939187 scopus 로고
    • Integrin-mediated cell adhesion activates mitogen-activated protein kinases
    • Chen, Q. M., Kinch, M. S., Lin, T. H., Burridge, K. and Juliano, R. L. (1994). Integrin-mediated cell adhesion activates mitogen-activated protein kinases. J. Biol. Chem. 269, 26602-26605.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26602-26605
    • Chen, Q.M.1    Kinch, M.S.2    Lin, T.H.3    Burridge, K.4    Juliano, R.L.5
  • 9
    • 0024279848 scopus 로고
    • Tenascin interferes with fibronectin action
    • Chiquet-Ehrismann, R., Kalla, P. and Pearson, C. A. (1989a). Tenascin interferes with fibronectin action. Cell 53, 383-390.
    • (1989) Cell , vol.53 , pp. 383-390
    • Chiquet-Ehrismann, R.1    Kalla, P.2    Pearson, C.A.3
  • 10
    • 0024382080 scopus 로고
    • Participation of tenascin and TGF-β in reciprocal epithelial-mesenchymal interactions of MCF7 cells and fibroblasts
    • Chiquet-Ehrismann, R., Kalla, R. and Pearson, C. A. (1989b). Participation of tenascin and TGF-β in reciprocal epithelial-mesenchymal interactions of MCF7 cells and fibroblasts. Cancer Res. 49, 4322-4325.
    • (1989) Cancer Res. , vol.49 , pp. 4322-4325
    • Chiquet-Ehrismann, R.1    Kalla, R.2    Pearson, C.A.3
  • 11
    • 0026244872 scopus 로고
    • Anti-adhesive molecules of the extracellular matrix
    • Chiquet-Ehrismann, R. (1991). Anti-adhesive molecules of the extracellular matrix. Curr. Opin. Cell Biol. 3, 800-804.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 800-804
    • Chiquet-Ehrismann, R.1
  • 12
    • 0028305739 scopus 로고
    • Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C
    • Chung, C. Y. and Erickson, H. P. (1994). Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C. J. Cell Biol. 126, 539-548.
    • (1994) J. Cell Biol. , vol.126 , pp. 539-548
    • Chung, C.Y.1    Erickson, H.P.2
  • 13
    • 0030003154 scopus 로고    scopus 로고
    • Mitogenesis, cell migration and loss of focal adhesions induced by tenascin-C interacting with its cell surface receptor, annexin II
    • Chung, C. Y., Murphy-Ullrich, J. E. and Erickson, H. P. (1996). Mitogenesis, cell migration and loss of focal adhesions induced by tenascin-C interacting with its cell surface receptor, annexin II. Mol. Biol. Cell 7, 883-892.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 883-892
    • Chung, C.Y.1    Murphy-Ullrich, J.E.2    Erickson, H.P.3
  • 14
    • 0024476861 scopus 로고
    • 2+ by atriopeptin and 8-bromo-cyclic GMP is mediated by cyclic GMP-dependent protein kinase
    • 2+ by atriopeptin and 8-bromo-cyclic GMP is mediated by cyclic GMP-dependent protein kinase. J. Biol. Chem. 264, 1146-1155.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1146-1155
    • Cornwell, T.L.1    Lincoln, T.M.2
  • 15
    • 0027986509 scopus 로고
    • Inhibition of smooth muscle cell growth by nitric oxide and activation of cAMP-dependent protein kinase by cGMP
    • Cell Physiol. 36
    • Cornwell, T. L., Arnold, E., Boerth, N. J. and Lincoln, T. M. (1994a). Inhibition of smooth muscle cell growth by nitric oxide and activation of cAMP-dependent protein kinase by cGMP. Am. J. Physiol. 267 (Cell Physiol. 36), C1405-C1413.
    • (1994) Am. J. Physiol. , vol.267
    • Cornwell, T.L.1    Arnold, E.2    Boerth, N.J.3    Lincoln, T.M.4
  • 16
    • 0027946487 scopus 로고
    • Regulation of the expression of cyclic GMP-dependent protein kinase by cell density in vascular smooth muscle cells
    • Cornwell, T. L., Soff, G. A., Traynor, A. E. and Lincoln, T. M. (1994b). Regulation of the expression of cyclic GMP-dependent protein kinase by cell density in vascular smooth muscle cells. J. Vasc. Res. 31, 330-337.
    • (1994) J. Vasc. Res. , vol.31 , pp. 330-337
    • Cornwell, T.L.1    Soff, G.A.2    Traynor, A.E.3    Lincoln, T.M.4
  • 17
    • 0018651705 scopus 로고
    • The behaviour of fibroblasts migrating from chick heart explants: Changes in adhesion, locomotion, and growth, and in the distribution of actomyosin and fibronectin
    • Couchman, J. R. and Rees, D. A. (1979). The behaviour of fibroblasts migrating from chick heart explants: changes in adhesion, locomotion, and growth, and in the distribution of actomyosin and fibronectin. J. Cell Sci. 39, 149-165.
    • (1979) J. Cell Sci. , vol.39 , pp. 149-165
    • Couchman, J.R.1    Rees, D.A.2
  • 18
    • 0026938957 scopus 로고
    • Signal transduction from the extracellular matrix: Cooperative processing of extracellular information
    • Damsky, C. and Werb, Z. (1992). Signal transduction from the 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.1    Werb, Z.2
  • 19
    • 0028071546 scopus 로고
    • Cyclic GMP-dependent protein kinase activity in rat pulmonary microvascular endothelial cells
    • Diwan, A. H., Thompson, W. J., Lee, A. K. and Strada, S. S. (1994). Cyclic GMP-dependent protein kinase activity in rat pulmonary microvascular endothelial cells. Biochem. Biophys. Res. Commun. 202, 728-735.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 728-735
    • Diwan, A.H.1    Thompson, W.J.2    Lee, A.K.3    Strada, S.S.4
  • 20
    • 0028887945 scopus 로고
    • Interleukin-8 induces motile behavior and loss of focal adhesions in primary fibroblasts
    • Dunlevy, J. R. and Couchman, J. R. (1995). Interleukin-8 induces motile behavior and loss of focal adhesions in primary fibroblasts. J. Cell Sci. 108, 311-321.
    • (1995) J. Cell Sci. , vol.108 , pp. 311-321
    • Dunlevy, J.R.1    Couchman, J.R.2
  • 21
    • 0027685702 scopus 로고
    • Tenascin-C, tenascin-R, and teanscin-X: A family of talented proteins in search of functions
    • Erickson, H. P. (1993). Tenascin-C, tenascin-R, and teanscin-X: a family of talented proteins in search of functions. Curr Opin. Cell Biol. 5, 869-876.
    • (1993) Curr Opin. Cell Biol. , vol.5 , pp. 869-876
    • Erickson, H.P.1
  • 23
    • 0027508511 scopus 로고
    • Regulation of integrin-mediated adhesion at focal contacts by cyclic AMP
    • Glass, W. F. and Kreisberg, J. I. (1993). Regulation of integrin-mediated adhesion at focal contacts by cyclic AMP. J. Cell Physiol. 157, 296-306.
    • (1993) J. Cell Physiol. , vol.157 , pp. 296-306
    • Glass, W.F.1    Kreisberg, J.I.2
  • 25
    • 0016820947 scopus 로고
    • Femtomole sensitivity radioimmunoassay for cyclic AMP and cyclic GMP after 2′0 acetylation by acetic anhydride in aqueous solution
    • Harper, J. F. and Brooker, G. (1975). Femtomole sensitivity radioimmunoassay for cyclic AMP and cyclic GMP after 2′0 acetylation by acetic anhydride in aqueous solution. J. Cyclic Nucl. Res. 1, 207-218.
    • (1975) J. Cyclic Nucl. Res. , vol.1 , pp. 207-218
    • Harper, J.F.1    Brooker, G.2
  • 26
    • 0021956239 scopus 로고
    • Platelet-derived growth factor-induced alterations in vinculin and actin distribution in BALB/c-3T3 cells
    • Herman, B. and Pledger, W. J. (1985). Platelet-derived growth factor-induced alterations in vinculin and actin distribution in BALB/c-3T3 cells. J. Cell Biol. 100, 1031-1040.
    • (1985) J. Cell Biol. , vol.100 , pp. 1031-1040
    • Herman, B.1    Pledger, W.J.2
  • 27
    • 0022653593 scopus 로고
    • Identification of the cellular mechanisms responsible for platelet-derived growth factor induced alterations in cytoplasmic vinculin distribution
    • Herman, B., Harrington, M. A., Olashaw, N. E. and Pledger, W. J. (1986). Identification of the cellular mechanisms responsible for platelet-derived growth factor induced alterations in cytoplasmic vinculin distribution. J. Cell Physiol. 126, 115-125.
    • (1986) J. Cell Physiol. , vol.126 , pp. 115-125
    • Herman, B.1    Harrington, M.A.2    Olashaw, N.E.3    Pledger, W.J.4
  • 28
    • 0023637991 scopus 로고
    • Platelet-derived growth factor-induced alterations in vinculin distribution in porcine vascular smooth muscle cells
    • Herman, B., Roe, M. W., Harris, C., Wray, B. and Clemmons, D. (1987). Platelet-derived growth factor-induced alterations in vinculin distribution in porcine vascular smooth muscle cells. Cell Motil. Cytoskel. 8, 91-105.
    • (1987) Cell Motil. Cytoskel. , vol.8 , pp. 91-105
    • Herman, B.1    Roe, M.W.2    Harris, C.3    Wray, B.4    Clemmons, D.5
  • 29
    • 0021806633 scopus 로고
    • Diastereomersof adenosine 3′,5′-monothionophosphate (cAMP{S}) antagonize the activation of cGMP-dependent protein kinase
    • Hofmann, F., Gensheimer, H. P., Landgraf, W., Hullin, R. and Jastorff, B. (1985). Diastereomersof adenosine 3′,5′-monothionophosphate (cAMP{S}) antagonize the activation of cGMP-dependent protein kinase. Eur. J. Biochem. 150, 85-88.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 85-88
    • Hofmann, F.1    Gensheimer, H.P.2    Landgraf, W.3    Hullin, R.4    Jastorff, B.5
  • 31
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signaling in cell adhesion
    • Hynes, R. O. (1992). Integrins: versatility, modulation and signaling in cell adhesion. Cell 69, 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 32
    • 0027221483 scopus 로고
    • Cellular tensegrity: Defining new rules of biological design that govern the cytoskeleton
    • Ingber, D. E. (1993). Cellular tensegrity: defining 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.E.1
  • 33
    • 0026570943 scopus 로고
    • Direct evidence for cross-activation of cGMP-dependent protein kinase by cAMP in pig coronary arteries
    • Jiang, H., Colbran, J. L., Francis, S. H. and Corbin, J. D. (1992). Direct evidence for cross-activation of cGMP-dependent protein kinase by cAMP in pig coronary arteries. J. Biol. Chem. 267, 1015-1019.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1015-1019
    • Jiang, H.1    Colbran, J.L.2    Francis, S.H.3    Corbin, J.D.4
  • 34
    • 0027459771 scopus 로고
    • Signal transduction from the extracellular matrix
    • Juliano, R. L. and Haskill, S. (1993). Signal transduction from the extracellular matrix. J. Cell Biol. 120, 577-585.
    • (1993) J. Cell Biol. , vol.120 , pp. 577-585
    • Juliano, R.L.1    Haskill, S.2
  • 36
    • 0023676512 scopus 로고
    • Thrombospondin inhibits adhesion of endothelial cells
    • Lahav, J. (1988). Thrombospondin inhibits adhesion of endothelial cells. Exp. Cell Res. 177, 3290-3299.
    • (1988) Exp. Cell Res. , vol.177 , pp. 3290-3299
    • Lahav, J.1
  • 37
    • 0027319916 scopus 로고
    • The functions of thrombospondin and its involvement in physiology and pathophysiology
    • Lahav, J. (1993). The functions of thrombospondin and its involvement in physiology and pathophysiology. Biochim. Biophys. Acta 1182, 1-14.
    • (1993) Biochim. Biophys. Acta , vol.1182 , pp. 1-14
    • Lahav, J.1
  • 38
    • 0023695794 scopus 로고
    • Regulation of actin microfilament integrity in living nonmuscle cells by the cAMP-dependent protein kinase and the myosin light chain kinase
    • Lamb, N. J. C., Fernandez, A., Conti, M. A., Adelstein, R., Glass, D. B., Welch, W. J. and Fermaisco, J. R. (1988). Regulation of actin microfilament integrity in living nonmuscle cells by the cAMP-dependent protein kinase and the myosin light chain kinase. J. Cell Biol. 106, 1955-1971.
    • (1988) J. Cell Biol. , vol.106 , pp. 1955-1971
    • Lamb, N.J.C.1    Fernandez, A.2    Conti, M.A.3    Adelstein, R.4    Glass, D.B.5    Welch, W.J.6    Fermaisco, J.R.7
  • 39
    • 0025609345 scopus 로고
    • 2+-binding sites modulate cell shape
    • 2+-binding sites modulate cell shape. J. Cell Biol. 111, 3065-3076.
    • (1990) J. Cell Biol. , vol.111 , pp. 3065-3076
    • Lane, T.F.1    Sage, E.H.2
  • 40
    • 23444459571 scopus 로고
    • The biology of SPARC, a protein that modulates cell-matrix interactions
    • Lane, T. F. and Sage, E. H. (1994). The biology of SPARC, a protein that modulates cell-matrix interactions. FASEB J. 8, 163-173.
    • (1994) FASEB J. , vol.8 , pp. 163-173
    • Lane, T.F.1    Sage, E.H.2
  • 41
    • 0025098987 scopus 로고
    • Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion
    • Lightner, V. A. and Erickson, H. P. (1990). Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion. J. Cell Sci. 95, 263-277.
    • (1990) J. Cell Sci. , vol.95 , pp. 263-277
    • Lightner, V.A.1    Erickson, H.P.2
  • 43
    • 0027404913 scopus 로고
    • Intracellular cyclic GMP receptor proteins
    • Lincoln, T. M. and Cornwell, T. L. (1993). Intracellular cyclic GMP receptor proteins. FASEB J. 7, 328-338.
    • (1993) FASEB J. , vol.7 , pp. 328-338
    • Lincoln, T.M.1    Cornwell, T.L.2
  • 45
    • 0028047388 scopus 로고
    • Focal adhesions as a signal transduction organelle
    • Lo, S. H. and Chen, L. B. (1994). Focal adhesions as a signal transduction organelle. Cancer Metast. Rev. 13, 9-24.
    • (1994) Cancer Metast. Rev. , vol.13 , pp. 9-24
    • Lo, S.H.1    Chen, L.B.2
  • 46
    • 0024461009 scopus 로고
    • Cell adhesion to fibronectin and tenascin: Quantitative measurements of initial binding and subsequent strengthening response
    • Lotz, M. M., Burdsal, C. A., Erickson, H. P. and McClay, D. R. (1989). Cell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response. J. Cell Biol. 109, 1795-1805.
    • (1989) J. Cell Biol. , vol.109 , pp. 1795-1805
    • Lotz, M.M.1    Burdsal, C.A.2    Erickson, H.P.3    McClay, D.R.4
  • 47
    • 0028339988 scopus 로고
    • Identification and possible localization of cGMP-dependent protein kinase in bovine aortic endothelial cells
    • MacMillan-Crow, L., Murphy-Ullrich, J. E. and Lincoln, T. M. (1994). Identification and possible localization of cGMP-dependent protein kinase in bovine aortic endothelial cells. Biochem. Biophys. Res. Commun. 201, 531-537.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 531-537
    • MacMillan-Crow, L.1    Murphy-Ullrich, J.E.2    Lincoln, T.M.3
  • 48
    • 0023664529 scopus 로고
    • Induction of thrombospondin messenger RNA levels occurs as an immediate primary response to platelet-derived growth factor
    • Majack, R. A., Milbrandt, J. and Dixit, V. M. (1987). Induction of thrombospondin messenger RNA levels occurs as an immediate primary response to platelet-derived growth factor. J. Biol. Chem. 262, 8821-8825.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8821-8825
    • Majack, R.A.1    Milbrandt, J.2    Dixit, V.M.3
  • 49
    • 0027428648 scopus 로고
    • Nitric oxide regulates luteinizing hormone-releasing hormone secretion
    • Moretto, M., Lopez, F. J. and Negro-Vilar, A. (1993). Nitric oxide regulates luteinizing hormone-releasing hormone secretion. Endocrinology 133, 2399-2402.
    • (1993) Endocrinology , vol.133 , pp. 2399-2402
    • Moretto, M.1    Lopez, F.J.2    Negro-Vilar, A.3
  • 50
    • 0023367879 scopus 로고
    • Interactions of thrombospondin with cells culture: Rapid degradation of both soluble and matrix thrombospondin
    • Murphy-Ullrich, J. E. and Mosher, D. F. (1987). Interactions of thrombospondin with cells culture: rapid degradation of both soluble and matrix thrombospondin. Semin. Thromb. Hemost. 13, 343-351.
    • (1987) Semin. Thromb. Hemost. , vol.13 , pp. 343-351
    • Murphy-Ullrich, J.E.1    Mosher, D.F.2
  • 51
    • 0024415409 scopus 로고
    • Thrombospondin modulates focal adhesions in endothelial cells
    • Murphy-Ullrich, J. E. and Höök, M. (1989). Thrombospondin modulates focal adhesions in endothelial cells. J. Cell Biol. 109, 1309-1919.
    • (1989) J. Cell Biol. , vol.109 , pp. 1309-1919
    • Murphy-Ullrich, J.E.1    Höök, M.2
  • 52
    • 0026321941 scopus 로고
    • Focal adhesion integrity is downregulated by the alternatively spliced domain of tenascin
    • Murphy-Ullrich, J. E., Lightner, V. A., Aukhil, I., Yan, Y. Z., Erickson, H. P. and Höök, M. (1991). Focal adhesion integrity is downregulated by the alternatively spliced domain of 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    Höök, M.6
  • 53
    • 0027377783 scopus 로고
    • Heparin-binding peptides from thrombospondins 1 and 2 contain focal adhesion-labilizing activity
    • Murphy-Ullrich, J. E., Gurusiddappa, S., Frazier, W. A. and Höök, M. (1993). Heparin-binding peptides from thrombospondins 1 and 2 contain focal adhesion-labilizing activity. J. Biol. Chem. 268, 26784-26789.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26784-26789
    • Murphy-Ullrich, J.E.1    Gurusiddappa, S.2    Frazier, W.A.3    Höök, M.4
  • 54
    • 84998446072 scopus 로고
    • Anti-adhesive proteins of the extracellular matrix: Thrombospondin, tenascin, and SPARC
    • Murphy-Ullrich, J. E. (1995). Anti-adhesive proteins of the extracellular matrix: thrombospondin, tenascin, and SPARC. Trends Glycosci. Glycotechnol. 7, 89-100.
    • (1995) Trends Glycosci. Glycotechnol. , vol.7 , pp. 89-100
    • Murphy-Ullrich, J.E.1
  • 56
    • 0028961293 scopus 로고
    • Rho. Rac, and Cdc42 GTPases regulates the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D. and Hall, A. (1995) Rho. Rac, and Cdc42 GTPases regulates the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 57
    • 0343292988 scopus 로고
    • Transforming growth factor β increases mRNA for matrix proteins both in the presence and in the absence of changes in mRNA stability
    • Penttinen, R. O., Kobayashi, S. and Bornstein, P. (1988). Transforming growth factor β increases mRNA for matrix proteins both in the presence and in the absence of changes in mRNA stability. Proc. Nat. Acad. Sci. USA 85, 1105-1108.
    • (1988) Proc. Nat. Acad. Sci. USA , vol.85 , pp. 1105-1108
    • Penttinen, R.O.1    Kobayashi, S.2    Bornstein, P.3
  • 58
    • 0026732724 scopus 로고
    • Characterization of multiple adhesive and counteradhesive domains in the extracellular matrix protein cytotactin
    • Prieto, A. L., Andersson-Fisone, C. and Crossin, K. L. (1992). Characterization of multiple adhesive and counteradhesive domains in the extracellular matrix protein cytotactin. J. Cell Biol. 119, 663-678.
    • (1992) J. Cell Biol. , vol.119 , pp. 663-678
    • Prieto, A.L.1    Andersson-Fisone, C.2    Crossin, K.L.3
  • 59
    • 0028843028 scopus 로고
    • Cyclic guanosine monophosphate-dependent protein kinase is targeted to intermediate filaments and phosphorylates vimentin in A23187-stimulated human neutrophils
    • Pryzwansky, K.B., Wyatt, J. A. and Lincoln, T. M. (1995). Cyclic guanosine monophosphate-dependent protein kinase is targeted to intermediate filaments and phosphorylates vimentin in A23187-stimulated human neutrophils. Blood 85, 222-230.
    • (1995) Blood , vol.85 , pp. 222-230
    • Pryzwansky, K.B.1    Wyatt, J.A.2    Lincoln, T.M.3
  • 60
    • 0025976932 scopus 로고
    • Interleukin 1β induces rapid phosphorylation and redistribution of talin: A possible mechanism for modulation of fibroblast focal adhesions
    • Qwarnström, E. E., MacFarlane, S. A., Page, R. C. and Dower, S. K. (1991). Interleukin 1β induces rapid phosphorylation and redistribution of talin: a possible mechanism for modulation of fibroblast focal adhesions. Proc. Nat. Acad. Sci USA 88, 1232-1236.
    • (1991) Proc. Nat. Acad. Sci USA , vol.88 , pp. 1232-1236
    • Qwarnström, E.E.1    MacFarlane, S.A.2    Page, R.C.3    Dower, S.K.4
  • 61
    • 0026563095 scopus 로고
    • The 46/50 kDa VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts
    • Reinhard, M., Halbrugge, M., Sheer, U., Wiegand, C., Jockbusch, B. M. and Walter, U. (1992). The 46/50 kDa VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts. EMBO J. 11, 2063-2070.
    • (1992) EMBO J. , vol.11 , pp. 2063-2070
    • Reinhard, M.1    Halbrugge, M.2    Sheer, U.3    Wiegand, C.4    Jockbusch, B.M.5    Walter, U.6
  • 62
    • 0029025248 scopus 로고
    • The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins
    • Reinhard, M., Giehl, K., Abel, K., Haffner, C., Jarchau, T., Hoppe, V., Jockusch, B. M and Walter, U. (1995a). The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins. EMBO J. 14, 1583-1589.
    • (1995) EMBO J. , vol.14 , pp. 1583-1589
    • Reinhard, M.1    Giehl, K.2    Abel, K.3    Haffner, C.4    Jarchau, T.5    Hoppe, V.6    Jockusch, B.M.7    Walter, U.8
  • 63
    • 0029157584 scopus 로고
    • Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein)
    • Reinhard, M., Jouvenal, K., Tripier, D. and Walter, U. (1995b). Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). Proc. Nat. Acad. Sci. USA 92, 7956-7960.
    • (1995) Proc. Nat. Acad. Sci. USA , vol.92 , pp. 7956-7960
    • Reinhard, M.1    Jouvenal, K.2    Tripier, D.3    Walter, U.4
  • 64
    • 0028321785 scopus 로고
    • Signal transaction pathways regulating rho-mediated stress fiber formation: Requirement for a tyrosine kinase
    • Ridley, A. J. and Hall, A. (1994). Signal transaction pathways regulating rho-mediated stress fiber formation: requirement for a tyrosine kinase. EMBO J. 13, 2600-2610.
    • (1994) EMBO J. , vol.13 , pp. 2600-2610
    • Ridley, A.J.1    Hall, A.2
  • 67
    • 0024312865 scopus 로고
    • Distribution of the calcium-binding protein SPARC in tissues of embryonic and adult mice
    • Sage, E. H., Vernon, R. B., Decker, J., Funk, S. and Iruela-Arispe, M. L. (1989). Distribution of the calcium-binding protein SPARC in tissues of embryonic and adult mice. J. Histochem. Cytochem. 37, 819-829.
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 819-829
    • Sage, E.H.1    Vernon, R.B.2    Decker, J.3    Funk, S.4    Iruela-Arispe, M.L.5
  • 68
    • 0025823515 scopus 로고
    • Extracellular proteins that modulate cell-matrix interactions: SPARC, tenascin, and thrombospondin
    • Sage, E. H. and Bornstein, P. (1991). Extracellular proteins that modulate cell-matrix interactions: SPARC, tenascin, and thrombospondin. J. Biol. Chem. 266, 14831-14834.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14831-14834
    • Sage, E.H.1    Bornstein, P.2
  • 70
    • 0021210339 scopus 로고
    • A tumor promotor induces rapid and coordinated reorganization of actin and vinculin in cultured cells
    • Schliwa, M., Nakamura, T., Porter, K. R. and Eutneneuer, U. (1984). A tumor promotor induces rapid and coordinated reorganization of actin and vinculin in cultured cells. J. Cell Biol. 99, 1045-1059.
    • (1984) J. Cell Biol. , vol.99 , pp. 1045-1059
    • Schliwa, M.1    Nakamura, T.2    Porter, K.R.3    Eutneneuer, U.4
  • 71
    • 0026674188 scopus 로고
    • Transmembrane signalling by integrins
    • Schwartz, M. A. (1992). Transmembrane signalling by integrins. Trends Cell Biol. 2, 304-308.
    • (1992) Trends Cell Biol. , vol.2 , pp. 304-308
    • Schwartz, M.A.1
  • 72
    • 0027090097 scopus 로고
    • Altering the cellular mechanical force results in integrated changes in cell, cytoskeletal and nuclear shape
    • Sims, J. R., Karp, S. and Ingber, D. E. (1992). Altering the cellular mechanical force results in integrated changes in cell, cytoskeletal and nuclear shape. J. Cell Science 103, 1215-1222.
    • (1992) J. Cell Science , vol.103 , pp. 1215-1222
    • Sims, J.R.1    Karp, S.2    Ingber, D.E.3
  • 73
    • 0024347096 scopus 로고
    • Two contrary functions of tenascin: Dissection of the active sites by recombinant tenascin fragments
    • Spring, J., Beck, K. and Chiquet-Ehrismann, R. (1989). Two contrary functions of tenascin: dissection of the active sites by recombinant tenascin fragments. Cell 59, 325-334.
    • (1989) Cell , vol.59 , pp. 325-334
    • Spring, J.1    Beck, K.2    Chiquet-Ehrismann, R.3
  • 74
    • 0027303968 scopus 로고
    • Endothelial cell attachment and spreading on human tenascin is mediated by α2β1 and αvβ3 integrins
    • Sriramarao, P., Mendler, M. and Bourdon, M. A. (1993). Endothelial cell attachment and spreading on human tenascin is mediated by α2β1 and αvβ3 integrins. J. Cell Sci. 105, 1001-1012.
    • (1993) J. Cell Sci. , vol.105 , pp. 1001-1012
    • Sriramarao, P.1    Mendler, M.2    Bourdon, M.A.3
  • 76
    • 0027424314 scopus 로고
    • PDGF stimulation induces phosphorylation of talin and cytoskeletal reorganization in skeletal muscle
    • Tidball, J. G. and Spencer, M. J. (1993). PDGF stimulation induces phosphorylation of talin and cytoskeletal reorganization in skeletal muscle. J. Cell Biol. 123, 627-635.
    • (1993) J. Cell Biol. , vol.123 , pp. 627-635
    • Tidball, J.G.1    Spencer, M.J.2
  • 77
    • 0027409130 scopus 로고
    • The in situ localization of tenascin splice variants and thrombospondin 2 mRNA in the avian embryo
    • Tucker, R. P. (1993). The in situ localization of tenascin splice variants and thrombospondin 2 mRNA in the avian embryo. Development 117, 347-358.
    • (1993) Development , vol.117 , pp. 347-358
    • Tucker, R.P.1
  • 78
    • 0024379267 scopus 로고
    • The role of phosphorylation and limited proteolytic cleavage of talin and vinculin in the disruption of focal adhesion integrity
    • Turner, C. E., Pavalko, F. M. and Burridge, K. (1989). The role of phosphorylation and limited proteolytic cleavage of talin and vinculin in the disruption of focal adhesion integrity. J. Biol. Chem. 264, 11938-11944.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11938-11944
    • Turner, C.E.1    Pavalko, F.M.2    Burridge, K.3
  • 79
    • 0026042575 scopus 로고
    • Paxillin is a major phosphotyrosine-containing protein during embryonic development
    • Turner, C. E. (1991). Paxillin is a major phosphotyrosine-containing protein during embryonic development. J. Cell Biol. 115, 201-207.
    • (1991) J. Cell Biol. , vol.115 , pp. 201-207
    • Turner, C.E.1
  • 80
    • 0026603414 scopus 로고
    • Protein kinase C involvement in focal adhesion formation
    • Woods, A. and Couchman, J. R. (1992). Protein kinase C involvement in focal adhesion formation. J. Cell Sci. 101, 277-290.
    • (1992) J. Cell Sci. , vol.101 , pp. 277-290
    • Woods, A.1    Couchman, J.R.2
  • 81
    • 0028213641 scopus 로고
    • Syndecan 4 heparan sulfate proteoglycan is a selectively enriched and widespread focal adhesion component
    • Woods, A. and Couchman, J. R. (1994). Syndecan 4 heparan sulfate proteoglycan is a selectively enriched and widespread focal adhesion component. Mol. Biol. Cell 5, 183-192.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 183-192
    • Woods, A.1    Couchman, J.R.2
  • 82
    • 0025833747 scopus 로고
    • Vimentin is transiently co-localized with and phosphorylated by cyclic GMP-dependent protein kinase in formyl-peptide stimulated neutrophils
    • Wyatt, T. A., Lincoln, T. M. and Pryzwansky, K. B. (1991). Vimentin is transiently co-localized with and phosphorylated by cyclic GMP-dependent protein kinase in formyl-peptide stimulated neutrophils. J. Biol. Chem. 266, 21274-21280.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21274-21280
    • Wyatt, T.A.1    Lincoln, T.M.2    Pryzwansky, K.B.3
  • 83
    • 0027200752 scopus 로고
    • Regulation of human neutrophil degranulation by LY-83583 and L-arginine: Role of cGMP-dependent protein kinase
    • Cell Physiol 34
    • Wyatt, T. A., Lincoln, T. M. and Pryzwansky, K. B. (1993). Regulation of human neutrophil degranulation by LY-83583 and L-arginine: role of cGMP-dependent protein kinase. Am. J. Physiol. 265 (Cell Physiol 34), C201-C211.
    • (1993) Am. J. Physiol. , vol.265
    • Wyatt, T.A.1    Lincoln, T.M.2    Pryzwansky, K.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.