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Volumn 276, Issue 6 20-6, 1999, Pages

Regulation of endothelial cell myosin light chain kinase by Rho, cortactin, and p60(src)

Author keywords

Endothelial cell contraction; Myosin phosphorylation; Permeability; Src kinases

Indexed keywords

CORTACTIN; EXOTOXIN; KT 5926; MYOSIN; MYOSIN LIGHT CHAIN KINASE; PHOSPHATASE; PROTEIN KINASE P60; PROTEIN TYROSINE KINASE; RHO FACTOR; VANADIC ACID;

EID: 0033060019     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1999.276.6.l989     Document Type: Article
Times cited : (164)

References (54)
  • 1
    • 0019348630 scopus 로고
    • The role of phosphorylation in regulating contractile proteins
    • Adelstein, R. S., M. D. Pato, and M. A. Conti. The role of phosphorylation in regulating contractile proteins. Adv. Cyclic Nucleotide Res. 14: 361-373, 1981.
    • (1981) Adv. Cyclic Nucleotide Res. , vol.14 , pp. 361-373
    • Adelstein, R.S.1    Pato, M.D.2    Conti, M.A.3
  • 3
    • 0022552257 scopus 로고
    • Vasoconstriction: A new action for platelet-derived growth factor
    • Berk, B. C., R. W. Alexander, T. A. Brock, M. A. Gimbrone, and R. C. Webb. Vasoconstriction: a new action for platelet-derived growth factor. Science 232: 87-90, 1986.
    • (1986) Science , vol.232 , pp. 87-90
    • Berk, B.C.1    Alexander, R.W.2    Brock, T.A.3    Gimbrone, M.A.4    Webb, R.C.5
  • 4
    • 0029614706 scopus 로고
    • Peroxovanadium compounds: Biological actions and mechanism of insulin-mimesis
    • Bevan, A. P., P. G. Drake, J. F. Yale, A. Shaver, and B. I. Posner. Peroxovanadium compounds: biological actions and mechanism of insulin-mimesis. Mol. Cell. Biochem. 153: 49-58, 1995.
    • (1995) Mol. Cell. Biochem. , vol.153 , pp. 49-58
    • Bevan, A.P.1    Drake, P.G.2    Yale, J.F.3    Shaver, A.4    Posner, B.I.5
  • 5
    • 0026058812 scopus 로고
    • Myosin phosphorylation/dephosphorylation and regulation of airway smooth muscle contractility
    • Lung Cell. Mol. Physiol. 5
    • DeLanerolle, P., and R. J. Paul. Myosin phosphorylation/dephosphorylation and regulation of airway smooth muscle contractility. Am. J. Physiol. 261 (Lung Cell. Mol. Physiol. 5): L1-L14, 1991.
    • (1991) Am. J. Physiol. , vol.261
    • DeLanerolle, P.1    Paul, R.J.2
  • 7
    • 0027291402 scopus 로고
    • Vanadate-induced contraction of smooth muscle and enhanced protein tyrosine phosphorylation
    • Di Salvo, J., L. A. Semenchuk, and J. Lauer. Vanadate-induced contraction of smooth muscle and enhanced protein tyrosine phosphorylation. Arch. Biochem. Biophys. 304: 386-391, 1993.
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 386-391
    • Di Salvo, J.1    Semenchuk, L.A.2    Lauer, J.3
  • 10
    • 0029012398 scopus 로고
    • Regulation of endothelial cell gap formation and barrier dysfunction: Role of myosin light chain phosphorylation
    • Garcia, J. G. N., H. W. Davis, and C. E. Patterson. Regulation of endothelial cell gap formation and barrier dysfunction: role of myosin light chain phosphorylation. J. Cell. Physiol. 163: 510-522, 1995.
    • (1995) J. Cell. Physiol. , vol.163 , pp. 510-522
    • Garcia, J.G.N.1    Davis, H.W.2    Patterson, C.E.3
  • 11
    • 0345624690 scopus 로고    scopus 로고
    • Regulation of myosin phosphorylation and barrier function in endothelium
    • Armonk, NY: Futura
    • Garcia, J. G. N., and L. I. Gilbert-McClain. Regulation of myosin phosphorylation and barrier function in endothelium. In: Pulmonary Edema. Armonk, NY: Futura, 1998, p. 261-273.
    • (1998) Pulmonary Edema. , pp. 261-273
    • Garcia, J.G.N.1    Gilbert-McClain, L.I.2
  • 13
    • 0029283128 scopus 로고
    • Regulation of endothelial cell gap formation and paracellular permeability
    • Garcia, J. G. N., and K. L. Schaphorst. Regulation of endothelial cell gap formation and paracellular permeability. J. Investig. Med. 43: 117-126, 1995.
    • (1995) J. Investig. Med. , vol.43 , pp. 117-126
    • Garcia, J.G.N.1    Schaphorst, K.L.2
  • 15
    • 0031958291 scopus 로고    scopus 로고
    • Adherent neutrophils activate endothelial myosin light chain kinase: Role in transendothelial migration
    • Garcia, J. G. N., A. D. Verin, M. Herenyiova, and D. English. Adherent neutrophils activate endothelial myosin light chain kinase: role in transendothelial migration. J. Appl. Physiol. 84: 1817-1821, 1998.
    • (1998) J. Appl. Physiol. , vol.84 , pp. 1817-1821
    • Garcia, J.G.N.1    Verin, A.D.2    Herenyiova, M.3    English, D.4
  • 16
    • 0032127329 scopus 로고    scopus 로고
    • Regulation of endothelial cell myosin light chain phosphorylation and permeability by vanadate
    • Gilbert-McClain, L. I., A. D. Verin, S. Shi, R. P. Irwin, and J. G. N. Garcia. Regulation of endothelial cell myosin light chain phosphorylation and permeability by vanadate. J. Cell. Biochem. 70: 141-155, 1998.
    • (1998) J. Cell. Biochem. , vol.70 , pp. 141-155
    • Gilbert-McClain, L.I.1    Verin, A.D.2    Shi, S.3    Irwin, R.P.4    Garcia, J.G.N.5
  • 17
    • 0025193521 scopus 로고
    • 2 and vanadate stimulate protein tyrosine phosphorylation in intact cells
    • 2 and vanadate stimulate protein tyrosine phosphorylation in intact cells. J. Biol. Chem. 265: 2896-2902, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2896-2902
    • Hefletz, D.1    Bushkin, I.2    Dror, R.3    Zick, Y.4
  • 18
    • 33751291473 scopus 로고    scopus 로고
    • Stimulated neutrophils induce myosin light chain phosphorylation and isometric tension in endothelial cells
    • Heart Circ. Physiol. 42
    • Hixenbaugh, E. A., Z. M. Goeckeler., N. N. Papaiya, R. B. Wysolmerski, S. C. Silverstein, and A. J. Huang. Stimulated neutrophils induce myosin light chain phosphorylation and isometric tension in endothelial cells. Am. J. Physiol. 273 (Heart Circ. Physiol. 42): H981-H988, 1997.
    • (1997) Am. J. Physiol. , vol.273
    • Hixenbaugh, E.A.1    Goeckeler, Z.M.2    Papaiya, N.N.3    Wysolmerski, R.B.4    Silverstein, S.C.5    Huang, A.J.6
  • 19
    • 0027460296 scopus 로고
    • Endothelial cell cytosolic free calcium regulates neutrophil migration across monolayers of endothelial cells
    • Huang, A. J., J. E. Manning, T. M. Bandak, M. C. Ratau, K. R. Hanser, and S. C. Silverstein. Endothelial cell cytosolic free calcium regulates neutrophil migration across monolayers of endothelial cells. J. Cell Biol. 120: 1371-1380, 1993.
    • (1993) J. Cell Biol. , vol.120 , pp. 1371-1380
    • Huang, A.J.1    Manning, J.E.2    Bandak, T.M.3    Ratau, M.C.4    Hanser, K.R.5    Silverstein, S.C.6
  • 20
    • 0030971098 scopus 로고    scopus 로고
    • Down-regulation of the filamentous actin cross-linking activity of cortactin by Src-mediated tyrosine phosphorylation
    • Huang, C., Y. Ni, T. Wang, Y. Gao, C. C. Haudenschild, and X. Zhan. Down-regulation of the filamentous actin cross-linking activity of cortactin by Src-mediated tyrosine phosphorylation. J. Biol. Chem. 21: 13911-13915, 1996.
    • (1996) J. Biol. Chem. , vol.21 , pp. 13911-13915
    • Huang, C.1    Ni, Y.2    Wang, T.3    Gao, Y.4    Haudenschild, C.C.5    Zhan, X.6
  • 21
    • 0028140140 scopus 로고
    • Induction of tyrosine phosphorylation and T-cell activation by vanadate peroxide, an inhibitor of protein tyrosine phosphatases
    • Imbert, V., J. F. Pegram, D. Farahi Far, B. Mari, P. Auberger, and B. Ross. Induction of tyrosine phosphorylation and T-cell activation by vanadate peroxide, an inhibitor of protein tyrosine phosphatases. Biochem. J. 297: 163-173, 1994.
    • (1994) Biochem. J. , vol.297 , pp. 163-173
    • Imbert, V.1    Pegram, J.F.2    Farahi Far, D.3    Mari, B.4    Auberger, P.5    Ross, B.6
  • 22
    • 0030575919 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and translocation of phospholipase C-gamma 2 in polymorphonuclear leukocytes treated with pervanadate
    • Kawakami, N., S. Shimohama, T. Hayakawa, Y. Sumida, and S. Fujimoto. Tyrosine phosphorylation and translocation of phospholipase C-gamma 2 in polymorphonuclear leukocytes treated with pervanadate. Biochim. Biophys. Acta 1314: 167-174, 1996.
    • (1996) Biochim. Biophys. Acta , vol.1314 , pp. 167-174
    • Kawakami, N.1    Shimohama, S.2    Hayakawa, T.3    Sumida, Y.4    Fujimoto, S.5
  • 23
    • 0025882268 scopus 로고
    • Cytoskeletal targets for oncogenic tyrosine kinases
    • Kellie, S., A. R. Horvath, and M. A. Elmore. Cytoskeletal targets for oncogenic tyrosine kinases. J. Cell Sci. 99: 207-211, 1991.
    • (1991) J. Cell Sci. , vol.99 , pp. 207-211
    • Kellie, S.1    Horvath, A.R.2    Elmore, M.A.3
  • 24
    • 0025765803 scopus 로고
    • SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins
    • Koch, C. A., D. Anderson, M. F. Moran, C. Ellis, and T. Pawson. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 252: 668-674, 1991.
    • (1991) Science , vol.252 , pp. 668-674
    • Koch, C.A.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 25
    • 0030798009 scopus 로고    scopus 로고
    • Pervanadate elicits proliferation and mediates activation of mitogen-activated protein (MAP) kinase in the nucleus
    • Krady, M. M., S. Freyermuth, P. Rogue, and A. N. Malviya. Pervanadate elicits proliferation and mediates activation of mitogen-activated protein (MAP) kinase in the nucleus. FEBS Lett. 412: 420-424, 1997.
    • (1997) FEBS Lett. , vol.412 , pp. 420-424
    • Krady, M.M.1    Freyermuth, S.2    Rogue, P.3    Malviya, A.N.4
  • 26
    • 0030977123 scopus 로고    scopus 로고
    • Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation
    • Kureishi, Y., S. Kobayashi, M. Amano, K. Kimura, H. Kanaide, T. Nakano, K. Kaibuchi, and M. Ito. Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation. J. Biol. Chem. 272: 12257-12260, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12257-12260
    • Kureishi, Y.1    Kobayashi, S.2    Amano, M.3    Kimura, K.4    Kanaide, H.5    Nakano, T.6    Kaibuchi, K.7    Ito, M.8
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of the bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during assembly of the head of the bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0028121374 scopus 로고
    • Regulation of vascular endothelial barrier function
    • Lung Cell. Mol. Physiol. 11
    • Lum, H., and A. B. Malik. Regulation of vascular endothelial barrier function. Am. J. Physiol. 267 (Lung Cell. Mol. Physiol. 11): L223-L241, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Lum, H.1    Malik, A.B.2
  • 29
    • 0030340292 scopus 로고    scopus 로고
    • Phosphorylation and activation of smooth muscle myosin light chain kinase by MAP kinase and cyclic-dependent kinase-1
    • Morrison, D. L., J. S. Sanghera, J. Stewart, C. Sutherland, M. P. Walsh, and S. L. Pelech. Phosphorylation and activation of smooth muscle myosin light chain kinase by MAP kinase and cyclic-dependent kinase-1. Biochem. Cell Biol. 74: 549-557, 1996.
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 549-557
    • Morrison, D.L.1    Sanghera, J.S.2    Stewart, J.3    Sutherland, C.4    Walsh, M.P.5    Pelech, S.L.6
  • 30
    • 0027961045 scopus 로고
    • Identification of major tyrosine-phosphorylated proteins in Csk-deficient cells
    • Nada, S., M. Okada, S. Aizawa, and H. Nakagawa. Identification of major tyrosine-phosphorylated proteins in Csk-deficient cells. Oncogene 9: 3571-3578, 1994.
    • (1994) Oncogene , vol.9 , pp. 3571-3578
    • Nada, S.1    Okada, M.2    Aizawa, S.3    Nakagawa, H.4
  • 32
    • 0028837170 scopus 로고
    • Activation of the small GTP-binding proteins rho and rac by growth factor receptors
    • Nobes, C. D., P. Hawkins, L. Stephens, and A. Hall. Activation of the small GTP-binding proteins rho and rac by growth factor receptors. J. Cell Sci. 108: 225-233, 1995.
    • (1995) J. Cell Sci. , vol.108 , pp. 225-233
    • Nobes, C.D.1    Hawkins, P.2    Stephens, L.3    Hall, A.4
  • 33
    • 0028970587 scopus 로고
    • p80/85 cortactin associates with the Src SH2 domain and colocalizes with v-Src in transformed cells
    • Okamura, H., and M. D. Resh. p80/85 cortactin associates with the Src SH2 domain and colocalizes with v-Src in transformed cells. J. Biol. Chem. 270: 26613-26618, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26613-26618
    • Okamura, H.1    Resh, M.D.2
  • 34
    • 0029897555 scopus 로고    scopus 로고
    • Pervanadate mediates an increased generation of inositol phosphates and tension in rat myometrium. Activation and phosphorylation of phospholipase C-gamma 1
    • Palmier, B., D. Leiber, and S. Harbon. Pervanadate mediates an increased generation of inositol phosphates and tension in rat myometrium. Activation and phosphorylation of phospholipase C-gamma 1. Biol. Reprod. 54: 1383-1389, 1996.
    • (1996) Biol. Reprod. , vol.54 , pp. 1383-1389
    • Palmier, B.1    Leiber, D.2    Harbon, S.3
  • 35
    • 0026941991 scopus 로고
    • Phosphatidylinositol 3-kinase: A novel effector
    • Parker, P. J., and M. D. Waterfield. Phosphatidylinositol 3-kinase: a novel effector. Cell Growth Differ. 3: 747-752, 1992.
    • (1992) Cell Growth Differ. , vol.3 , pp. 747-752
    • Parker, P.J.1    Waterfield, M.D.2
  • 36
    • 0027986575 scopus 로고
    • Mechanisms of cholera toxin prevention of thrombin-and PMA-induced endothelial cell barrier dysfunction
    • Patterson, C. E., H. W. Davis, K. L. Schaphorst, and J. G. N. Garcia. Mechanisms of cholera toxin prevention of thrombin-and PMA-induced endothelial cell barrier dysfunction. Microvasc. Res. 48: 212-235, 1994.
    • (1994) Microvasc. Res. , vol.48 , pp. 212-235
    • Patterson, C.E.1    Davis, H.W.2    Schaphorst, K.L.3    Garcia, J.G.N.4
  • 38
    • 0026806366 scopus 로고
    • Activation of signal transduction in platelets by tyrosine phosphatase inhibitors pervanadate (vanadyl hydroperoxide)
    • Pumiglia, K. M., L. F. Lau, C. K. Huang, S. Burroughs, and M. Feinstein. Activation of signal transduction in platelets by tyrosine phosphatase inhibitors pervanadate (vanadyl hydroperoxide). Biochemistry 286: 441-449, 1992.
    • (1992) Biochemistry , vol.286 , pp. 441-449
    • Pumiglia, K.M.1    Lau, L.F.2    Huang, C.K.3    Burroughs, S.4    Feinstein, M.5
  • 39
    • 0028218727 scopus 로고
    • Differential detergent fractionation of isolated hepatocytes: Biochemical, immunochemical and two-dimensional gel electrophoresis characterization of cytoskeletal and noncytoskeletal compartments
    • Ramsby, M. L., G. S. Makowski, and E. A. Khairallah. Differential detergent fractionation of isolated hepatocytes: biochemical, immunochemical and two-dimensional gel electrophoresis characterization of cytoskeletal and noncytoskeletal compartments. Electrophoresis 15: 265-277, 1994.
    • (1994) Electrophoresis , vol.15 , pp. 265-277
    • Ramsby, M.L.1    Makowski, G.S.2    Khairallah, E.A.3
  • 40
    • 0028321785 scopus 로고
    • Signal transduction pathways regulating Rho-mediated stress fibre formation: Requirements for a tyrosine kinase
    • Ridley, A., and A. Hall. Signal transduction pathways regulating Rho-mediated stress fibre formation: requirements for a tyrosine kinase. EMBO J. 13: 2600-2610, 1994.
    • (1994) EMBO J. , vol.13 , pp. 2600-2610
    • Ridley, A.1    Hall, A.2
  • 42
    • 0031012543 scopus 로고    scopus 로고
    • Peroxovanadate induces tyrosine phosphorylation of multiple signaling proteins in mouse liver and kidney
    • Ruff, S. J., K. Chen, and S. Cohen. Peroxovanadate induces tyrosine phosphorylation of multiple signaling proteins in mouse liver and kidney. J. Biol. Chem. 272: 1263-1267, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1263-1267
    • Ruff, S.J.1    Chen, K.2    Cohen, S.3
  • 43
    • 0030965296 scopus 로고    scopus 로고
    • Cell to substratum adhesion is involved in v-Src-induced cellular protein tyrosine phosphorylation: Implication for the adhesion-regulated protein tyrosine phosphatase activity
    • Sabe, H., M. Hamaguchi, and H. Hanafusa. Cell to substratum adhesion is involved in v-Src-induced cellular protein tyrosine phosphorylation: implication for the adhesion-regulated protein tyrosine phosphatase activity. Oncogene 14: 1779-1788, 1997.
    • (1997) Oncogene , vol.14 , pp. 1779-1788
    • Sabe, H.1    Hamaguchi, M.2    Hanafusa, H.3
  • 44
    • 0031255581 scopus 로고    scopus 로고
    • Thrombin-mediated barrier dysfunction in endothelium. Role of adhesion protein phosphorylation
    • Schaphorst, K. L., F. Pavalko, C. E. Patterson, and J. G. N. Garcia. Thrombin-mediated barrier dysfunction in endothelium. Role of adhesion protein phosphorylation. Am. J. Respir. Cell Mol. Biol. 17: 441-455, 1997.
    • (1997) Am. J. Respir. Cell Mol. Biol. , vol.17 , pp. 441-455
    • Schaphorst, K.L.1    Pavalko, F.2    Patterson, C.E.3    Garcia, J.G.N.4
  • 49
  • 50
    • 0029131091 scopus 로고
    • Regulation of endothelial cell gap formation and barrier function by myosin-associated phosphatase activities
    • Lung Cell. Mol. Physiol. 13
    • Verin, A. D., C. E. Patterson, M. A. Day, and J. G. N. Garcia. Regulation of endothelial cell gap formation and barrier function by myosin-associated phosphatase activities. Am. J. Physiol. 269 (Lung Cell. Mol. Physiol. 13): L99-L108, 1995.
    • (1995) Am. J. Physiol. , vol.269
    • Verin, A.D.1    Patterson, C.E.2    Day, M.A.3    Garcia, J.G.N.4
  • 51
    • 0029993903 scopus 로고    scopus 로고
    • Serotonin stimulates protein tyrosyl phosphorylation and vascular contraction via tyrosine kinase
    • Watts, S. W., C. H. Yeum, G. Campbell, and R. C. Webb. Serotonin stimulates protein tyrosyl phosphorylation and vascular contraction via tyrosine kinase. J. Vasc. Res. 33: 288-298, 1996.
    • (1996) J. Vasc. Res. , vol.33 , pp. 288-298
    • Watts, S.W.1    Yeum, C.H.2    Campbell, G.3    Webb, R.C.4
  • 52
    • 0027419589 scopus 로고
    • Cortactin, an 80-85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex
    • Wu, H., and J. T. Parsons. Cortactin, an 80-85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex. J. Cell Biol. 120: 1417-1426, 1993.
    • (1993) J. Cell Biol. , vol.120 , pp. 1417-1426
    • Wu, H.1    Parsons, J.T.2
  • 53
    • 0025940103 scopus 로고
    • Identification and characterization of a novel cytoskeleton-associated pp60src substrate
    • Wu, H., A. B. Reynolds, S. B. Kanner, R. R. Vines, and J. T. Parsons. Identification and characterization of a novel cytoskeleton-associated pp60src substrate. Mol. Cell. Biol. 11: 5113-5124, 1991.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5113-5124
    • Wu, H.1    Reynolds, A.B.2    Kanner, S.B.3    Vines, R.R.4    Parsons, J.T.5
  • 54
    • 0029831037 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein (MAP) kinase pathway by pervanadate, a potent inhibitor of tyrosine phosphatases
    • Zhao, Z., Z. Tan, C. D. Diltz, M. You, and E. H. Fischer. Activation of mitogen-activated protein (MAP) kinase pathway by pervanadate, a potent inhibitor of tyrosine phosphatases. J. Biol. Chem. 271: 22251-22255, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22251-22255
    • Zhao, Z.1    Tan, Z.2    Diltz, C.D.3    You, M.4    Fischer, E.H.5


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