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Volumn 272, Issue 2 16-2, 1997, Pages

Thrombin inhibits myosin light chain dephosphorylation in endothelial cells

Author keywords

myosin light chain kinase; phosphatase

Indexed keywords

MYOSIN LIGHT CHAIN; THROMBIN;

EID: 0030961509     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1997.272.2.l311     Document Type: Article
Times cited : (41)

References (32)
  • 2
    • 0028097766 scopus 로고
    • Three genes for protein phosphatase 1 map to different human chromosomes: Sequence, expression and gene localization to protein serine/threonine phosphatase 1 beta (PPP1CB)
    • Barker, H., N. Brewis, A. Street, N. Spurr, and P. Cohen. Three genes for protein phosphatase 1 map to different human chromosomes: sequence, expression and gene localization to protein serine/threonine phosphatase 1 beta (PPP1CB). Biochim. Biophys. Acta 1220: 212-218, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1220 , pp. 212-218
    • Barker, H.1    Brewis, N.2    Street, A.3    Spurr, N.4    Cohen, P.5
  • 3
    • 0024425865 scopus 로고
    • Histamine and inositol phosphate accumulation in endothelium: CAMP and G-protein
    • Lung Cell. Mol. Physiol. 1
    • Carson, M., S. Shasby, and D. M. Shasby. Histamine and inositol phosphate accumulation in endothelium: cAMP and G-protein. Am. J. Physiol. 257 (Lung Cell. Mol. Physiol. 1): L259-L264, 1989.
    • (1989) Am. J. Physiol. , vol.257
    • Carson, M.1    Shasby, S.2    Shasby, D.M.3
  • 4
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen, P. The structure and regulation of protein phosphatases. Annu. Rev. Biochem. 58: 453-508, 1989.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 453-508
    • Cohen, P.1
  • 5
    • 0025181418 scopus 로고
    • Okadaic acid, a new probe for the study of cellular regulation
    • Cohen, P., C. Holmes, and Y. Tsukitani. Okadaic acid, a new probe for the study of cellular regulation. Trends Biochem. Sci. 15: 98-102, 1990.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 98-102
    • Cohen, P.1    Holmes, C.2    Tsukitani, Y.3
  • 7
    • 0027336045 scopus 로고
    • Okadaic acid-induced actin assembly in neutrophils: Role of protein phosphatases
    • Downy, G. P., A. Takai, R. Zamel, S. Grinstein, and C. K. Chan. Okadaic acid-induced actin assembly in neutrophils: role of protein phosphatases. J. Cell. Physiol. 155: 505-519, 1993.
    • (1993) J. Cell. Physiol. , vol.155 , pp. 505-519
    • Downy, G.P.1    Takai, A.2    Zamel, R.3    Grinstein, S.4    Chan, C.K.5
  • 8
    • 0025363197 scopus 로고
    • Protein phosphatase type-1, not type-2A, modulates actin microfilament integrity and myosin light chain phosphorylation in living nonmuscle cells
    • Fernandez, A., D. L. Brautigan, M. Mumby, and N. J. C. Lamb. Protein phosphatase type-1, not type-2A, modulates actin microfilament integrity and myosin light chain phosphorylation in living nonmuscle cells. J. Cell Biol. 111: 103-112, 1990.
    • (1990) J. Cell Biol. , vol.111 , pp. 103-112
    • Fernandez, A.1    Brautigan, D.L.2    Mumby, M.3    Lamb, N.J.C.4
  • 9
    • 0029119895 scopus 로고
    • Myosin light chain kinase-regulated endothelial cell contraction: The relationship between isometric tension, actin polymerization and myosin phosphorylation
    • Goeckeler, Z. M., and R. B. Wysolmerski. Myosin light chain kinase-regulated endothelial cell contraction: the relationship between isometric tension, actin polymerization and myosin phosphorylation. J. Cell Biol. 130: 613-627, 1995.
    • (1995) J. Cell Biol. , vol.130 , pp. 613-627
    • Goeckeler, Z.M.1    Wysolmerski, R.B.2
  • 10
    • 0024552836 scopus 로고
    • In situ phosphorylation of human platelet myosin heavy and light chains by protein kinase C
    • Kawamoto, S., A. Bengur, J. Sellers, and R. Adelstein. In situ phosphorylation of human platelet myosin heavy and light chains by protein kinase C. J. Biol. Chem. 264: 2258-2265, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2258-2265
    • Kawamoto, S.1    Bengur, A.2    Sellers, J.3    Adelstein, R.4
  • 12
    • 0026048788 scopus 로고
    • G protein-mediated inhibition of myosin light-chain phosphatase in vascular smooth muscle
    • Kitazawa, T., M. Masatoshi, and A. P. Somlyo. G protein-mediated inhibition of myosin light-chain phosphatase in vascular smooth muscle. Proc. Natl. Acad Sci. USA 88: 9307-9310, 1991.
    • (1991) Proc. Natl. Acad Sci. USA , vol.88 , pp. 9307-9310
    • Kitazawa, T.1    Masatoshi, M.2    Somlyo, A.P.3
  • 13
    • 0026493689 scopus 로고
    • Protein phosphatase inhibitors okadaic acid and calyculin A alter cell shape and f-actin distribution and inhibit stimulus dependent increases in cytoskeletal actin of human neutrophils
    • Kreiebuhl, P., H. Keller, and V. Niggli. Protein phosphatase inhibitors okadaic acid and calyculin A alter cell shape and f-actin distribution and inhibit stimulus dependent increases in cytoskeletal actin of human neutrophils. Blood 80: 2911-2919, 1992.
    • (1992) Blood , vol.80 , pp. 2911-2919
    • Kreiebuhl, P.1    Keller, H.2    Niggli, V.3
  • 14
    • 0026509167 scopus 로고
    • GTPγS-dependent regulation of smooth muscle contractile elements
    • Cell Physiol. 31
    • Kubota, Y., M. Nomura, K. E. Kamm, M. C. Mumby, and J. T. Stull. GTPγS-dependent regulation of smooth muscle contractile elements. Am. J. Physiol. 262 (Cell Physiol. 31): C405-C410, 1992.
    • (1992) Am. J. Physiol. , vol.262
    • Kubota, Y.1    Nomura, M.2    Kamm, K.E.3    Mumby, M.C.4    Stull, J.T.5
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature Lond. 227: 680-685, 1970.
    • (1970) Nature Lond. , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0020557296 scopus 로고
    • Thrombin-induced gap formation in confluent endothelial cell monolayers in vitro
    • Laposata, M., D. Dovnarsky, and H. Shin. Thrombin-induced gap formation in confluent endothelial cell monolayers in vitro. Blood 62: 549-556, 1983.
    • (1983) Blood , vol.62 , pp. 549-556
    • Laposata, M.1    Dovnarsky, D.2    Shin, H.3
  • 18
    • 73049179795 scopus 로고
    • Studies on inflammation. I. Effect of histamine and serotonin on vascular permeability: An electron microscopic study
    • Majno, G., and G. Palade. Studies on inflammation. I. Effect of histamine and serotonin on vascular permeability: an electron microscopic study. J. Biophys. Biochem. Cytol. 11: 571-605, 1961.
    • (1961) J. Biophys. Biochem. Cytol. , vol.11 , pp. 571-605
    • Majno, G.1    Palade, G.2
  • 19
    • 0027178669 scopus 로고
    • The effect of histamine and cAMP on myosin light chain phosphorylation in human umbilical vein endothelial cells
    • Moy, A. B., S. S. Shasby, B. D. Scott, and D. M. Shasby. The effect of histamine and cAMP on myosin light chain phosphorylation in human umbilical vein endothelial cells. J. Clin. Invest. 92: 1198-1206, 1993.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1198-1206
    • Moy, A.B.1    Shasby, S.S.2    Scott, B.D.3    Shasby, D.M.4
  • 21
    • 0024410089 scopus 로고
    • The fission yeast dis2+ gene required for chromosome disjoining encodes one of two putative type 1 protein phosphatases
    • Ohkura, H., N. Kinoshita, S. Miyatani, T. Toda, and M. Yanagida. The fission yeast dis2+ gene required for chromosome disjoining encodes one of two putative type 1 protein phosphatases. Cell 57: 997-1007, 1989.
    • (1989) Cell , vol.57 , pp. 997-1007
    • Ohkura, H.1    Kinoshita, N.2    Miyatani, S.3    Toda, T.4    Yanagida, M.5
  • 22
    • 0026553098 scopus 로고
    • Evans blue-albumin binding as a new marker of transendothelial macromolecule permeability
    • Patterson, C. E., R. A. Rhodes, and J. G. N. Garcia. Evans blue-albumin binding as a new marker of transendothelial macromolecule permeability. J. Appl. Physiol. 72: 865-873, 1992.
    • (1992) J. Appl. Physiol. , vol.72 , pp. 865-873
    • Patterson, C.E.1    Rhodes, R.A.2    Garcia, J.G.N.3
  • 23
    • 0023002888 scopus 로고
    • Histamine type 1 receptor occupancy increases endothelial cell calcium, reduces f-actin, and promotes albumin diffusion across cultured endothelial monolayers
    • Rotrosen, D., and J. I. Gallin. Histamine type 1 receptor occupancy increases endothelial cell calcium, reduces f-actin, and promotes albumin diffusion across cultured endothelial monolayers. J. Cell. Biol. 103: 2379-2387, 1986.
    • (1986) J. Cell. Biol. , vol.103 , pp. 2379-2387
    • Rotrosen, D.1    Gallin, J.I.2
  • 24
    • 0025642947 scopus 로고
    • Role of actin and myosin in the control of paracellular permeability in pig, rat and human vascular endothelium
    • Schnittler, H., A. Wilke, T. Gress, N. Suttorp, and D. Drenckhahn. Role of actin and myosin in the control of paracellular permeability in pig, rat and human vascular endothelium. J. Physiol. Lond. 431: 379-401, 1990.
    • (1990) J. Physiol. Lond. , vol.431 , pp. 379-401
    • Schnittler, H.1    Wilke, A.2    Gress, T.3    Suttorp, N.4    Drenckhahn, D.5
  • 25
    • 0021987654 scopus 로고
    • Reversible oxidant-induced increases in albumin transfer across cultured endothelium: Alterations in cell shape and calcium homeostasis
    • Shasby, D. M., S. Lind, S. Shasby, J. Goldsmith, and G. Hunninghake. Reversible oxidant-induced increases in albumin transfer across cultured endothelium: alterations in cell shape and calcium homeostasis. Blood 65: 605-614, 1985.
    • (1985) Blood , vol.65 , pp. 605-614
    • Shasby, D.M.1    Lind, S.2    Shasby, S.3    Goldsmith, J.4    Hunninghake, G.5
  • 26
    • 0027756098 scopus 로고
    • Role of myosin light chain phosphorylation in endothelial cell retraction
    • Lung Cell. Mol. Physiol. 9
    • Sheldon, R., A. Moy, K. Lindsley, S. Shasby, and D. M. Shasby. Role of myosin light chain phosphorylation in endothelial cell retraction. Am. J. Physiol. 265 (Lung Cell. Mol. Physiol. 9): L606-L612, 1993.
    • (1993) Am. J. Physiol. , vol.265
    • Sheldon, R.1    Moy, A.2    Lindsley, K.3    Shasby, S.4    Shasby, D.M.5
  • 27
    • 0025142419 scopus 로고
    • Okadaic acid uncouples myosin light chain phosphorylation and tension in smooth muscle
    • Tansey, M. G., M. Hori, K. Karaki, K. E. Kamm, and J. T. Stull. Okadaic acid uncouples myosin light chain phosphorylation and tension in smooth muscle. FEBS Lett. 270: 219-221, 1990.
    • (1990) FEBS Lett. , vol.270 , pp. 219-221
    • Tansey, M.G.1    Hori, M.2    Karaki, K.3    Kamm, K.E.4    Stull, J.T.5
  • 28
    • 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
  • 29
    • 0025602324 scopus 로고
    • Multiplicity of protein serine-threonine phosphatases in PC12 pheochromocytoma and FTO-2B hepatoma cells
    • Waszinski, B. E., L. E. Heasley, and G. L. Johnson. Multiplicity of protein serine-threonine phosphatases in PC12 pheochromocytoma and FTO-2B hepatoma cells. J. Biol. Chem 265: 21504-21508, 1990.
    • (1990) J. Biol. Chem , vol.265 , pp. 21504-21508
    • Waszinski, B.E.1    Heasley, L.E.2    Johnson, G.L.3
  • 30
    • 0025975376 scopus 로고
    • Okadaic acid, a phosphatase inhibitor, decreases macrophage motility
    • Lung Cell. Mol. Physiol. 4
    • Wilson, A. K., A. Takai, J. C. Ruegg, and P. de Lanerolle. Okadaic acid, a phosphatase inhibitor, decreases macrophage motility. Am. J. Physiol. 260 (Lung Cell. Mol. Physiol. 4): L105-L112, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Wilson, A.K.1    Takai, A.2    Ruegg, J.C.3    De Lanerolle, P.4
  • 31
    • 0026664091 scopus 로고
    • Transient venular permeability increase and endothelial gap formation induced by histamine
    • Heart Circ. Physiol. 31
    • Wu, N. Z., and A. L. Baldwin. Transient venular permeability increase and endothelial gap formation induced by histamine. Am. J. Physiol. 262 (Heart Circ. Physiol. 31): H1238-H1247 1992.
    • (1992) Am. J. Physiol. , vol.262
    • Wu, N.Z.1    Baldwin, A.L.2
  • 32
    • 0025743578 scopus 로고
    • Regulation of permeabilized endothelial cell retraction by myosin phosphorylation
    • Cell Physiol. 30
    • Wysolmerski, R., and D. Lagunoff. Regulation of permeabilized endothelial cell retraction by myosin phosphorylation. Am. J. Physiol. 261 (Cell Physiol. 30): C32-C40, 1991.
    • (1991) Am. J. Physiol. , vol.261
    • Wysolmerski, R.1    Lagunoff, D.2


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