메뉴 건너뛰기




Volumn 12, Issue 3, 1998, Pages 341-348

An essential role of myosin light-chain kinase in the regulation of agonist- and fluid flow-stimulated Ca2+ influx in endothelial cells

Author keywords

Bradykinin; Calcium; Fluid flow; Thapsigargin

Indexed keywords

CALCIUM ION; MYOSIN LIGHT CHAIN KINASE;

EID: 0031929741     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.12.3.341     Document Type: Article
Times cited : (81)

References (33)
  • 1
    • 0024390169 scopus 로고
    • Endothelium-derived relaxing and contracting factors
    • Furchgott, R. F., and Vanhoutte, P. M. (1989) Endothelium-derived relaxing and contracting factors. FASEB J. 3, 2007-2018
    • (1989) FASEB J. , vol.3 , pp. 2007-2018
    • Furchgott, R.F.1    Vanhoutte, P.M.2
  • 2
    • 0027326007 scopus 로고
    • Nitric oxide-mediated vasorelaxation
    • Ignarro, L. J. (1993) Nitric oxide-mediated vasorelaxation. Thromb. Haemost. 70, 148-151
    • (1993) Thromb. Haemost. , vol.70 , pp. 148-151
    • Ignarro, L.J.1
  • 3
    • 0026749918 scopus 로고
    • Modulation of venular microvessel permeability by calcium influx into endothelial cells
    • Curry, F. E. (1992) Modulation of venular microvessel permeability by calcium influx into endothelial cells. FASEB J. 6, 2456-2466
    • (1992) FASEB J. , vol.6 , pp. 2456-2466
    • Curry, F.E.1
  • 6
    • 0023760164 scopus 로고
    • Cytoplasmic calcium response to fluid shear stress in cultured vascular endothelial cells
    • Ando, J., Komatsuda, T., and Kamiya, A. (1988) Cytoplasmic calcium response to fluid shear stress in cultured vascular endothelial cells. In Vitro Cell Dev. Biol. 24, 871-877
    • (1988) In Vitro Cell Dev. Biol. , vol.24 , pp. 871-877
    • Ando, J.1    Komatsuda, T.2    Kamiya, A.3
  • 8
    • 0023000296 scopus 로고
    • Bradykinin stimulation of inositol polyphosphate production in porcine aortic endothelial cells
    • Lambert, T. L., Kent, R. S., and Whorton, A. R. (1986) Bradykinin stimulation of inositol polyphosphate production in porcine aortic endothelial cells. J. Biol. Chem. 261, 15288-15293
    • (1986) J. Biol. Chem. , vol.261 , pp. 15288-15293
    • Lambert, T.L.1    Kent, R.S.2    Whorton, A.R.3
  • 9
    • 0024423885 scopus 로고
    • Ion channels and regulation of intracellular calcium in vascular endothelial cells
    • Adams, D. J., Barakeh, J., Laskey, R., and van Breemen, C. (1989) Ion channels and regulation of intracellular calcium in vascular endothelial cells. FASEB J. 3, 2389-2400
    • (1989) FASEB J. , vol.3 , pp. 2389-2400
    • Adams, D.J.1    Barakeh, J.2    Laskey, R.3    Van Breemen, C.4
  • 10
    • 0027486748 scopus 로고
    • The inositol phosphate-calcium signaling system in nonexcitable cells
    • Putney, J. W., and Bird, G. J. (1993) The inositol phosphate-calcium signaling system in nonexcitable cells. Endocrin. Rev. 14, 610-631
    • (1993) Endocrin. Rev. , vol.14 , pp. 610-631
    • Putney, J.W.1    Bird, G.J.2
  • 12
    • 0025090570 scopus 로고
    • Shear stress increases inositol triphosphate levels in human endothelial cells
    • Nollert, M. U., Eskin, S. G., and McIntyre, L. V. (1990) Shear stress increases inositol triphosphate levels in human endothelial cells. Biochem. Biophys. Res. Commun. 170, 281-287
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 281-287
    • Nollert, M.U.1    Eskin, S.G.2    McIntyre, L.V.3
  • 13
    • 0027462466 scopus 로고
    • Flow-related responses of intracellular inositol phosphate levels in cultured aortic endothelial cells
    • Prasad, A. R. S., Logan, S., A., Nerem, R. M., Schwartz, C. J., and Sprague, E. A. (1993) Flow-related responses of intracellular inositol phosphate levels in cultured aortic endothelial cells. Circ. Res. 72, 827-836
    • (1993) Circ. Res. , vol.72 , pp. 827-836
    • Prasad, A.R.S.1    Logan, S.A.2    Nerem, R.M.3    Schwartz, C.J.4    Sprague, E.A.5
  • 15
    • 0025760391 scopus 로고
    • Macromolecule permeability of coronary and aortic endothelial monolayers under energy depletion
    • Watanabe, H., Kuhne, W., Spahr, R., Schwartz, P., and Piper, H. M. (1991) Macromolecule permeability of coronary and aortic endothelial monolayers under energy depletion. Am. J. Physiol. 260, H1344-1352
    • (1991) Am. J. Physiol. , vol.260
    • Watanabe, H.1    Kuhne, W.2    Spahr, R.3    Schwartz, P.4    Piper, H.M.5
  • 16
    • 0023616788 scopus 로고
    • Quantisation of intracellular free calcium in single adult cardiomyocytes by fura-2 fluorescence microscopy: Calibration of fura-2 ratios
    • Li, Q., Altschuld, R. A., and Stokes, B. T. (1987) Quantisation of intracellular free calcium in single adult cardiomyocytes by fura-2 fluorescence microscopy: calibration of fura-2 ratios. Biochem. Biophys. Res. Commun. 147, 120-126
    • (1987) Biochem. Biophys. Res. Commun. , vol.147 , pp. 120-126
    • Li, Q.1    Altschuld, R.A.2    Stokes, B.T.3
  • 18
    • 0029887450 scopus 로고    scopus 로고
    • Myosin light chain diphosphorylation is enhanced by growth promotion of cultured smooth muscle cells
    • Seto, M., Sakurada, K., Kamm, K. E., Stull, J. T., and Sasaki, Y. (1996) Myosin light chain diphosphorylation is enhanced by growth promotion of cultured smooth muscle cells. Pfluegers Arch. 432, 7-13
    • (1996) Pfluegers Arch. , vol.432 , pp. 7-13
    • Seto, M.1    Sakurada, K.2    Kamm, K.E.3    Stull, J.T.4    Sasaki, Y.5
  • 19
    • 0023019582 scopus 로고
    • Different phosphorylated forms of myosin in contracting tracheal smooth muscle
    • Persechini, A., Kamm, K. E., and Stull, J. T. (1986) Different phosphorylated forms of myosin in contracting tracheal smooth muscle. J. Biol. Chem. 261, 6293-6299
    • (1986) J. Biol. Chem. , vol.261 , pp. 6293-6299
    • Persechini, A.1    Kamm, K.E.2    Stull, J.T.3
  • 20
    • 0019888289 scopus 로고
    • Purification and characterization of smooth muscle myosin light chain kinase
    • Adelstein, R. S., and Klee, C. B. (1981) Purification and characterization of smooth muscle myosin light chain kinase. J. Biol. Chem. 256, 7501-7509
    • (1981) J. Biol. Chem. , vol.256 , pp. 7501-7509
    • Adelstein, R.S.1    Klee, C.B.2
  • 21
    • 0023644877 scopus 로고
    • Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase
    • Saitoh, M., Ishikawa, T., Matsushima, S., Naka, M., and Hidaka, H. (1987) Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase. J. Biol. Chem. 262, 7796-7801
    • (1987) J. Biol. Chem. , vol.262 , pp. 7796-7801
    • Saitoh, M.1    Ishikawa, T.2    Matsushima, S.3    Naka, M.4    Hidaka, H.5
  • 22
    • 0026061774 scopus 로고
    • Effects of HA1077, a protein kinase inhibitor, on myosin phosphorylation and tension in smooth muscle
    • Seto, M., Sasaki, Y., Hidaka, H., and Sasaki, Y. (1991) Effects of HA1077, a protein kinase inhibitor, on myosin phosphorylation and tension in smooth muscle. Eur. J. Pharmacol. 195, 267-272
    • (1991) Eur. J. Pharmacol. , vol.195 , pp. 267-272
    • Seto, M.1    Sasaki, Y.2    Hidaka, H.3    Sasaki, Y.4
  • 24
    • 0022971509 scopus 로고
    • Cytochemical identification of the regulatory subunit of cAMP-dependent protein kinase by use of fluorescently labeled catalytic subunit. Examination of protein kinase dissociation in hepatoma cells responding to 8-Br-cAMP stimulation
    • Fletcher, W. H., Van Patten, S. M., Cheng, H. C., and Walsh, D. A. (1986) Cytochemical identification of the regulatory subunit of cAMP-dependent protein kinase by use of fluorescently labeled catalytic subunit. Examination of protein kinase dissociation in hepatoma cells responding to 8-Br-cAMP stimulation. J. Biol. Chem. 261, 5504-5513
    • (1986) J. Biol. Chem. , vol.261 , pp. 5504-5513
    • Fletcher, W.H.1    Van Patten, S.M.2    Cheng, H.C.3    Walsh, D.A.4
  • 27
    • 0021894617 scopus 로고
    • The function of myosin and myosin light chain kinase phosphorylation smooth muscle
    • Kamm, K. E., and Stull, J. T. (1985) The function of myosin and myosin light chain kinase phosphorylation smooth muscle. Annu. Rev. Pharmacol. Toxicol. 25, 593-620
    • (1985) Annu. Rev. Pharmacol. Toxicol. , vol.25 , pp. 593-620
    • Kamm, K.E.1    Stull, J.T.2
  • 28
    • 0025743578 scopus 로고
    • Regulation of permeabilized endothelial cell retraction by myosin phosphorylation
    • Wysolmerski, R. B., and Langunoff, D. (1991) Regulation of permeabilized endothelial cell retraction by myosin phosphorylation. Am. J. Physiol. 261, C32-C40
    • (1991) Am. J. Physiol. , vol.261
    • Wysolmerski, R.B.1    Langunoff, D.2
  • 30
    • 0027338205 scopus 로고
    • + current by means of a phosphatase and a diffusible messenger
    • + current by means of a phosphatase and a diffusible messenger. Nature (London) 364, 814-818
    • (1993) Nature (London) , vol.364 , pp. 814-818
    • Parekh, A.B.1    Terlau, H.2    Stühmer, W.3
  • 31
    • 0028965735 scopus 로고
    • Calcium signaling in endothelial cells involves activation of tyrosine kinases and leads to activation of mitogen-activated protein kinases
    • Fleming, I., Fisslthaler, B., and Busse, R (1995) Calcium signaling in endothelial cells involves activation of tyrosine kinases and leads to activation of mitogen-activated protein kinases. Circ. Res. 76, 522-529
    • (1995) Circ. Res. , vol.76 , pp. 522-529
    • Fleming, I.1    Fisslthaler, B.2    Busse, R.3
  • 32
    • 0031587976 scopus 로고    scopus 로고
    • Roles of inhibitors of myosin light chain kinase and tyrosine kinase on cation influx in agonist-stimulated endothelial cells
    • Takahashi, R., Watanabe, H., Zhang, X. X., Kakizawa, H., Hayashi, H., and Ohno, R. (1997) Roles of inhibitors of myosin light chain kinase and tyrosine kinase on cation influx in agonist-stimulated endothelial cells. Biochem. Biophys. Res. Commun. 235, 657-662
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 657-662
    • Takahashi, R.1    Watanabe, H.2    Zhang, X.X.3    Kakizawa, H.4    Hayashi, H.5    Ohno, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.