메뉴 건너뛰기




Volumn 143, Issue 1, 1998, Pages 241-252

Modulation of calcium current in arteriolar smooth muscle by α(v)β3 and α5β1 integrin ligands

Author keywords

Extracellular matrix; Integrin mediated signaling; Vascular smooth muscle; Voltage gated Ca2+ channel; Wound repair

Indexed keywords

INTEGRIN;

EID: 0032487441     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.143.1.241     Document Type: Article
Times cited : (167)

References (57)
  • 1
    • 0023712779 scopus 로고
    • Calcium currents in single isolated smooth muscle cells from the rabbit ear artery in normal-calcium and high-barium solutions
    • Aaronson, P.I., T.B. Bolton, R.J. Lang, and I. MacKenzie. 1988. Calcium currents in single isolated smooth muscle cells from the rabbit ear artery in normal-calcium and high-barium solutions. J. Physiol. 405:57-75.
    • (1988) J. Physiol. , vol.405 , pp. 57-75
    • Aaronson, P.I.1    Bolton, T.B.2    Lang, R.J.3    MacKenzie, I.4
  • 2
    • 0030224080 scopus 로고    scopus 로고
    • Integrins in cell adhesion and signaling
    • Akiyama, S.K. 1996. Integrins in cell adhesion and signaling. Hum. Cell. 9:181-186.
    • (1996) Hum. Cell , vol.9 , pp. 181-186
    • Akiyama, S.K.1
  • 3
    • 0025091183 scopus 로고
    • Signal transduction initiated by extracellular nucleotides regulates the high affinity ligand recognition of the adhesive receptor CD 11b/CD18
    • Altieri, D.C., W.L. Wiltse, and T.S. Edgington. 1990. Signal transduction initiated by extracellular nucleotides regulates the high affinity ligand recognition of the adhesive receptor CD 11b/CD18. J. Immunol. 145:662-670.
    • (1990) J. Immunol. , vol.145 , pp. 662-670
    • Altieri, D.C.1    Wiltse, W.L.2    Edgington, T.S.3
  • 6
    • 0024325561 scopus 로고
    • Voltage-dependent transient calcium currents in freshly dissociated capillary endothelial cells
    • Bossu, J.L., A. Feltz, J.L. Rodeau, and F. Tanzi. 1989. Voltage-dependent transient calcium currents in freshly dissociated capillary endothelial cells. FEBS Lett. 255:377-380.
    • (1989) FEBS Lett. , vol.255 , pp. 377-380
    • Bossu, J.L.1    Feltz, A.2    Rodeau, J.L.3    Tanzi, F.4
  • 8
    • 1842296953 scopus 로고
    • Signal transduction from leukocyte integrins
    • M.E. Hemler and E. Mihich, editors. Plenum Press, New York
    • Brown, E.J. 1993. Signal transduction from leukocyte integrins. In Cell Adhesion Molecules. M.E. Hemler and E. Mihich, editors. Plenum Press, New York. 105-125.
    • (1993) Cell Adhesion Molecules , pp. 105-125
    • Brown, E.J.1
  • 9
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E.A., and J.S. Brugge. 1995. Integrins and signal transduction pathways: the road taken. Science. 268:233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 10
    • 0026758957 scopus 로고
    • Characteristics of calcium currents in rabbit portal vein myocytes
    • Cox, R.H., D. Katzka, and M. Morad. 1992. Characteristics of calcium currents in rabbit portal vein myocytes. Am. J. Physiol. 263:H453-H463.
    • (1992) Am. J. Physiol. , vol.263
    • Cox, R.H.1    Katzka, D.2    Morad, M.3
  • 12
    • 0026554217 scopus 로고
    • 3 binds to denatured collagen type I through RGD sites
    • 3 binds to denatured collagen type I through RGD sites. Biochem. Biophys. Res. Commun. 182:1025-1031.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1025-1031
    • Davis, G.E.1
  • 13
    • 0029201897 scopus 로고
    • Voltage-dependent calcium channels and their modulation by neurotransmitters and G proteins
    • Dolphin, A.C. 1995. Voltage-dependent calcium channels and their modulation by neurotransmitters and G proteins. Exp. Physiol. 80:1-36.
    • (1995) Exp. Physiol. , vol.80 , pp. 1-36
    • Dolphin, A.C.1
  • 14
    • 0028032853 scopus 로고
    • Voltage window for sustained elevation of cytosolic calcium in smooth muscle cells
    • Fleischmann, B.K., R.K. Murray, and M.I. Kotlikoff. 1994. Voltage window for sustained elevation of cytosolic calcium in smooth muscle cells. Proc. Natl. Acad. Sci. USA. 91:11914-11918.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11914-11918
    • Fleischmann, B.K.1    Murray, R.K.2    Kotlikoff, M.I.3
  • 15
    • 0025754427 scopus 로고
    • Depolarization-mediated intracellular calcium transients in isolated smooth muscle cells of guinea-pig urinary bladder
    • Ganitkevich, V. Y., and G. Isenberg. 1991. Depolarization-mediated intracellular calcium transients in isolated smooth muscle cells of guinea-pig urinary bladder. J. Physiol. 435:187-205.
    • (1991) J. Physiol. , vol.435 , pp. 187-205
    • Ganitkevich, V.Y.1    Isenberg, G.2
  • 16
    • 0028284043 scopus 로고
    • Whole-cell and single-channel calcium currents in guinea pig basal forebrain neurons
    • Griffith, W.H., L. Taylor, and M.J. Davis. 1994. Whole-cell and single-channel calcium currents in guinea pig basal forebrain neurons. J. Neurophysiol. 71: 2359-2376.
    • (1994) J. Neurophysiol. , vol.71 , pp. 2359-2376
    • Griffith, W.H.1    Taylor, L.2    Davis, M.J.3
  • 17
    • 0025218924 scopus 로고
    • VLA proteins in the integrin family: Structures, functions, and their role on leukocytes
    • Hemler, M.E. 1990. VLA proteins in the integrin family: structures, functions, and their role on leukocytes. Annu. Rev. Immunol. 8:365-400.
    • (1990) Annu. Rev. Immunol. , vol.8 , pp. 365-400
    • Hemler, M.E.1
  • 18
    • 0028088043 scopus 로고
    • Calcium entry and myogenic phenomena in skeletal muscle arterioles
    • Hill, M.A., and G.A. Meininger. 1994. Calcium entry and myogenic phenomena in skeletal muscle arterioles. Am. J. Physiol. 267:H1085-H1092.
    • (1994) Am. J. Physiol. , vol.267
    • Hill, M.A.1    Meininger, G.A.2
  • 19
    • 0030094383 scopus 로고    scopus 로고
    • Calcium dependence of indolactam-mediated contractions in resistance vessels
    • Hill, M.A., M.J. Davis, J.B. Song, and H. Zou. 1996. Calcium dependence of indolactam-mediated contractions in resistance vessels. J. Pharmacol. Exp. Ther. 276:867-874.
    • (1996) J. Pharmacol. Exp. Ther. , vol.276 , pp. 867-874
    • Hill, M.A.1    Davis, M.J.2    Song, J.B.3    Zou, H.4
  • 20
    • 0023619395 scopus 로고
    • Investigations of avidin and biotin for imaging applications
    • Hnatowich, D.J., F. Virzi, and M. Ruschowski. 1987. Investigations of avidin and biotin for imaging applications. J. Nucl. Med. 28:1294-1302.
    • (1987) J. Nucl. Med. , vol.28 , pp. 1294-1302
    • Hnatowich, D.J.1    Virzi, F.2    Ruschowski, M.3
  • 21
  • 22
    • 0029610703 scopus 로고
    • Calcium channels in vascular smooth muscle cells
    • Hughes, A.D. 1995. Calcium channels in vascular smooth muscle cells. J. Vasc. Res. 32:353-370.
    • (1995) J. Vasc. Res. , vol.32 , pp. 353-370
    • Hughes, A.D.1
  • 23
    • 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
  • 24
    • 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
  • 25
    • 0025130915 scopus 로고
    • cDNA cloning of a dihydropyridine-sensitive calcium channel from rat aorta. Evidence for the existence of alternatively spliced forms
    • Koch, W.J., P.T. Ellinor, and A. Schwartz. 1990. cDNA cloning of a dihydropyridine-sensitive calcium channel from rat aorta. Evidence for the existence of alternatively spliced forms. J. Biol. Chem. 265:17786-17791.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17786-17791
    • Koch, W.J.1    Ellinor, P.T.2    Schwartz, A.3
  • 26
    • 0026788082 scopus 로고
    • Effect of fibronectin on early embryo development in cows
    • Larson, R.C., G.G. Ignotz, and W.B. Currie. 1992. Effect of fibronectin on early embryo development in cows. J. Reprod. Fert. 96:289-297.
    • (1992) J. Reprod. Fert. , vol.96 , pp. 289-297
    • Larson, R.C.1    Ignotz, G.G.2    Currie, W.B.3
  • 28
    • 0027176804 scopus 로고
    • Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown
    • McNamee, H.P., D.E. Ingber, and M.A. Schwartz. 1993. Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown. J. Cell Biol. 121:673-678.
    • (1993) J. Cell Biol. , vol.121 , pp. 673-678
    • McNamee, H.P.1    Ingber, D.E.2    Schwartz, M.A.3
  • 29
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto, S., S.K. Akiyama, and K.M. Yamada. 1995a. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science. 267:883-885.
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 32
    • 0030808413 scopus 로고    scopus 로고
    • 1 integrin causes sustained endothelin-dependent vasoconstriction of rat skeletal muscle arterioles
    • 1 integrin causes sustained endothelin-dependent vasoconstriction of rat skeletal muscle arterioles. J. Clin. Invest. 100:1647-1653.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1647-1653
    • Mogford, J.E.1    Davis, G.E.2    Meininger, G.A.3
  • 33
    • 0023755714 scopus 로고
    • Noradrenaline contracts arteries by activating voltage-dependent calcium channels
    • Nelson, M.T., N.B. Standen, J.E. Brayden, and J.F. Worley III. 1988. Noradrenaline contracts arteries by activating voltage-dependent calcium channels. Nature. 336:382-385.
    • (1988) Nature , vol.336 , pp. 382-385
    • Nelson, M.T.1    Standen, N.B.2    Brayden, J.E.3    Worley III, J.F.4
  • 34
    • 0025298548 scopus 로고
    • Calcium channels, potassium channels, and voltage dependence of arterial smooth muscle tone
    • Nelson, M.T., J.B. Patlak, J.F. Worley, and N.B. Standen. 1990. Calcium channels, potassium channels, and voltage dependence of arterial smooth muscle tone. Am. J. Physiol. 259:C3-C18.
    • (1990) Am. J. Physiol. , vol.259
    • Nelson, M.T.1    Patlak, J.B.2    Worley, J.F.3    Standen, N.B.4
  • 35
    • 0023609864 scopus 로고
    • Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion
    • Pierschbacher, M.D., and E. Ruoslahti. 1987. Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J. Biol. Chem. 262:17294-17298.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17294-17298
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 36
    • 0028817908 scopus 로고
    • Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex
    • Plopper, G.E., H.P. McNamee, L.E. Dike, K. Bojanowski, and D.E. Ingber. 1995. Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex. Mol. Biol. Cell. 6:1349-1365.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1349-1365
    • Plopper, G.E.1    McNamee, H.P.2    Dike, L.E.3    Bojanowski, K.4    Ingber, D.E.5
  • 37
    • 0029072048 scopus 로고
    • Regulation of cytosolic calcium by collagen in single human platelets
    • Poole, A.W., and S.P. Watson. 1995. Regulation of cytosolic calcium by collagen in single human platelets. Br. J. Pharmacol. 115:101-106.
    • (1995) Br. J. Pharmacol. , vol.115 , pp. 101-106
    • Poole, A.W.1    Watson, S.P.2
  • 38
    • 0000563260 scopus 로고
    • Perforated patch recordings in physiology
    • Rae, J.L., and J. Fernandez. 1991. Perforated patch recordings in physiology. NIPS (News Physiol. Sci). 6:273-277.
    • (1991) NIPS (News Physiol. Sci) , vol.6 , pp. 273-277
    • Rae, J.L.1    Fernandez, J.2
  • 39
    • 0028990157 scopus 로고
    • 3-class integrins mediate fibronectin binding activity at the surface of developing mouse peri-implantation blastocysts
    • 3-class integrins mediate fibronectin binding activity at the surface of developing mouse peri-implantation blastocysts. J. Biol. Chem. 270:11522-11531.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11522-11531
    • Schultz, J.F.1    Armant, D.R.2
  • 40
    • 0027397549 scopus 로고
    • Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular-free calcium
    • Schwartz, M.A. 1993. Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular-free calcium. J. Cell Biol. 120: 1003-1010.
    • (1993) J. Cell Biol. , vol.120 , pp. 1003-1010
    • Schwartz, M.A.1
  • 41
    • 0028179351 scopus 로고
    • v integrins mediate the rise in intracellular calcium in endothelial cells on fibronectin even though they play a minor role in adhesion
    • v integrins mediate the rise in intracellular calcium in endothelial cells on fibronectin even though they play a minor role in adhesion. J. Biol. Chem. 269:11133-11137.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11133-11137
    • Schwartz, M.A.1    Denninghoff, K.2
  • 42
  • 44
    • 0027170760 scopus 로고
    • A 50 kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells
    • Schwartz, M.A., E.J. Brown, and B. Fazeli. 1993. A 50 kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells. J. Biol. Chem. 268:19931-19934.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19931-19934
    • Schwartz, M.A.1    Brown, E.J.2    Fazeli, B.3
  • 45
    • 0025744802 scopus 로고
    • Fibronectin: From gene to protein
    • Schwarzbauer, J.E. 1991. Fibronectin: from gene to protein. Curr. Opin. Cell Biol. 3:786-791.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 786-791
    • Schwarzbauer, J.E.1
  • 46
    • 0031025120 scopus 로고    scopus 로고
    • Integrin-mediated calcium signaling and regulation of cell adhesion by intracellular calcium
    • Sjaastad, M.D., and W.J. Nelson. 1997. Integrin-mediated calcium signaling and regulation of cell adhesion by intracellular calcium. Bio Essays. 19:47-55.
    • (1997) Bio Essays , vol.19 , pp. 47-55
    • Sjaastad, M.D.1    Nelson, W.J.2
  • 49
    • 0025352273 scopus 로고
    • Intradermal injections of bradykinin or histamine cause a flare-like vasodilation in monkey: Evidence from laser Doppler studies
    • Treede, R.D., R.A. Meyer, K.D. Davis, and J.N. Campbell. 1990. Intradermal injections of bradykinin or histamine cause a flare-like vasodilation in monkey: evidence from laser Doppler studies. Neurosci. Lett. 115:201-206.
    • (1990) Neurosci. Lett. , vol.115 , pp. 201-206
    • Treede, R.D.1    Meyer, R.A.2    Davis, K.D.3    Campbell, J.N.4
  • 50
    • 0027172919 scopus 로고
    • Mechanotransduction across the cell surface and through the cytoskeleton
    • Wang, N., J.P. Butler, and D.E. Ingber. 1993. Mechanotransduction across the cell surface and through the cytoskeleton. Science. 260:1124-1127.
    • (1993) Science , vol.260 , pp. 1124-1127
    • Wang, N.1    Butler, J.P.2    Ingber, D.E.3
  • 51
    • 0019382872 scopus 로고
    • Inhibition by free radical scavengers and by cyclooxygenase inhibitors of pial arteriolar abnormalities from concussive brain injury in cats
    • Wei, E.P., H.A. Kontos, W.D. Dietrich, J.T. Povlishock, and E.F. Ellis. 1981. Inhibition by free radical scavengers and by cyclooxygenase inhibitors of pial arteriolar abnormalities from concussive brain injury in cats. Circ. Res. 48: 95-103.
    • (1981) Circ. Res. , vol.48 , pp. 95-103
    • Wei, E.P.1    Kontos, H.A.2    Dietrich, W.D.3    Povlishock, J.T.4    Ellis, E.F.5
  • 52
    • 0030968165 scopus 로고    scopus 로고
    • Evaluation of arginine-glycine-aspartate-containing peptides as inhibitors of equine platelet function
    • Weiss, D.J., O.A. Evanson, and R.E. Wells. 1997. Evaluation of arginine-glycine-aspartate-containing peptides as inhibitors of equine platelet function. Am. J. Vet. Res. 58:457-460.
    • (1997) Am. J. Vet. Res. , vol.58 , pp. 457-460
    • Weiss, D.J.1    Evanson, O.A.2    Wells, R.E.3
  • 53
    • 0029417186 scopus 로고
    • c-src increases voltage-operated calcium channel currents in vascular smooth muscle cells
    • c-src increases voltage-operated calcium channel currents in vascular smooth muscle cells. Biochem. Biophys. Res. Commun. 217:1039-1044.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 1039-1044
    • Wijetunge, S.1    Hughes, A.D.2
  • 54
    • 0030577388 scopus 로고    scopus 로고
    • Activation of endogenous c-Src or a related tyrosine kinase by intracellular (PY)EEI peptide increases voltage-operated calcium channel currents in rabbit ear artery cells
    • Wijetunge, S., and A.D. Hughes. 1996. Activation of endogenous c-Src or a related tyrosine kinase by intracellular (PY)EEI peptide increases voltage-operated calcium channel currents in rabbit ear artery cells. FEBS Lett. 399: 63-66.
    • (1996) FEBS Lett. , vol.399 , pp. 63-66
    • Wijetunge, S.1    Hughes, A.D.2
  • 55
    • 0027054195 scopus 로고
    • Tyrosine kinase inhibitors block calcium channel currents in vascular smooth muscle cells
    • Wijetunge, S., C. Aalkjaer, M. Schachter, and A.D. Hughes. 1992. Tyrosine kinase inhibitors block calcium channel currents in vascular smooth muscle cells. Biochem. Biophys. Res. Commun. 189:1620-1623.
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 1620-1623
    • Wijetunge, S.1    Aalkjaer, C.2    Schachter, M.3    Hughes, A.D.4
  • 56
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complexes
    • Yamada, K.M., and B. Geiger. 1997. Molecular interactions in cell adhesion complexes. Curr. Opin. Cell Biol. 9:76-85.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 76-85
    • Yamada, K.M.1    Geiger, B.2
  • 57
    • 0030701893 scopus 로고    scopus 로고
    • An Arg-Gly-Asp peptide stimulates constriction in rat afferent arteriole
    • Yip, K.P., and D.J. Marsh. 1997. An Arg-Gly-Asp peptide stimulates constriction in rat afferent arteriole. Am. J. Physiol. 273:F768-F776.
    • (1997) Am. J. Physiol. , vol.273
    • Yip, K.P.1    Marsh, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.