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Volumn 63, Issue 4, 2004, Pages 673-681

Investigation of signaling pathways that mediate the inotropic effect of urotensin-II in human heart

Author keywords

Contractile function; Protein kinase C; Signal transduction; Urotensin II

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; 4ALPHA PHORBOL; CHELERYTHRINE; MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN KINASE INHIBITOR; PHORBOL 12 ACETATE 13 MYRISTATE; PROTEIN KINASE C; PROTEIN KINASE C INHIBITOR; PROTEIN KINASE INHIBITOR; RHO KINASE; UROTENSIN II; WORTMANNIN;

EID: 4043056592     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cardiores.2004.05.009     Document Type: Article
Times cited : (40)

References (29)
  • 1
    • 0035827716 scopus 로고    scopus 로고
    • Human urotensin II-induced contraction and arterial smooth muscle cell proliferation are mediated by RhoA and Rho-kinase
    • Sauzeau V., Mellionnec E.L., Bertoglio J., Scalbert E., Pacaud P., Loirand G. Human urotensin II-induced contraction and arterial smooth muscle cell proliferation are mediated by RhoA and Rho-kinase. Circ. Res. 88:2001;1102-1104
    • (2001) Circ. Res. , vol.88 , pp. 1102-1104
    • Sauzeau, V.1    Mellionnec, E.L.2    Bertoglio, J.3    Scalbert, E.4    Pacaud, P.5    Loirand, G.6
  • 2
    • 0035146524 scopus 로고    scopus 로고
    • Cardiostimulant effects of urotensin-II in human heart in vitro
    • Russell F.D., Molenaar P., O'Brien D. Cardiostimulant effects of urotensin-II in human heart in vitro. Br. J. Pharmacol. 132:2001;5-9
    • (2001) Br. J. Pharmacol. , vol.132 , pp. 5-9
    • Russell, F.D.1    Molenaar, P.2    O'Brien, D.3
  • 5
    • 0027248968 scopus 로고
    • Role of protein kinase C in the phosphorylation of cardiac myosin light chain 2
    • Venema R.C., Raynor R.L., Noland T.A., Kuo J.F. Role of protein kinase C in the phosphorylation of cardiac myosin light chain 2. Biochem. J. 294:1993;401-406
    • (1993) Biochem. J. , vol.294 , pp. 401-406
    • Venema, R.C.1    Raynor, R.L.2    Noland, T.A.3    Kuo, J.F.4
  • 6
    • 0029757994 scopus 로고    scopus 로고
    • Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments
    • Levine R.J., Kensler R.W., Yang Z., Stull J.T., Sweeney H.L. Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments. Biophys. J. 71:1996;898-907
    • (1996) Biophys. J. , vol.71 , pp. 898-907
    • Levine, R.J.1    Kensler, R.W.2    Yang, Z.3    Stull, J.T.4    Sweeney, H.L.5
  • 7
    • 0024312136 scopus 로고
    • Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. Implications for twitch potentiation in intact muscle
    • Metzger J.M., Greaser M.L., Moss R.L. Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. Implications for twitch potentiation in intact muscle. J. Gen. Physiol. 93:1989;855-883
    • (1989) J. Gen. Physiol. , vol.93 , pp. 855-883
    • Metzger, J.M.1    Greaser, M.L.2    Moss, R.L.3
  • 8
    • 0029049190 scopus 로고
    • Arachidonic acid-dependent phosphorylation of troponin I and myosin light chain 2 in cardiac myocytes
    • Damron D.S., Darvish A., Murphy L.A., Sweet W., Moravec C.S., Bond M. Arachidonic acid-dependent phosphorylation of troponin I and myosin light chain 2 in cardiac myocytes. Circ. Res. 76:1995;1011-1019
    • (1995) Circ. Res. , vol.76 , pp. 1011-1019
    • Damron, D.S.1    Darvish, A.2    Murphy, L.A.3    Sweet, W.4    Moravec, C.S.5    Bond, M.6
  • 9
    • 0030734153 scopus 로고    scopus 로고
    • Mechanism of action of endothelin in rat cardiac muscle: Cross-bridge kinetics and myosin light chain phosphorylation
    • Rossmanith G.H., Hoh J.F.Y., Turnbull L., Ludowyke R.I. Mechanism of action of endothelin in rat cardiac muscle: cross-bridge kinetics and myosin light chain phosphorylation. J. Physiol. 505(1):1997;217-227
    • (1997) J. Physiol. , vol.505 , Issue.1 , pp. 217-227
    • Rossmanith, G.H.1    Hoh, J.F.Y.2    Turnbull, L.3    Ludowyke, R.I.4
  • 11
    • 4043069105 scopus 로고    scopus 로고
    • 1-adrenergic positive inotropic effect dependes on myosin light chain-2 phosphorylation in human atrium, but not in ventricle
    • (Abstract)
    • 1- adrenergic positive inotropic effect dependes on myosin light chain-2 phosphorylation in human atrium, but not in ventricle. Naunyn Schmiedebergs Arch. Pharmacol. 367:2003;R28. (Abstract)
    • (2003) Naunyn Schmiedebergs Arch. Pharmacol. , vol.367 , pp. 28
    • Haas, P.1    Grimm, M.2    Weyand, M.3    Eschenhagen, T.4
  • 12
    • 0033615977 scopus 로고    scopus 로고
    • Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo
    • Kawano Y., Fukata Y., Oshiro N., et al. Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo. J. Cell Biol. 147:1999;1023-1037
    • (1999) J. Cell Biol. , vol.147 , pp. 1023-1037
    • Kawano, Y.1    Fukata, Y.2    Oshiro, N.3
  • 13
    • 0036708589 scopus 로고    scopus 로고
    • Occupation of the prostaglandin E2-type 1 receptor increases rat atrial contractility via a Y-27632-sensitive pathway
    • Wolkowicz P.E., Ku D.D., Grenett H.E., Urthaler F. Occupation of the prostaglandin E2-type 1 receptor increases rat atrial contractility via a Y-27632-sensitive pathway. Prostaglandins Other Lipid Mediat. 70:2002;91-105
    • (2002) Prostaglandins Other Lipid Mediat. , vol.70 , pp. 91-105
    • Wolkowicz, P.E.1    Ku, D.D.2    Grenett, H.E.3    Urthaler, F.4
  • 15
    • 0030068247 scopus 로고    scopus 로고
    • Influence of endothelin 1 on human atrial myocardium - Myocardial function and subcellular pathways
    • Meyer M., Lehnart S., Pieske B., et al. Influence of endothelin 1 on human atrial myocardium - myocardial function and subcellular pathways. Basic Res. Cardiol. 91:1996;86-93
    • (1996) Basic Res. Cardiol. , vol.91 , pp. 86-93
    • Meyer, M.1    Lehnart, S.2    Pieske, B.3
  • 17
    • 0033553417 scopus 로고    scopus 로고
    • Activated protein kinase C isoforms target to cardiomyocyte caveolae. Stimulation of local protein phosphorylation
    • Rybin V.O., Xu X., Steinberg S.F. Activated protein kinase C isoforms target to cardiomyocyte caveolae. Stimulation of local protein phosphorylation. Circ. Res. 84:1999;980-988
    • (1999) Circ. Res. , vol.84 , pp. 980-988
    • Rybin, V.O.1    Xu, X.2    Steinberg, S.F.3
  • 20
    • 0020647583 scopus 로고
    • The effects of changes of pH on intracellular calcium transients in mammalian cardiac muscle
    • Allen D.G., Orchard C.H. The effects of changes of pH on intracellular calcium transients in mammalian cardiac muscle. J. Physiol. 335:1983;555-567
    • (1983) J. Physiol. , vol.335 , pp. 555-567
    • Allen, D.G.1    Orchard, C.H.2
  • 21
    • 0029813865 scopus 로고    scopus 로고
    • Phosphorylation specificities of protein kinase C isozymes for bovine cardiac troponin I and troponin T and sites within these proteins and regulation of myofilament properties
    • Jideama N.M., Noland T.A., Raynor R.L., et al. Phosphorylation specificities of protein kinase C isozymes for bovine cardiac troponin I and troponin T and sites within these proteins and regulation of myofilament properties. J. Biol. Chem. 271:1996;23277-23283
    • (1996) J. Biol. Chem. , vol.271 , pp. 23277-23283
    • Jideama, N.M.1    Noland, T.A.2    Raynor, R.L.3
  • 22
    • 0036852106 scopus 로고    scopus 로고
    • Slick signalling
    • Shaw A.S.Y. Slick signalling. Nat. Immunol. 3:2002;1058-1059
    • (2002) Nat. Immunol. , vol.3 , pp. 1058-1059
    • Shaw, A.S.Y.1
  • 23
    • 0035413601 scopus 로고    scopus 로고
    • Protein kinase C: Structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions
    • Newton A.C. Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions. Chem. Rev. 101:2001;2353-2364
    • (2001) Chem. Rev. , vol.101 , pp. 2353-2364
    • Newton, A.C.1
  • 24
    • 0035213641 scopus 로고    scopus 로고
    • AGC protein kinase phosphorylation and protein kinase C
    • Parker P.J., Parkinson S.J. AGC protein kinase phosphorylation and protein kinase C. Biochem. Soc. Trans. 29:2001;860-863
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 860-863
    • Parker, P.J.1    Parkinson, S.J.2
  • 26
    • 0034017744 scopus 로고    scopus 로고
    • Pharmacological properties of Y-27632, a specific inhibitor of Rho-associated kinases
    • Ishizaki T., Uehata M., Tamechika I., et al. Pharmacological properties of Y-27632, a specific inhibitor of Rho-associated kinases. Mol. Pharmacol. 57:2000;976-983
    • (2000) Mol. Pharmacol. , vol.57 , pp. 976-983
    • Ishizaki, T.1    Uehata, M.2    Tamechika, I.3
  • 28
    • 0030656619 scopus 로고    scopus 로고
    • Calcium sensitisation of smooth muscle mediated by a Rho-associated protein kinase in hypertension
    • Uehata M., Ishizaki T., Satoh H., et al. Calcium sensitisation of smooth muscle mediated by a Rho-associated protein kinase in hypertension. Nature. 389:1997;990-994
    • (1997) Nature , vol.389 , pp. 990-994
    • Uehata, M.1    Ishizaki, T.2    Satoh, H.3
  • 29
    • 0141751697 scopus 로고    scopus 로고
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: Modulated by G proteins, kinases, and myosin phosphatase
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase. Physiol. Rev. 83:2003;1325-1358
    • (2003) Physiol. Rev. , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.