메뉴 건너뛰기




Volumn 275, Issue 6 44-6, 1998, Pages

Ischemic preconditioning translocates PKC-δ and-ε, which mediate functional protection in isolated rat heart

Author keywords

Contractile function; Ischemia; Low calcium perfusion; Protein kinase C inhibitors; Protein kinase C isoforms

Indexed keywords

BISINDOLYLMALEIMIDE; ISOENZYME; PROTEIN KINASE C;

EID: 33750865610     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.1998.275.6.h2266     Document Type: Article
Times cited : (144)

References (36)
  • 2
    • 0026766553 scopus 로고
    • Protein kinase C enhances myosin light-chain kinase effects on force development and ATPase activity in rat single skinned cardiac cells
    • Clement, O., M. Puceat, M. P. Walsh, and G. Vassort. Protein kinase C enhances myosin light-chain kinase effects on force development and ATPase activity in rat single skinned cardiac cells. Biochem. J. 285: 311-317, 1992.
    • (1992) Biochem. J. , vol.285 , pp. 311-317
    • Clement, O.1    Puceat, M.2    Walsh, M.P.3    Vassort, G.4
  • 3
    • 0029885316 scopus 로고    scopus 로고
    • Preconditioning in rabbit cardiomyocytes: Role of pH, vacuolar proton ATPase, and apoptosis
    • Gottlieb, R. A., D. L. Gruol, J. Y. Zhu, and R. L. Engler. Preconditioning in rabbit cardiomyocytes: role of pH, vacuolar proton ATPase, and apoptosis. J. Clin. Invest. 97: 2391-2398, 1996.
    • (1996) J. Clin. Invest. , vol.97 , pp. 2391-2398
    • Gottlieb, R.A.1    Gruol, D.L.2    Zhu, J.Y.3    Engler, R.L.4
  • 4
    • 0030609162 scopus 로고    scopus 로고
    • A selective epsilon-protein kinase C antagonist inhibits protection of cardiac myocytes from hypoxia-induced cell death
    • Gray, M. O., J. S. Karliner, and D. Mochly-Rosen. A selective epsilon-protein kinase C antagonist inhibits protection of cardiac myocytes from hypoxia-induced cell death. J. Biol. Chem. 272: 30945-30951, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30945-30951
    • Gray, M.O.1    Karliner, J.S.2    Mochly-Rosen, D.3
  • 7
    • 0028868582 scopus 로고
    • 1β-adrenoceptors, pertussis toxin-sensitive G proteins, and protein kinase C
    • 1β-adrenoceptors, pertussis toxin-sensitive G proteins, and protein kinase C. Circulation 92: 2259-2265, 1995.
    • (1995) Circulation , vol.92 , pp. 2259-2265
    • Keli, H.1    Stanley, N.2
  • 8
    • 0030033229 scopus 로고    scopus 로고
    • Role of activation of protein kinase C in the infarct size-limiting effect of ischemic preconditioning through activation of ecto-5′-nucleotidase
    • Kitakaze, M., K. Node, T. Minamino, K. Komamura, H. Funaya, Y. Shinozaki, M. Chujo, H. Mori, M. Inoue, M. Hori, and T. Kamada. Role of activation of protein kinase C in the infarct size-limiting effect of ischemic preconditioning through activation of ecto-5′-nucleotidase. Circulation 93: 781-791, 1996.
    • (1996) Circulation , vol.93 , pp. 781-791
    • Kitakaze, M.1    Node, K.2    Minamino, T.3    Komamura, K.4    Funaya, H.5    Shinozaki, Y.6    Chujo, M.7    Mori, H.8    Inoue, M.9    Hori, M.10    Kamada, T.11
  • 9
    • 0025316036 scopus 로고
    • Antiplatelet effects of chelerythrine chloride isolated from Zanthoxylum simulans
    • Ko, F. N., I. S. Chen, S. J. Wu, L. G. Lee, T. F. Haung, and C. M. Teng. Antiplatelet effects of chelerythrine chloride isolated from Zanthoxylum simulans. Biochim. Biophys. Acta 1052: 360-365, 1990.
    • (1990) Biochim. Biophys. Acta , vol.1052 , pp. 360-365
    • Ko, F.N.1    Chen, I.S.2    Wu, S.J.3    Lee, L.G.4    Haung, T.F.5    Teng, C.M.6
  • 11
    • 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 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0028287617 scopus 로고
    • Evidence that translocation of protein kinase C is a key event during ischemic preconditioning of rabbit myocardium
    • Liu, Y., K. Ytrehus, and J. M. Downey. Evidence that translocation of protein kinase C is a key event during ischemic preconditioning of rabbit myocardium. J. Mol. Cell. Cardiol. 26: 661-668, 1994.
    • (1994) J. Mol. Cell. Cardiol. , vol.26 , pp. 661-668
    • Liu, Y.1    Ytrehus, K.2    Downey, J.M.3
  • 17
  • 18
    • 0029934577 scopus 로고    scopus 로고
    • Calcium preconditioning elicits strong protection against ischemic injury via protein kinase C signaling pathway
    • Miyawaki, H., X. Zhou, and M. Ashraf. Calcium preconditioning elicits strong protection against ischemic injury via protein kinase C signaling pathway. Circ. Res. 79: 137-146, 1996.
    • (1996) Circ. Res. , vol.79 , pp. 137-146
    • Miyawaki, H.1    Zhou, X.2    Ashraf, M.3
  • 19
    • 0031029249 scopus 로고    scopus 로고
    • Nuclear translocation of PKC during ischemia and its inhibition by wortmannin, an inhibitor of phosphatidylinositol 3-kinase
    • Mizukami, Y., T. Hirata, and K. Yoshida. Nuclear translocation of PKC during ischemia and its inhibition by wortmannin, an inhibitor of phosphatidylinositol 3-kinase. FEBS Lett. 401: 247-251, 1997.
    • (1997) FEBS Lett. , vol.401 , pp. 247-251
    • Mizukami, Y.1    Hirata, T.2    Yoshida, K.3
  • 20
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: A delay of lethal cell injury in ischemic myocardium
    • Murry, C. E., R. B. Jennings, and K. A. Reimer. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circ. Res. 74: 1124-1136, 1986.
    • (1986) Circ. Res. , vol.74 , pp. 1124-1136
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 21
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function and regulation
    • Newton, A. C. Protein kinase C: structure, function and regulation. J. Biol. Chem. 270: 28495-28498, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 22
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka, Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 258: 607-614, 1992.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 23
    • 0030872474 scopus 로고    scopus 로고
    • Ischemic preconditioning induces selective translocation of protein kinase C isoforms ε and η in the heart of conscious rabbits without subcellular redistribution of total protein kinase C activity
    • Ping, P., J. Zhang, Y. Qiu, X.-L. Tang, S. Manchikalapudi, X. Cao, and R. Bolli. Ischemic preconditioning induces selective translocation of protein kinase C isoforms ε and η in the heart of conscious rabbits without subcellular redistribution of total protein kinase C activity. Circ. Res. 81: 404-414, 1997.
    • (1997) Circ. Res. , vol.81 , pp. 404-414
    • Ping, P.1    Zhang, J.2    Qiu, Y.3    Tang, X.-L.4    Manchikalapudi, S.5    Cao, X.6    Bolli, R.7
  • 24
    • 33751335033 scopus 로고    scopus 로고
    • PKC-λ is the atypical protein kinase C isoform expressed by immature ventricle
    • Heart Circ. Physiol. 41
    • Rybin, V. O., P. M. Buttrick, and S. F. Steinberg. PKC-λ is the atypical protein kinase C isoform expressed by immature ventricle. Am. J. Physiol. 272 (Heart Circ. Physiol. 41): H1636-H1642, 1997.
    • (1997) Am. J. Physiol. , vol.272
    • Rybin, V.O.1    Buttrick, P.M.2    Steinberg, S.F.3
  • 25
    • 0027197933 scopus 로고
    • Signal transduction pathways of angiotensin II-induced c-fos gene expression in cardiac myocytes in vitro: Roles of phospholipid-derived second messengers
    • Sadoshima, J., and S. Izumo. Signal transduction pathways of angiotensin II-induced c-fos gene expression in cardiac myocytes in vitro: roles of phospholipid-derived second messengers. Circ. Res. 73: 424-438, 1993.
    • (1993) Circ. Res. , vol.73 , pp. 424-438
    • Sadoshima, J.1    Izumo, S.2
  • 26
    • 0025219050 scopus 로고
    • Ischemic preconditioning reduces infarct size in swine myocardium
    • Schott, R. J., E. R. Rohman, E. R. Braun, and W. Schaper. Ischemic preconditioning reduces infarct size in swine myocardium. Circ. Res. 66: 1133-1142, 1990.
    • (1990) Circ. Res. , vol.66 , pp. 1133-1142
    • Schott, R.J.1    Rohman, E.R.2    Braun, E.R.3    Schaper, W.4
  • 27
    • 0028808229 scopus 로고
    • + channel? Studies of contractile function after simulated ischemia in an atrial in vivo model
    • + channel? Studies of contractile function after simulated ischemia in an atrial in vivo model. Circ. Res. 77: 1030-1035, 1995.
    • (1995) Circ. Res. , vol.77 , pp. 1030-1035
    • Speechly-Dick, M.E.1    Grover, G.J.2    Yellon, D.M.3
  • 28
    • 0027980893 scopus 로고
    • Protein kinase C: Its role in ischemic preconditioning in the rat
    • Speechly-Dick, M. E., M. M. Mocanu, and D. M. Yellon. Protein kinase C: its role in ischemic preconditioning in the rat. Circ. Res. 75: 586-590, 1994.
    • (1994) Circ. Res. , vol.75 , pp. 586-590
    • Speechly-Dick, M.E.1    Mocanu, M.M.2    Yellon, D.M.3
  • 30
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylarnide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. Electrophoretic transfer of proteins from polyacrylarnide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76: 4350-4354, 1979.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 32
    • 0027248968 scopus 로고
    • Role of protein kinase C in the phosphorylation of cardiac myosin light chain 2
    • Venema, R. C., R. L. Raynor, T. A. Noland, and J. F. Kuo. Role of protein kinase C in the phosphorylation of cardiac myosin light chain 2. Biochem. J. 294: 401-406, 1993.
    • (1993) Biochem. J. , vol.294 , pp. 401-406
    • Venema, R.C.1    Raynor, R.L.2    Noland, T.A.3    Kuo, J.F.4
  • 33
    • 0028904681 scopus 로고
    • Cardioprotection in an in vitro model of hypoxic preconditioning
    • Webster, K. A., D. J. Discher, and N. H. Bishopric. Cardioprotection in an in vitro model of hypoxic preconditioning. J. Mol. Cell. Cardiol. 27: 453-458, 1995.
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , pp. 453-458
    • Webster, K.A.1    Discher, D.J.2    Bishopric, N.H.3
  • 34
    • 0027248964 scopus 로고
    • Isoenzyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase C
    • Wilkinson, S. E., P. J. Parker, and J. S. Nixon. Isoenzyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase C. Biochem. J. 294: 335-337, 1993.
    • (1993) Biochem. J. , vol.294 , pp. 335-337
    • Wilkinson, S.E.1    Parker, P.J.2    Nixon, J.S.3
  • 35
    • 0029113594 scopus 로고
    • Reperfusion of rat heart after brief ischemia induces proteolysis of calspectin (nonerythroid spectrin or fodrin) by calpain
    • Yoshida, K., M. Inui, K. Harada, T. C. Saido, Y. Sorimachi, T. Ishihara, S. Kawashima, and K. Sobue. Reperfusion of rat heart after brief ischemia induces proteolysis of calspectin (nonerythroid spectrin or fodrin) by calpain. Circ. Res. 77: 603-610, 1995.
    • (1995) Circ. Res. , vol.77 , pp. 603-610
    • Yoshida, K.1    Inui, M.2    Harada, K.3    Saido, T.C.4    Sorimachi, Y.5    Ishihara, T.6    Kawashima, S.7    Sobue, K.8
  • 36
    • 0028348870 scopus 로고
    • Preconditioning protects ischemic rabbit heart by protein kinase C activation
    • Heart Circ. Physiol. 35
    • Ytrehus, K., Y. Liu, and J. M. Downey. Preconditioning protects ischemic rabbit heart by protein kinase C activation. Am. J. Physiol. 266 (Heart Circ. Physiol. 35): H1145-H1152, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Ytrehus, K.1    Liu, Y.2    Downey, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.