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Volumn 27, Issue 3, 2012, Pages 130-139

Cardiac actions of protein kinase C isoforms

Author keywords

[No Author keywords available]

Indexed keywords

ISOENZYME; PROTEIN KINASE C;

EID: 84862235945     PISSN: 15489213     EISSN: 15489221     Source Type: Journal    
DOI: 10.1152/physiol.00009.2012     Document Type: Review
Times cited : (93)

References (82)
  • 3
    • 77956197814 scopus 로고    scopus 로고
    • Vitamin A metabolite, all-trans-retinoic acid, mediates alternative splicing of protein kinase C-δVIII (PKCδVIII) isoform via splicing factor SC35
    • Apostolatos H, Apostolatos A, Vickers T, Watson JE, Song S, Vale F, Cooper DR, Sanchez-Ramos J, Patel NA. Vitamin A metabolite, all-trans-retinoic acid, mediates alternative splicing of protein kinase C-δVIII (PKCδVIII) isoform via splicing factor SC35. J Biol Chem 285: 25987-25995, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 25987-25995
    • Apostolatos, H.1    Apostolatos, A.2    Vickers, T.3    Watson, J.E.4    Song, S.5    Vale, F.6    Cooper, D.R.7    Sanchez-Ramos, J.8    Patel, N.A.9
  • 6
    • 0030696157 scopus 로고    scopus 로고
    • Expression of protein kinase C-β in the heart causes hypertrophy in adult mice and sudden death in neonates
    • Bowman JC, Steinberg SF, Jiang T, Gennan D, Fishman GI, Buttrick PM. Expression of protein kinase C-β in the heart causes hypertrophy in adult mice and sudden death in neonates. J Clin Invest 100: 2189-2195, 1997.
    • (1997) J Clin Invest , vol.100 , pp. 2189-2195
    • Bowman, J.C.1    Steinberg, S.F.2    Jiang, T.3    Gennan, D.4    Fishman, G.I.5    Buttrick, P.M.6
  • 7
    • 0037018154 scopus 로고    scopus 로고
    • PKCa regulates the hypertrophic growth of cardiomyocytes through extracellular signal-regulated kinase1/2 (ERK1/2)
    • Braz JC, Bueno OF, De Windt LJ, Molkentin JD. PKCa regulates the hypertrophic growth of cardiomyocytes through extracellular signal-regulated kinase1/2 (ERK1/2). J Cell Biol 156: 905-919, 2002.
    • (2002) J Cell Biol , vol.156 , pp. 905-919
    • Braz, J.C.1    Bueno, O.F.2    de Windt, L.J.3    Molkentin, J.D.4
  • 11
    • 38849142607 scopus 로고    scopus 로고
    • A critical role of protein kinase Cδ activation loop phosphorylation in formyl-methionyl-leucyl-phenylalanine-induced phosphorylation of p47phox and rapid activation of nicotinamide adenine dinu-cleotide phosphate Oxidase
    • Cheng N, He R, Tian J, Dinauer MC, Ye RD. A critical role of protein kinase Cδ activation loop phosphorylation in formyl-methionyl-leucyl-phenylalanine-induced phosphorylation of p47phox and rapid activation of nicotinamide adenine dinu-cleotide phosphate Oxidase. J Immunol 179: 7720-7728, 2007.
    • (2007) J Immunol , vol.179 , pp. 7720-7728
    • Cheng, N.1    He, R.2    Tian, J.3    Dinauer, M.C.4    Ye, R.D.5
  • 13
    • 21544446752 scopus 로고    scopus 로고
    • Translocation of δPKC to mitochondria during cardiac reperfusion enhances superoxide anion production and induces loss in mitochondrial function
    • Churchill EN, Szweda LI. Translocation of δPKC to mitochondria during cardiac reperfusion enhances superoxide anion production and induces loss in mitochondrial function. Arch Biochem Biophys 439: 194-199, 2005.
    • (2005) Arch Biochem Biophys , vol.439 , pp. 194-199
    • Churchill, E.N.1    Szweda, L.I.2
  • 14
    • 77953654365 scopus 로고    scopus 로고
    • Inhibition of protein kinase C-(3 by ruboxistaurin preserves cardiac function and reduces extracellular matrix production in diabetic cardiomyopathy
    • Connelly KA, Kelly DJ, Zhang Y, Prior DL, Advani A, Cox AJ, Thai K, Krum H, Gilbert RE. Inhibition of protein kinase C-(3 by ruboxistaurin preserves cardiac function and reduces extracellular matrix production in diabetic cardiomyopathy. Circ Heart Fail 2: 129-137, 2009.
    • (2009) Circ Heart Fail , vol.2 , pp. 129-137
    • Connelly, K.A.1    Kelly, D.J.2    Zhang, Y.3    Prior, D.L.4    Advani, A.5    Cox, A.J.6    Thai, K.7    Krum, H.8    Gilbert, R.E.9
  • 15
    • 4344692221 scopus 로고    scopus 로고
    • Diabetic cardiomyocyte dysfunction and myocyte insulin resistance: Role of glucose-induced PKC activity
    • Davidoff AJ, Davidson MB, Carmody MW, Davis ME, Ren J. Diabetic cardiomyocyte dysfunction and myocyte insulin resistance: role of glucose-induced PKC activity. Mol Cell Biochem 262: 155-163, 2004.
    • (2004) Mol Cell Biochem , vol.262 , pp. 155-163
    • Davidoff, A.J.1    Davidson, M.B.2    Carmody, M.W.3    Davis, M.E.4    Ren, J.5
  • 16
    • 0028289497 scopus 로고
    • Localization of protein kinase C isozymes in cardiac myocytes
    • Disatnik MH, Buraggi G, Mochly-Rosen D. Localization of protein kinase C isozymes in cardiac myocytes. Exp Cell Res 210: 287-297, 1994.
    • (1994) Exp Cell Res , vol.210 , pp. 287-297
    • Disatnik, M.H.1    Buraggi, G.2    Mochly-Rosen, D.3
  • 19
    • 1842290997 scopus 로고    scopus 로고
    • Hypoxia alters the subcellular distribution of protein kinase C isoforms in neonatal rat ventricular myocytes
    • Goldberg M, Zhang HL, Steinberg SF. Hypoxia alters the subcellular distribution of protein kinase C isoforms in neonatal rat ventricular myocytes. J Clin Invest 99: 55-61, 1997.
    • (1997) J Clin Invest , vol.99 , pp. 55-61
    • Goldberg, M.1    Zhang, H.L.2    Steinberg, S.F.3
  • 20
    • 0942298111 scopus 로고    scopus 로고
    • Preservation of base-line hemodynamic function and loss of inducible cardioprotection in adult mice lacking protein kinase C-e
    • Gray MO, Zhou HZ, Schafhalter-Zoppoth I, Zhu P, Mochly-Rosen D, Messing RO. Preservation of base-line hemodynamic function and loss of inducible cardioprotection in adult mice lacking protein kinase C-e. J Biol Chem 279: 3596-3604, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 3596-3604
    • Gray, M.O.1    Zhou, H.Z.2    Schafhalter-Zoppoth, I.3    Zhu, P.4    Mochly-Rosen, D.5    Messing, R.O.6
  • 22
    • 79953190769 scopus 로고    scopus 로고
    • Protein kinase D isoforms are activated in an agonist-specific manner in cardiomyocytes
    • Guo J, Gertsberg Z, Ozgen N, Sabri A, Steinberg SF. Protein kinase D isoforms are activated in an agonist-specific manner in cardiomyocytes. J Biol Chem 286: 6500-6509, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 6500-6509
    • Guo, J.1    Gertsberg, Z.2    Ozgen, N.3    Sabri, A.4    Steinberg, S.F.5
  • 23
    • 33845655155 scopus 로고    scopus 로고
    • 1-adrenergic receptors activate AKT via a Pyk2/PDK-1 pathway that is tonically inhibited by novel protein kinase C isoforms in cardiomyocytes
    • Guo J, Sabri A, Elouardighi H, Rybin V, Steinberg SF. Alpha1-adrenergic receptors activate AKT via a Pyk2/PDK-1 pathway that is tonically inhibited by novel protein kinase C isoforms in cardiomyocytes. Circ Res 99: 1367-1375, 2006.
    • (2006) Circ Res , vol.99 , pp. 1367-1375
    • Guo, J.1    Sabri, A.2    Elouardighi, H.3    Rybin, V.4    Steinberg, S.F.5
  • 25
    • 0035834817 scopus 로고    scopus 로고
    • Differential activation of mitogen-activated protein kinase cascades and apoptosis by protein kinase c e{open} and δ in neonatal rat ventricular myocytes
    • Heidkamp MC, Bayer AL, Martin JL, Samarel AM. Differential activation of mitogen-activated protein kinase cascades and apoptosis by protein kinase c e{open} and δ in neonatal rat ventricular myocytes. Circ Res 89: 882-890, 2001.
    • (2001) Circ Res , vol.89 , pp. 882-890
    • Heidkamp, M.C.1    Bayer, A.L.2    Martin, J.L.3    Samarel, A.M.4
  • 26
    • 70349668973 scopus 로고    scopus 로고
    • PKC phosphorylation of titin's PEVK element: A novel and conserved pathway for modulating myocardial stiffness
    • Hidalgo C, Hudson B, Bogomolovas J, Zhu Y, Anderson B, Greaser M, Labeit S, Granzier H. PKC phosphorylation of titin's PEVK element: a novel and conserved pathway for modulating myocardial stiffness. Circ Res 105: 631-638, 17, 2009.
    • (2009) Circ Res , vol.105 , Issue.17 , pp. 631-638
    • Hidalgo, C.1    Hudson, B.2    Bogomolovas, J.3    Zhu, Y.4    Anderson, B.5    Greaser, M.6    Labeit, S.7    Granzier, H.8
  • 30
    • 0026489335 scopus 로고
    • Preferential elevation of protein kinase C isoform β-II and diacylglycerol levels in the aorta and heart of diabetic rats: Differential reversibility to glycemic control by islet cell transplantation
    • Inoguchi T, Battan R, Handler E, Sportsman JR, Heath W, King GL. Preferential elevation of protein kinase C isoform β-II and diacylglycerol levels in the aorta and heart of diabetic rats: differential reversibility to glycemic control by islet cell transplantation. Proc Natl Acad Sci USA 89: 11059-11063, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11059-11063
    • Inoguchi, T.1    Battan, R.2    Handler, E.3    Sportsman, J.R.4    Heath, W.5    King, G.L.6
  • 31
    • 77958006009 scopus 로고    scopus 로고
    • Receptor-independent cardiac protein kinase Cα activation by calpain-mediated truncation of regulatory domains
    • Kang MY, Zhang Y, Matkovich SJ, Diwan A, Chishti AH, Dorn GW. Receptor-independent cardiac protein kinase Cα activation by calpain-mediated truncation of regulatory domains. Circ Res 107: 903-912, 2010.
    • (2010) Circ Res , vol.107 , pp. 903-912
    • Kang, M.Y.1    Zhang, Y.2    Matkovich, S.J.3    Diwan, A.4    Chishti, A.H.5    Dorn, G.W.6
  • 33
    • 33747372839 scopus 로고    scopus 로고
    • Protein kinase Cδ-annexin V interaction: A required step in SPKC translocation and function
    • Kheifets V, Bright R, Inagaki K, Schechtman D, Mochly-Rosen D. Protein kinase Cδ-annexin V interaction: a required step in SPKC translocation and function. J Biol Chem 281: 23218-23226, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 23218-23226
    • Kheifets, V.1    Bright, R.2    Inagaki, K.3    Schechtman, D.4    Mochly-Rosen, D.5
  • 34
    • 34250757608 scopus 로고    scopus 로고
    • Insight into intra-and inter-molecular interactions of PKC: Design of specific modulators of kinase function
    • Kheifets V, Mochly-Rosen D. Insight into intra-and inter-molecular interactions of PKC: design of specific modulators of kinase function. Pharmacol Res 55: 467-476, 2007.
    • (2007) Pharmacol Res , vol.55 , pp. 467-476
    • Kheifets, V.1    Mochly-Rosen, D.2
  • 40
    • 69949148383 scopus 로고    scopus 로고
    • Recognition of an intra-chain tandem 14-3-3 binding site within PKCe{open}
    • Kostelecky B, Saurin AT, Purkiss A, Parker PJ, McDonald NQ. Recognition of an intra-chain tandem 14-3-3 binding site within PKCe{open}. EMBO Rep 10: 983-989, 2009.
    • (2009) EMBO Rep , vol.10 , pp. 983-989
    • Kostelecky, B.1    Saurin, A.T.2    Purkiss, A.3    Parker, P.J.4    McDonald, N.Q.5
  • 41
    • 80052180666 scopus 로고    scopus 로고
    • Inhibition of PI3K binding to activators by serine phosphorylation of PI3K regulatory subunit p85α Src homology-2 domains
    • Lee JY, Chiu YH, Asara J, Cantley LC. Inhibition of PI3K binding to activators by serine phosphorylation of PI3K regulatory subunit p85α Src ho-mology-2 domains. Proc Natl Acad Sci USA 108: 14157-14162, 2011.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 14157-14162
    • Lee, J.Y.1    Chiu, Y.H.2    Asara, J.3    Cantley, L.C.4
  • 44
    • 68049086486 scopus 로고    scopus 로고
    • Protein kinase Cα, but not PKCβ or PKC7, regulates contractility and heart failure susceptibility: Implications for ruboxistaurin as a novel therapeutic approach
    • Liu Q, Chen X, MacDonnell SM, Kranias EG, Lorenz JN, Leitges M, Houser SR, Molkentin JD. Protein kinase Cα, but not PKCβ or PKC7, regulates contractility and heart failure susceptibility: implications for ruboxistaurin as a novel therapeutic approach. Circ Res 105: 194-200, 2009.
    • (2009) Circ Res , vol.105 , pp. 194-200
    • Liu, Q.1    Chen, X.2    Macdonnell, S.M.3    Kranias, E.G.4    Lorenz, J.N.5    Leitges, M.6    Houser, S.R.7    Molkentin, J.D.8
  • 45
    • 34548425994 scopus 로고    scopus 로고
    • The phosphorylation of tyrosine 332 is necessary for the caspase 3-dependent cleavage of PKCδ and the regulation of cell apoptosis
    • Lu W, Lee HK, Xiang C, Finniss S, Brodie C. The phosphorylation of tyrosine 332 is necessary for the caspase 3-dependent cleavage of PKCδ and the regulation of cell apoptosis. Cell Signal 19: 2165-2173, 2007.
    • (2007) Cell Signal , vol.19 , pp. 2165-2173
    • Lu, W.1    Lee, H.K.2    Xiang, C.3    Finniss, S.4    Brodie, C.5
  • 47
    • 77951520888 scopus 로고    scopus 로고
    • q-mediated activation of GRK2 by mechanical stretch in cardiac myocytes: The role of protein kinase C
    • Malhotra R, D'Souza KM, Staron ML, Birukov KG, Bodi I, Akhter SA. Gαq-mediated activation of GRK2 by mechanical stretch in cardiac myocytes: the role of protein kinase C. J Biol Chem 285: 13748-13760, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 13748-13760
    • Malhotra, R.1    D'souza, K.M.2    Staron, M.L.3    Birukov, K.G.4    Bodi, I.5    Akhter, S.A.6
  • 48
    • 33646832740 scopus 로고    scopus 로고
    • Regulation of protein kinase C δ by phorbol ester, endothelin-1, and platelet-derived growth factor in cardiac myocytes
    • Markou T, Yong CS, Sugden PH, Clerk A. Regulation of protein kinase C δ by phorbol ester, endothelin-1, and platelet-derived growth factor in cardiac myocytes. J Biol Chem 281: 8321-8331, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 8321-8331
    • Markou, T.1    Yong, C.S.2    Sugden, P.H.3    Clerk, A.4
  • 50
    • 79953241079 scopus 로고    scopus 로고
    • Glomerular-specific protein kinase C-β-induced insulin receptor substrate-1 dysfunction and insulin resistance in rat models of diabetes and obesity
    • Mima A, Ohshiro Y, Kitada M, Matsumoto M, Geraldes P, Li C, Li Q, White GS, Cahill C, Rask-Madsen C, King GL. Glomerular-specific protein kinase C-β-induced insulin receptor substrate-1 dysfunction and insulin resistance in rat models of diabetes and obesity. Kidney Int 79: 883-896, 2011.
    • (2011) Kidney Int , vol.79 , pp. 883-896
    • Mima, A.1    Ohshiro, Y.2    Kitada, M.3    Matsumoto, M.4    Geraldes, P.5    Li, C.6    Li, Q.7    White, G.S.8    Cahill, C.9    Rask-Madsen, C.10    King, G.L.11
  • 51
    • 9144256765 scopus 로고    scopus 로고
    • Protein kinase Cδ activation induces apoptosis in response to cardiac ischemia and reperfusion damage: A mechanism involving BAD and the mitochondria
    • Murriel CL, Churchill E, Inagaki K, Szweda LI, Mochly-Rosen D. Protein kinase Cδ activation induces apoptosis in response to cardiac ischemia and reperfusion damage: a mechanism involving BAD and the mitochondria. J Biol Chem 279: 47985-47991, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 47985-47991
    • Murriel, C.L.1    Churchill, E.2    Inagaki, K.3    Szweda, L.I.4    Mochly-Rosen, D.5
  • 52
    • 0037337159 scopus 로고    scopus 로고
    • Regulation of the ABC kinases by phosphorylation: Protein kinase C as a paradigm
    • Newton AC. Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm. Biochem J 370: 361-371, 2003.
    • (2003) Biochem J , vol.370 , pp. 361-371
    • Newton, A.C.1
  • 55
    • 1842478943 scopus 로고    scopus 로고
    • Insulin regulates protein kinase CβII alternative splicing in multiple target tissues: Development of a hormonally responsive heterologous mini-gene
    • Patel NA, Apostolatos HS, Mebert K, Chalfant CE, Watson JE, Pillay TS, Sparks J, Cooper DR. Insulin regulates protein kinase CβII alternative splicing in multiple target tissues: development of a hormonally responsive heterologous mini-gene. Mol Endocrinol 18: 899-911, 2004.
    • (2004) Mol Endocrinol , vol.18 , pp. 899-911
    • Patel, N.A.1    Apostolatos, H.S.2    Mebert, K.3    Chalfant, C.E.4    Watson, J.E.5    Pillay, T.S.6    Sparks, J.7    Cooper, D.R.8
  • 56
    • 0030872474 scopus 로고    scopus 로고
    • Ischemic preconditioning induces selective translocation of protein kinase C isoforms epsilon and eta in the heart of conscious rabbits without subcellular redistribution of total protein kinase C activity
    • Ping P, Zhang J, Qiu Y, Tang XL, Manchikalapudi S, Cao X, Bolli R. Ischemic preconditioning induces selective translocation of protein kinase C isoforms epsilon and eta 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
  • 60
    • 34548183625 scopus 로고    scopus 로고
    • Protein kinase Ce{open} and Src control PKCS activation loop phosphorylation in cardio-myocytes
    • Rybin VO, Guo J, Gertsberg Z, Elouardighi H, Steinberg SF. Protein kinase Ce{open} and Src control PKCδ activation loop phosphorylation in cardio-myocytes. J Biol Chem 282: 23631-23638, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 23631-23638
    • Rybin, V.O.1    Guo, J.2    Gertsberg, Z.3    Elouardighi, H.4    Steinberg, S.F.5
  • 63
    • 2442498430 scopus 로고    scopus 로고
    • Stimulus-specific differences in protein kinase C-δ localization and activation mechanisms in cardiomyocytes
    • Rybin VO, Guo J, Sabri A, Elouardighi H, Schaefer E, Steinberg SF. Stimulus-specific differences in protein kinase C-δ localization and activation mechanisms in cardiomyocytes. J Biol Chem 279: 19350-19361, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 19350-19361
    • Rybin, V.O.1    Guo, J.2    Sabri, A.3    Elouardighi, H.4    Schaefer, E.5    Steinberg, S.F.6
  • 64
    • 0030911501 scopus 로고    scopus 로고
    • Do adult rat ventricular myocytes express protein kinase Cα?
    • Rybin VO, Steinberg SF. Do adult rat ventricular myocytes express protein kinase Cα? Am J Physiol Heart Circ Physiol 272: H2485-H2491, 1997.
    • (1997) Am J Physiol Heart Circ Physiol , vol.272
    • Rybin, V.O.1    Steinberg, S.F.2
  • 65
    • 0028158867 scopus 로고
    • Protein kinase C isoform expression and regulation in the developing rat heart
    • Rybin VO, Steinberg SF. Protein kinase C isoform expression and regulation in the developing rat heart. Circ Res 74: 299-309, 1994.
    • (1994) Circ Res , vol.74 , pp. 299-309
    • Rybin, V.O.1    Steinberg, S.F.2
  • 66
    • 0035839578 scopus 로고    scopus 로고
    • Binding specificity for RACK1 resides in the V5 region of βII protein kinase C
    • Stebbins EG, Mochly-Rosen D. Binding specificity for RACK1 resides in the V5 region of βII protein kinase C. J Biol Chem 276: 29644-29650, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 29644-29650
    • Stebbins, E.G.1    Mochly-Rosen, D.2
  • 67
    • 10944238407 scopus 로고    scopus 로고
    • Distinctive activation mechanisms and functions for protein kinase C-δ
    • Steinberg SF. Distinctive activation mechanisms and functions for protein kinase C-δ. Biochem J 384: 449-459, 2004.
    • (2004) Biochem J , vol.384 , pp. 449-459
    • Steinberg, S.F.1
  • 68
    • 55949109631 scopus 로고    scopus 로고
    • Structural basis of protein kinase C isoform function
    • Steinberg SF. Structural basis of protein kinase C isoform function. Physiol Rev 88: 1341-1378, 2008.
    • (2008) Physiol Rev , vol.88 , pp. 1341-1378
    • Steinberg, S.F.1
  • 69
    • 0030894024 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase Cδ at threonine 505 is not a prerequisite for enzymatic activity
    • Stempka L, Girod A, Muller HJ, Rincke G, Marks F, Gschwendt M, Bossemeyer D. Phosphorylation of protein kinase Cδ at threonine 505 is not a prerequisite for enzymatic activity. J Biol Chem 272: 6805-6811, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 6805-6811
    • Stempka, L.1    Girod, A.2    Muller, H.J.3    Rincke, G.4    Marks, F.5    Gschwendt, M.6    Bossemeyer, D.7
  • 70
    • 0041816273 scopus 로고    scopus 로고
    • Identification of a functionally critical protein kinase C phosphorylation residue of cardiac troponin T
    • Sumandea MP, Pyle WG, Kobayashi T, de Tombe PP, Solaro RJ. Identification of a functionally critical protein kinase C phosphorylation residue of cardiac troponin T. J Biol Chem 278: 35135-35144, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 35135-35144
    • Sumandea, M.P.1    Pyle, W.G.2    Kobayashi, T.3    de Tombe, P.P.4    Solaro, R.J.5
  • 73
    • 0033529591 scopus 로고    scopus 로고
    • Responses of cardiac protein kinase C isoforms to distinct pathological stimuli are differentially regulated
    • Takeishi Y, Jalili T, Ball NA, Walsh RA. Responses of cardiac protein kinase C isoforms to distinct pathological stimuli are differentially regulated. Circ Res 85: 264-271, 1999.
    • (1999) Circ Res , vol.85 , pp. 264-271
    • Takeishi, Y.1    Jalili, T.2    Ball, N.A.3    Walsh, R.A.4
  • 74
    • 0034705485 scopus 로고    scopus 로고
    • Transgenic overexpression of con-stitutively active protein kinase Ce causes concentric cardiac hypertrophy
    • Takeishi Y, Ping P, Bolli R, Kirkpatrick DL, Hoit BD, Walsh RA. Transgenic overexpression of con-stitutively active protein kinase Ce causes concentric cardiac hypertrophy. Circ Res 86: 1218-1223, 2000.
    • (2000) Circ Res , vol.86 , pp. 1218-1223
    • Takeishi, Y.1    Ping, P.2    Bolli, R.3    Kirkpatrick, D.L.4    Hoit, B.D.5    Walsh, R.A.6
  • 75
    • 33244464562 scopus 로고    scopus 로고
    • Critical nodes in signalling pathways: Insights into insulin action
    • Taniguchi CM, Emanuelli B, Kahn CR. Critical nodes in signalling pathways: insights into insulin action. Nat Rev Mol Cell Biol 7: 85-96, 2006.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 85-96
    • Taniguchi, C.M.1    Emanuelli, B.2    Kahn, C.R.3
  • 78
    • 0034942907 scopus 로고    scopus 로고
    • Crucial role of calpain in hypoxic PC12 cell death: Calpain, but not caspases, mediates degradation of cytoskeletal proteins and protein kinase C-al-pha and -delta
    • Yamakawa H, Banno Y, Nakashima S, Yoshimura S, Sawada M, Nishimura Y, Nozawa Y, Sakai N. Crucial role of calpain in hypoxic PC12 cell death: calpain, but not caspases, mediates degradation of cytoskeletal proteins and protein kinase C-al-pha and -delta. Neurol Res 23: 522-530, 2001.
    • (2001) Neurol Res , vol.23 , pp. 522-530
    • Yamakawa, H.1    Banno, Y.2    Nakashima, S.3    Yoshimura, S.4    Sawada, M.5    Nishimura, Y.6    Nozawa, Y.7    Sakai, N.8
  • 82
    • 79960679247 scopus 로고    scopus 로고
    • Receptor-independent protein kinase C-a signaling by calpain-generated free catalytic domains induces HDAC5 nuclear export and regulates cardiac transcription
    • Zhang Y, Matkovich SJ, Duan X, Diwan A, Kang MY, Dorn GW. Receptor-independent protein kinase C-a signaling by calpain-generated free catalytic domains induces HDAC5 nuclear export and regulates cardiac transcription. J Biol Chem 286: 26943-26951, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 26943-26951
    • Zhang, Y.1    Matkovich, S.J.2    Duan, X.3    Diwan, A.4    Kang, M.Y.5    Dorn, G.W.6


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