메뉴 건너뛰기




Volumn 3, Issue 7, 2010, Pages 2111-2145

Protein kinases as drug development targets for heart disease therapy

Author keywords

Mitogen activated protein kinases; Phosphoinositide 3 kinase; Protein kinase A; Protein kinase C

Indexed keywords

1 [7 (4 FLUOROPHENYL) 1,2,3,4 TETRAHYDRO 8 (4 PYRIDYL)PYRAZOLO[5,1 C][1,2,4]TRIAZIN 2 YL] 2 PHENYLETHANEDIONE; 2 MORPHOLINO 8 PHENYLCHROMONE; 2 [1 (3 DIMETHYLAMINOPROPYL) 3 INDOLYL] 3 (3 INDOLYL)MALEIMIDE; 2 [1 (3 DIMETHYLAMINOPROPYL) 5 METHOXY 1H INDOL 3 YL] 3 (1H INDOL 3 YL)MALEIMIDE; 3 [8 [(DIMETHYLAMINO)METHYL] 6,7,8,9 TETRAHYDROPYRIDO[1,2 A]INDOL 10 YL] 4 (1 METHYL 1H INDOL 3 YL) 1H PYRROLE 2,5 DIONE; 4 (4 FLUOROPHENYL) 2 (4 HYDROXYPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 4 [4 (4 FLUOROPHENYL) 5 (2 METHOXY 4 PYRIMIDINYL) 1 IMIDAZOLYL]CYCLOHEXANOL; ANGIOTENSIN II; BREVISCAPINE; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE; INDUCIBLE NITRIC OXIDE SYNTHASE; KT 5720; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE; PROTEIN KINASE C; PROTEIN KINASE C ALPHA INHIBITOR; PROTEIN KINASE C BETA INHIBITOR; RO 318110; RUBOXISTAURIN; UNCLASSIFIED DRUG; WORTMANNIN;

EID: 77955690900     PISSN: None     EISSN: 14248247     Source Type: Journal    
DOI: 10.3390/ph3072111     Document Type: Review
Times cited : (31)

References (246)
  • 1
    • 0021227676 scopus 로고
    • The role of protein kinase C in cell surface signal transduction and tumourpromotion
    • Nishizuka, Y. The role of protein kinase C in cell surface signal transduction and tumourpromotion. Nature 1984, 308, 693-698.
    • (1984) Nature , vol.308 , pp. 693-698
    • Nishizuka, Y.1
  • 2
    • 0030042940 scopus 로고    scopus 로고
    • Precisionsubstrate targeting of protein kinases. The cGMP- and cAMP-dependent protein kinases
    • Wood, J. S.; Yan, X.; Mendelow, M.; Corbin, J. D.; Francis, S. H.; Lawrence, D. S. Precisionsubstrate targeting of protein kinases. The cGMP- and cAMP-dependent protein kinases. J. Biol.Chem. 1996, 271, 174-179.
    • (1996) J. Biol.Chem , vol.271 , pp. 174-179
    • Wood, J.S.1    Yan, X.2    Mendelow, M.3    Corbin, J.D.4    Francis, S.H.5    Lawrence, D.S.6
  • 3
    • 0037547800 scopus 로고    scopus 로고
    • Role of protein kinase C and protein kinase A in heart function in healthand disease
    • Dhalla, N. S.; Wang, J. Role of protein kinase C and protein kinase A in heart function in healthand disease. Exp. Clin. Cardiol. 1999, 4, 7-14.
    • (1999) Exp. Clin. Cardiol , vol.4 , pp. 7-14
    • Dhalla, N.S.1    Wang, J.2
  • 4
    • 0033967128 scopus 로고    scopus 로고
    • Apoptosis in cardiac diseases: Stress- and mitogen-activatedsignaling pathways
    • Feuerstein, G. Z.; Young, P. R. Apoptosis in cardiac diseases: Stress- and mitogen-activatedsignaling pathways. Cardiovasc. Res. 2000, 45, 560-569.
    • (2000) Cardiovasc. Res , vol.45 , pp. 560-569
    • Feuerstein, G.Z.1    Young, P.R.2
  • 5
    • 0028868828 scopus 로고
    • Intracellular signaling through protein kinases in the heart
    • Sugden, P. H.; Bogoyevitch, M. A. Intracellular signaling through protein kinases in the heart.Cardiovasc. Res. 1995, 30, 478-492.
    • (1995) Cardiovasc. Res , vol.30 , pp. 478-492
    • Sugden, P.H.1    Bogoyevitch, M.A.2
  • 6
    • 0028928616 scopus 로고
    • Other hypertrophic stimulimediated by G protein-coupled receptors activate tyrosine kinase, mitogen-activated proteinkinase, and 90-kD S6 kinase in cardiac myocytes. The critical role of Ca2+-dependent signaling
    • Sadoshima, J.; Qiu, Z.; Morgan, J. P.; Izumo, S. Angiotensin II and other hypertrophic stimulimediated by G protein-coupled receptors activate tyrosine kinase, mitogen-activated proteinkinase, and 90-kD S6 kinase in cardiac myocytes. The critical role of Ca2+-dependent signaling.Circ. Res. 1995, 76, 1-15.
    • (1995) Circ. Res , vol.76 , pp. 1-15
    • Sadoshima, J.1    Qiu, Z.2    Morgan, J.P.3    Izumo, S.4    Angiotensin, I.I.5
  • 8
    • 0025330489 scopus 로고
    • CAMP-dependent protein kinase: Framework for adiverse family of regulatory enzymes
    • Taylor, S. S.; Buechler, J. A.; Yonemoto, W. cAMP-dependent protein kinase: Framework for adiverse family of regulatory enzymes. Annu. Rev. Biochem. 1990, 59, 971-1005.
    • (1990) Annu. Rev. Biochem , vol.59 , pp. 971-1005
    • Taylor, S.S.1    Buechler, J.A.2    Yonemoto, W.3
  • 9
    • 2642707085 scopus 로고
    • Receptors and signal transduction
    • In The Heart, Physiology and Metabolism; Opie, L. H., ed., NY, USA
    • Opie, L. H. Receptors and signal transduction. In The Heart, Physiology and Metabolism; Opie, L. H., ed.; Raven Press: New York, NY, USA, 1991; pp. 147-175.
    • (1991) Raven Press: New York , pp. 147-175
    • Opie, L.H.1
  • 10
    • 77951634985 scopus 로고    scopus 로고
    • Phosphorylation and function of cardiac myosin binding protein-Cin health and disease
    • Barefield, D.; Sadayappan, S. Phosphorylation and function of cardiac myosin binding protein-Cin health and disease. J. Mol. Cell. Cardiol. 2010, 48, 866-875.
    • (2010) J. Mol. Cell. Cardiol , vol.48 , pp. 866-875
    • Barefield, D.1    Sadayappan, S.2
  • 11
    • 37349117667 scopus 로고    scopus 로고
    • Modulation of cardiac troponin C function by thecardiac-specific N-terminus of troponin I: Influence of PKA phosphorylation and involvement incardiomyopathies
    • Baryshnikova, O. K.; Li, M. X.; Sykes, B. D. Modulation of cardiac troponin C function by thecardiac-specific N-terminus of troponin I: Influence of PKA phosphorylation and involvement incardiomyopathies. J. Mol. Biol. 2008, 375, 735-751.
    • (2008) J. Mol. Biol , vol.375 , pp. 735-751
    • Baryshnikova, O.K.1    Li, M.X.2    Sykes, B.D.3
  • 12
    • 40449137643 scopus 로고    scopus 로고
    • Localization of PKA phosphorylation site, Ser(2030), in the three-dimensional structure ofcardiac ryanodine receptor
    • Jones, P. P.; Meng, X.; Xiao, B.; Cai, S.; Bolstad, J.; Wagenknecht, T.; Liu, Z.; Chen, S. R.Localization of PKA phosphorylation site, Ser(2030), in the three-dimensional structure ofcardiac ryanodine receptor. Biochem. J. 2008, 410, 261-270.
    • (2008) Biochem. J , vol.410 , pp. 261-270
    • Jones, P.P.1    Meng, X.2    Xiao, B.3    Cai, S.4    Bolstad, J.5    Wagenknecht, T.6    Liu, Z.7    Chen, S.R.8
  • 13
    • 1842591777 scopus 로고    scopus 로고
    • Conformational changes within the cytosolic portion ofphospholamban upon release of Ca-ATPase inhibition
    • Li, J.; Bigelow, D. J.; Squier, T. C. Conformational changes within the cytosolic portion ofphospholamban upon release of Ca-ATPase inhibition. Biochemistry 2004, 43, 3870-3879.
    • (2004) Biochemistry , vol.43 , pp. 3870-3879
    • Li, J.1    Bigelow, D.J.2    Squier, T.C.3
  • 14
    • 0030015928 scopus 로고    scopus 로고
    • Myofibrillar calciumsensitivity of isometric tension is increased in human dilated cardiomyopathies: Role of alteredbeta-adrenergically mediated protein phosphorylation
    • Wolff, M. R.; Buck, S. H.; Stoker, S. W.; Greaser, M. L.; Mentzer, R. M. Myofibrillar calciumsensitivity of isometric tension is increased in human dilated cardiomyopathies: Role of alteredbeta-adrenergically mediated protein phosphorylation. J. Clin. Invest. 1996, 98, 167-176.
    • (1996) J. Clin. Invest , vol.98 , pp. 167-176
    • Wolff, M.R.1    Buck, S.H.2    Stoker, S.W.3    Greaser, M.L.4    Mentzer, R.M.5
  • 16
    • 85047679474 scopus 로고
    • CAMP concentrations, cAMP dependentprotein kinase activity, and phospholamban in non-failing and failing myocardium
    • Bohm, M.; Reiger, B.; Schwinger, R. H.; Erdmann, E. cAMP concentrations, cAMP dependentprotein kinase activity, and phospholamban in non-failing and failing myocardium. Cardiovasc. Res. 1994, 28, 1713-1719.
    • (1994) Cardiovasc. Res , vol.28 , pp. 1713-1719
    • Bohm, M.1    Reiger, B.2    Schwinger, R.H.3    Erdmann, E.4
  • 17
    • 0027372328 scopus 로고
    • Phosphorylation of the L-type calciumchannel beta subunit is involved in beta-adrenergic signal transduction in canine myocardium
    • Haase, H.; Karczewski, P.; Beckert, R.; Krause, E. G. Phosphorylation of the L-type calciumchannel beta subunit is involved in beta-adrenergic signal transduction in canine myocardium.FEBS Lett. 1993, 335, 217-222.
    • (1993) FEBS Lett , vol.335 , pp. 217-222
    • Haase, H.1    Karczewski, P.2    Beckert, R.3    Krause, E.G.4
  • 18
    • 0030007989 scopus 로고    scopus 로고
    • A potential site of functionalmodulation by protein kinase A in the cardiac Ca2+ channel alpha 1C subunit
    • Perets, T.; Blumenstein, Y.; Shistik, E.; Lotan, I.; Dascal, N. A potential site of functionalmodulation by protein kinase A in the cardiac Ca2+ channel alpha 1C subunit. FEBS Lett. 1996,384, 189-192.
    • (1996) FEBS Lett , vol.384 , pp. 189-192
    • Perets, T.1    Blumenstein, Y.2    Shistik, E.3    Lotan, I.4    Dascal, N.5
  • 20
    • 0028321553 scopus 로고
    • The cAMP response element binding protein is expressed andphosphorylated in cardiac myocytes
    • Goldspink, P. H.; Russell, B. The cAMP response element binding protein is expressed andphosphorylated in cardiac myocytes. Circ. Res. 1994, 74, 1042-1049.
    • (1994) Circ. Res , vol.74 , pp. 1042-1049
    • Goldspink, P.H.1    Russell, B.2
  • 21
    • 33748446380 scopus 로고    scopus 로고
    • Roles of cardiac ryanodine receptor in heart failure andsudden cardiac death
    • Phrommintikul, A.; Chattipakorn, N. Roles of cardiac ryanodine receptor in heart failure andsudden cardiac death. Int. J. Cardiol. 2006, 112, 142-152.
    • (2006) Int. J. Cardiol , vol.112 , pp. 142-152
    • Phrommintikul, A.1    Chattipakorn, N.2
  • 22
    • 0028027011 scopus 로고
    • Protein kinase inhibitors reduce SR Ca transport inpermeabilized cardiac myocytes
    • Mattiazzi, A.; Hove-Madsen, L.; Bers, D. M. Protein kinase inhibitors reduce SR Ca transport inpermeabilized cardiac myocytes. Am. J. Physiol. Heart Circ. Physiol. 1994, 267, H812-H820.
    • (1994) Am. J. Physiol. Heart Circ. Physiol , vol.267
    • Mattiazzi, A.1    Hove-Madsen, L.2    Bers, D.M.3
  • 23
    • 0037869252 scopus 로고    scopus 로고
    • Trapidil protectsischemic hearts from reperfusion injury by stimulating PKAII activity
    • Sichelschmidt, O. J.; Hahnefeld, C.; Hohlfeld, T.; Herberg, F. W.; Schror, K. Trapidil protectsischemic hearts from reperfusion injury by stimulating PKAII activity. Cardiovasc. Res. 2003,58, 602-610.
    • (2003) Cardiovasc. Res , vol.58 , pp. 602-610
    • Sichelschmidt, O.J.1    Hahnefeld, C.2    Hohlfeld, T.3    Herberg, F.W.4    Schror, K.5
  • 24
    • 60549086753 scopus 로고    scopus 로고
    • Alterations of phospholamban function can exhibitcardiotoxic effects independent of excessive sarcoplasmic reticulum Ca2+-ATPase inhibition
    • Schmitt, J. P.; Ahmad, F.; Lorenz, K.; Hein, L.; Schulz, S.; Asahi, M.; Maclennan, D. H.;Seidman, C. E.Seidman, J. G.; Lohse, M. J. Alterations of phospholamban function can exhibitcardiotoxic effects independent of excessive sarcoplasmic reticulum Ca2+-ATPase inhibition.Circulation 2009, 119, 436-444.
    • (2009) Circulation , vol.119 , pp. 436-444
    • Schmitt, J.P.1    Ahmad, F.2    Lorenz, K.3    Hein, L.4    Schulz, S.5    Asahi, M.6    Maclennan, D.H.7    Seidman, C.E.8    Seidman, J.G.9    Lohse M., J.10
  • 25
    • 33646771721 scopus 로고    scopus 로고
    • Ser-2030, but not Ser-2808, is the major phosphorylation site incardiac ryanodine receptors responding to protein kinase A activation upon beta-adrenergicstimulation in normal and failing hearts
    • Xiao, B.; Zhong, G.; Obayashi, M.; Yang, D.; Chen, K.; Walsh, M. P.; Shimoni, Y.; Cheng, H.;Ter Keurs, H.; Chen, S. R. Ser-2030, but not Ser-2808, is the major phosphorylation site incardiac ryanodine receptors responding to protein kinase A activation upon beta-adrenergicstimulation in normal and failing hearts. Biochem. J. 2006, 396, 7-16.
    • (2006) Biochem. J , vol.396 , pp. 7-16
    • Xiao, B.1    Zhong, G.2    Obayashi, M.3    Yang, D.4    Chen, K.5    Walsh, M.P.6    Shimoni, Y.7    Cheng, H.8    Chen, S.R.9
  • 26
    • 70349973428 scopus 로고    scopus 로고
    • Protein kinase A-dependent phosphorylation of ryanodine receptors increasesCa2+ leak in mouse heart
    • Morimoto, S. J. O. U.; Kawai, M.; Hoshina, T.; Kusakari, Y.; Komukai, K.; Sasaki, H.; Hongo, K.; Kurihara, S. Protein kinase A-dependent phosphorylation of ryanodine receptors increasesCa2+ leak in mouse heart. Biochem. Biophys. Res. Commun. 2009, 390, 87-92
    • (2009) Biochem. Biophys. Res. Commun , vol.390 , pp. 87-92
    • Kawai, M.1    Hoshina, T.2    Kusakari, Y.3    Komukai, K.4    Sasaki, H.5
  • 27
    • 1542613385 scopus 로고    scopus 로고
    • Cellular basis of triggered arrhythmias in heart failure
    • Pogwizd, S. M.; Bers, D. M. Cellular basis of triggered arrhythmias in heart failure. Trends Cardiovasc. Med. 2004, 14, 61-66.
    • (2004) Trends Cardiovasc. Med , vol.14 , pp. 61-66
    • Pogwizd, S.M.1    Bers, D.M.2
  • 28
    • 0034724376 scopus 로고    scopus 로고
    • Regulation of PKA binding to AKAPs in the heart:Alterations in human heart failure
    • Zakhary, D. R.; Moravec, C. S.; Bond, M. Regulation of PKA binding to AKAPs in the heart:alterations in human heart failure. Circulation 2000, 101, 1459-1464.
    • (2000) Circulation , vol.101 , pp. 1459-1464
    • Zakhary, D.R.1    Moravec, C.S.2    Bond, M.3
  • 29
    • 0033514391 scopus 로고    scopus 로고
    • Protein kinase A (PKA)-dependenttroponin-I phosphorylation and PKA regulatory subunits are decreased in human dilatedcardiomyopathy
    • Zakhary, D. R.; Moravec, C. S.; Stewart, R. W.; Bond, M. Protein kinase A (PKA)-dependenttroponin-I phosphorylation and PKA regulatory subunits are decreased in human dilatedcardiomyopathy. Circulation 1999, 99, 505-510.
    • (1999) Circulation , vol.99 , pp. 505-510
    • Zakhary, D.R.1    Moravec, C.S.2    Stewart, R.W.3    Bond, M.4
  • 31
    • 34548211785 scopus 로고    scopus 로고
    • Effects of PKA phosphorylation ofcardiac troponin I and strong crossbridge on conformational transitions of the N-domain ofcardiac troponin C in regulated thin filaments
    • Dong, W. J.; Jayasundar, J. J.; An, J.; Xing, J.; Cheung, H. C. Effects of PKA phosphorylation ofcardiac troponin I and strong crossbridge on conformational transitions of the N-domain ofcardiac troponin C in regulated thin filaments. Biochemistry 2007, 46, 9752-9761.
    • (2007) Biochemistry , vol.46 , pp. 9752-9761
    • Dong, W.J.1    Jayasundar, J.J.2    An, J.3    Xing, J.4    Cheung, H.C.5
  • 32
    • 55449118232 scopus 로고    scopus 로고
    • Acceleration ofcrossbridge kinetics by protein kinase A phosphorylation of cardiac myosin binding protein Cmodulates cardiac function
    • Tong, C. W.; Stelzer, J. E.; Greaser, M. L.; Powers, P. A.; Moss, R. L. Acceleration ofcrossbridge kinetics by protein kinase A phosphorylation of cardiac myosin binding protein Cmodulates cardiac function. Circ. Res. 2008, 103, 974-982.
    • (2008) Circ. Res , vol.103 , pp. 974-982
    • Tong, C.W.1    Stelzer, J.E.2    Greaser, M.L.3    Powers, P.A.4    Moss, R.L.5
  • 33
    • 33747436524 scopus 로고    scopus 로고
    • Dobrev, D.Molecular determinants of altered Ca2+ handling in human chronic atrial fibrillation
    • El-Armouche, A.; Boknik, P.; Eschenhagen, T.; Carrier, L.; Knaut, M.; Ravens, U.; Dobrev, D.Molecular determinants of altered Ca2+ handling in human chronic atrial fibrillation. Circulation2006, 114, 670-680.
    • (2006) Circulation , vol.114 , pp. 670-680
    • El-Armouche, A.1    Boknik, P.2    Eschenhagen, T.3    Carrier, L.4    Knaut, M.5    Ravens, U.6
  • 36
    • 0017176627 scopus 로고
    • Phosphorylation of the inhibitory subunit of troponin and its effect onthe calcium dependence of cardiac myofibril adenosine triphosphatase
    • Ray, K. P.; England, P. J. Phosphorylation of the inhibitory subunit of troponin and its effect onthe calcium dependence of cardiac myofibril adenosine triphosphatase. FEBS Lett. 1976, 70,11-16.
    • (1976) FEBS Lett , vol.70 , pp. 11-16
    • Ray, K.P.1    England, P.J.2
  • 37
    • 0018625835 scopus 로고
    • The calcium binding properties of phosphorylated andunphosphorylated cardiac and skeletal myosins
    • Holroyde, M. J.; Potter, J. D.; Solaro, R. J. The calcium binding properties of phosphorylated andunphosphorylated cardiac and skeletal myosins. J. Biol. Chem. 1979, 254, 6478-6482.
    • (1979) J. Biol. Chem , vol.254 , pp. 6478-6482
    • Holroyde, M.J.1    Potter, J.D.2    Solaro, R.J.3
  • 38
    • 0035947749 scopus 로고    scopus 로고
    • Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cyclekinetics in mouse ventricular muscle
    • Kentish, J. C.; McCloskey, D. T.; Layland, J.; Palmer, S.; Leiden, J. M.; Martin, A. F.; Solaro, R.J. Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cyclekinetics in mouse ventricular muscle. Circ. Res. 2001, 88, 1059-1065.
    • (2001) Circ. Res , vol.88 , pp. 1059-1065
    • Kentish, J.C.1    McCloskey, D.T.2    Layland, J.3    Palmer, S.4    Leiden, J.M.5    Martin, A.F.6    Solaro, R.J.7
  • 39
    • 0035824911 scopus 로고    scopus 로고
    • Power output is increased after phosphorylation ofmyofibrillar proteins in rat skinned cardiac myocytes
    • Herron, T. J.; Korte, F. S.; McDonald, K. S. Power output is increased after phosphorylation ofmyofibrillar proteins in rat skinned cardiac myocytes. Circ. Res. 2001, 89, 1184-1190.
    • (2001) Circ. Res , vol.89 , pp. 1184-1190
    • Herron, T.J.1    Korte, F.S.2    McDonald, K.S.3
  • 40
    • 31044449218 scopus 로고    scopus 로고
    • Thin filament remodeling in failing myocardium
    • VanBuren, P.; Okada, Y. Thin filament remodeling in failing myocardium. Heart Fail. Rev.2005, 10, 199-209.
    • (2005) Heart Fail. Rev , vol.10 , pp. 199-209
    • Vanburen, P.1    Okada, Y.2
  • 41
    • 15744392510 scopus 로고    scopus 로고
    • H-89, a nonspecificinhibitor of protein kinase A, promotes post-ischemic cardiac contractile recovery andreduces infarct size
    • Makaula, S.; Lochner, A.; Genade, S.; Sack, M. N.; Awan, M. M.; Opie, L. H. H-89, a nonspecificinhibitor of protein kinase A, promotes post-ischemic cardiac contractile recovery andreduces infarct size. J. Cardiovasc. Pharmacol. 2005, 45, 341-347.
    • (2005) J. Cardiovasc. Pharmacol , vol.45 , pp. 341-347
    • Makaula, S.1    Lochner, A.2    Genade, S.3    Sack, M.N.4    Awan, M.M.5    Opie, L.H.6
  • 42
    • 0029779964 scopus 로고    scopus 로고
    • Activation isrequired for IL-1-induced nitric oxide production by cardiac myocytes
    • Oddis, C. V.; Simmons, R. L.; Hattler, B. G.; Finkel, M. S. Protein kinase A activation isrequired for IL-1-induced nitric oxide production by cardiac myocytes. Am. J. Physiol. Cell.Physiol. 1996, 271, C429-434.
    • (1996) Am. J. Physiol. Cell.Physiol , vol.271
    • Oddis, C.V.1    Simmons, R.L.2    Hattler, B.G.3    Finkel, M.S.4
  • 43
    • 36148964038 scopus 로고    scopus 로고
    • The effect of adrenomedullin on the L-type calciumcurrent in myocytes from septic shock rats: Signaling pathway
    • Zhang, X. H.; Li, G. R.; Bourreau, J. P. The effect of adrenomedullin on the L-type calciumcurrent in myocytes from septic shock rats: signaling pathway. Am. J. Physiol. Heart Circ.Physiol. 2007, 293, H2888-2893.
    • (2007) Am. J. Physiol. Heart Circ.Physiol , vol.293
    • Zhang, X.H.1    Li, G.R.2    Bourreau, J.P.3
  • 45
    • 0028063424 scopus 로고
    • Plasma levels of adrenomedullin, a newly identified hypotensive peptide, inpatients with hypertension and renal failure
    • Ishimitsu, T.; Nishikimi, T.; Saito, Y.; Kitamura, K.; Eto, T.; Kangawa, K.; Matsuo, H.; Omae, T.; Matsuoka, H. Plasma levels of adrenomedullin, a newly identified hypotensive peptide, inpatients with hypertension and renal failure. J. Clin. Invest. 1994, 94, 2158-2161.
    • (1994) J. Clin. Invest , vol.94 , pp. 2158-2161
    • Ishimitsu, T.1    Nishikimi, T.2    Saito, Y.3    Kitamura, K.4    Eto, T.5    Kangawa, K.6    Matsuo, H.7
  • 47
    • 0029081173 scopus 로고
    • Elevation of circulating andventricular adrenomedullin in human congestive heart failure
    • Jougasaki, M.; Wei, C. M.; McKinley, L. J.; Burnett, J. C., Jr. Elevation of circulating andventricular adrenomedullin in human congestive heart failure. Circulation 1995, 92, 286-289.
    • (1995) Circulation , vol.92 , pp. 286-289
    • Jougasaki, M.1    Wei, C.M.2    McKinley, L.J.3    Burnett Jr., J.C.4
  • 48
    • 0031972798 scopus 로고    scopus 로고
    • Plasma levels of adrenomedullin in patients with acute myocardialinfarction
    • Yoshitomi, Y.; Nishikimi, T.; Kojima, S.; Kuramochi, M.; Takishita, S.; Matsuoka, H.; Miyata, A.; Matsuo, H.; Kangawa, K. Plasma levels of adrenomedullin in patients with acute myocardialinfarction. Clin. Sci. 1998, 94, 135-139.
    • (1998) Clin. Sci , vol.94 , pp. 135-139
    • Yoshitomi, Y.1    Nishikimi, T.2    Kojima, S.3    Kuramochi, M.4    Takishita, S.5    Matsuoka, H.6
  • 49
    • 38849149695 scopus 로고    scopus 로고
    • Infarct size limitation by adrenomedullin:Protein kinase A but not PI3-kinase is linked to mitochondrial KCa channels
    • Nishida, H.; Sato, T.; Miyazaki, M.; Nakaya, H. Infarct size limitation by adrenomedullin:Protein kinase A but not PI3-kinase is linked to mitochondrial KCa channels. Cardiovasc. Res. 2008, 77, 398-405.
    • (2008) Cardiovasc. Res , vol.77 , pp. 398-405
    • Nishida, H.1    Sato, T.2    Miyazaki, M.3    Nakaya, H.4
  • 50
    • 0027495714 scopus 로고
    • Nitric oxide regulatescardiac Ca2+ current. Involvement of cGMP-inhibited and cGMP-stimulated phosphodiesterasesthrough guanylyl cyclase activation
    • Mery, P. F.; Pavoine, C.; Belhassen, L.; Pecker, F.; Fischmeister, R. Nitric oxide regulatescardiac Ca2+ current. Involvement of cGMP-inhibited and cGMP-stimulated phosphodiesterasesthrough guanylyl cyclase activation. J. Biol. Chem. 1993, 268, 26286-26295.
    • (1993) J. Biol. Chem , vol.268 , pp. 26286-26295
    • Mery, P.F.1    Pavoine, C.2    Belhassen, L.3    Pecker, F.4    Fischmeister, R.5
  • 51
    • 0028293196 scopus 로고
    • 8-bromo-cGMP reduces themyofilament response to Ca2+ in intact cardiac myocytes
    • Shah, A. M.; Spurgeon, H. A.; Sollott, S. J.; Talo, A.; Lakatta, E. G. 8-bromo-cGMP reduces themyofilament response to Ca2+ in intact cardiac myocytes. Circ. Res. 1994, 74, 970-978.
    • (1994) Circ. Res , vol.74 , pp. 970-978
    • Shah, A.M.1    Spurgeon, H.A.2    Sollott, S.J.3    Talo, A.4    Lakatta, E.G.5
  • 52
    • 0028896285 scopus 로고
    • Nitric oxide donor SIN-1 inhibits mammalian cardiac calciumcurrent through cGMP-dependent protein kinase
    • Wahler, G. M.; Dollinger, S. J. Nitric oxide donor SIN-1 inhibits mammalian cardiac calciumcurrent through cGMP-dependent protein kinase. Am. J. Physiol. Cell. Physiol. 1995, 268,45-54.
    • (1995) Am. J. Physiol. Cell. Physiol , vol.268 , pp. 45-54
    • Wahler, G.M.1    Dollinger, S.J.2
  • 53
    • 0001377920 scopus 로고
    • Myocardial metabolism in congestive heart failure
    • Olson, R. E. Myocardial metabolism in congestive heart failure. J. Chronic Dis. 1959, 9,442-464.
    • (1959) J. Chronic Dis , vol.9 , pp. 442-464
    • Olson, R.E.1
  • 54
    • 0025770664 scopus 로고
    • Pathological hypertrophy and cardiac interstitium. Fibrosis and reninangiotensin-aldosterone system
    • Weber, K. T.; Brilla, C. G. Pathological hypertrophy and cardiac interstitium. Fibrosis and reninangiotensin-aldosterone system. Circulation 1991, 83, 1849-1865.
    • (1991) Circulation , vol.83 , pp. 1849-1865
    • Weber, K.T.1    Brilla, C.G.2
  • 55
    • 30344454375 scopus 로고    scopus 로고
    • Role of tumournecrosis factor-alpha and other cytokines in ischemia-reperfusion-induced injury in the heart
    • Saini, H. K.; Xu, Y. J.; Zhang, M.; Liu, P. P.; Kirshenbaum, L. A.; Dhalla, N. S. Role of tumournecrosis factor-alpha and other cytokines in ischemia-reperfusion-induced injury in the heart. Exp. Clin. Cardiol. 2005, 10, 213-222.
    • (2005) Exp. Clin. Cardiol , vol.10 , pp. 213-222
    • Saini, H.K.1    Xu, Y.J.2    Zhang, M.3    Liu, P.P.4    Kirshenbaum, L.A.5    Dhalla, N.S.6
  • 56
    • 0018656917 scopus 로고
    • Effects of experimental right ventricularhypertrophy on myocardial blood flow in conscious dogs
    • Murray, P. A.; Baig, H.; Fishbein, M. C.; Vatner, S. F. Effects of experimental right ventricularhypertrophy on myocardial blood flow in conscious dogs. J. Clin. Invest. 1979, 64, 421-427.
    • (1979) J. Clin. Invest , vol.64 , pp. 421-427
    • Murray, P.A.1    Baig, H.2    Fishbein, M.C.3    Vatner, S.F.4
  • 57
    • 38649084713 scopus 로고    scopus 로고
    • Insulin inhibits betaadrenergicaction in ischemic/reperfused heart: A novel mechanism of insulin incardioprotection
    • Yu, Q. J.; Si, R.; Zhou, N.; Zhang, H. F.; Guo, W. Y.; Wang, H. C.; Gao, F. Insulin inhibits betaadrenergicaction in ischemic/reperfused heart: A novel mechanism of insulin incardioprotection. Apoptosis 2008, 13, 305-317.
    • (2008) Apoptosis , vol.13 , pp. 305-317
    • Yu, Q.J.1    Si, R.2    Zhou, N.3    Zhang, H.F.4    Guo, W.Y.5    Wang, H.C.6    Gao, F.7
  • 62
    • 0030031983 scopus 로고    scopus 로고
    • C.;Olivetti, G.; Anversa, P. Apoptotic and necrotic myocyte cell deaths are independentcontributing variables of infarct size in rats
    • Kajstura, J.; Cheng, W.; Reiss, K.; Clark, W. A.; Sonnenblick, E. H.; Krajewski, S.; Reed, J. C.;Olivetti, G.; Anversa, P. Apoptotic and necrotic myocyte cell deaths are independentcontributing variables of infarct size in rats. Lab. Invest. 1996, 74, 86-107.
    • (1996) Lab. Invest , vol.74 , pp. 86-107
    • Kajstura, J.1    Cheng, W.2    Reiss, K.3    Clark, W.A.4    Sonnenblick, E.H.5    Krajewski, S.6    Reed, J.7
  • 66
    • 39849104590 scopus 로고    scopus 로고
    • PDE4 inhibitor, roflumilast protects cardiomyocytes against NO-induced apoptosis via activation of PKA andEpac dual pathways
    • Kwak, H. J.; Park, K. M.; Choi, H. E.; Chung, K. S.; Lim, H. J.; Park, H. Y. PDE4 inhibitor, roflumilast protects cardiomyocytes against NO-induced apoptosis via activation of PKA andEpac dual pathways. Cell. Signal. 2008, 20, 803-814.
    • (2008) SCell. ignal , vol.20 , pp. 803-814
    • Kwak, H.J.1    Park, K.M.2    Choi, H.E.3    Chung, K.S.4    Lim, H.J.5    Park, H.Y.6
  • 67
    • 19444385802 scopus 로고    scopus 로고
    • 3-kinase, protein kinase C, and protein kinase A areinvolved in the trigger phase of beta1-adrenergic preconditioning
    • Robinet, A.; Hoizey, G.; Millart, H. PI 3-kinase, protein kinase C, and protein kinase A areinvolved in the trigger phase of beta1-adrenergic preconditioning. Cardiovasc. Res. 2005, 66,530-542.
    • (2005) Cardiovasc. Res , vol.66 , pp. 530-542
    • Robinet, A.1    Hoizey, G.2    Millart, H.3
  • 68
    • 2942578973 scopus 로고    scopus 로고
    • Cyclic adenosine monophosphate inhibits nitric oxideinducedapoptosis of cardiac muscle cells in a c-Jun N-terminal kinase-dependent manner
    • Chae, H. J.; Chae, S. W.; Kim, H. R. Cyclic adenosine monophosphate inhibits nitric oxideinducedapoptosis of cardiac muscle cells in a c-Jun N-terminal kinase-dependent manner. Immunopharmacol. Immunotoxicol. 2004, 26, 249-263.
    • (2004) Immunopharmacol. Immunotoxicol , vol.26 , pp. 249-263
    • Chae, H.J.1    Chae, S.W.2    Kim, H.R.3
  • 69
    • 33644867986 scopus 로고    scopus 로고
    • Protein kinase A-mediated phosphorylation modulates cytochrome c oxidase function andaugments hypoxia and myocardial ischemia-related injury
    • Prabu, S. K.; Anandatheerthavarada, H. K.; Raza, H.; Srinivasan, S.; Spear, J. F.; Avadhani, N.G. Protein kinase A-mediated phosphorylation modulates cytochrome c oxidase function andaugments hypoxia and myocardial ischemia-related injury. J. Biol. Chem. 2006, 281, 2061-2070.
    • (2006) J. Biol. Chem , vol.281 , pp. 2061-2070
    • Prabu, S.K.1    Anandatheerthavarada, H.K.2    Raza, H.3    Srinivasan, S.4    Spear, J.F.5    Avadhani, N.G.6
  • 70
    • 0345303850 scopus 로고    scopus 로고
    • Organization and evolution of multifunctionalCa(2+)/CaM-dependent protein kinase genes
    • Tombes, R. M.; Faison, M. O.; Turbeville, J. M. Organization and evolution of multifunctionalCa(2+)/CaM-dependent protein kinase genes. Gene 2003, 322, 17-31.
    • (2003) Gene , vol.322 , pp. 17-31
    • Tombes, R.M.1    Faison, M.O.2    Turbeville, J.M.3
  • 71
    • 0035997377 scopus 로고    scopus 로고
    • Neuronal Ca2+/calmodulin-dependent protein kinase II: The role ofstructure and autoregulation in cellular function
    • Hudmon, A.; Schulman, H. Neuronal Ca2+/calmodulin-dependent protein kinase II: The role ofstructure and autoregulation in cellular function. Annu. Rev. Biochem. 2002, 71, 473-510.
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 473-510
    • Hudmon, A.1    Schulman, H.2
  • 72
    • 0037097022 scopus 로고    scopus 로고
    • Structure-function of the multifunctional Ca2+/calmodulin-dependentprotein kinase II
    • Hudmon, A.; Schulman, H. Structure-function of the multifunctional Ca2+/calmodulin-dependentprotein kinase II. Biochem. J. 2002, 364, 593-611
    • (2002) Biochem. J , vol.364 , pp. 593-611
    • Hudmon, A.1    Schulman, H.2
  • 73
    • 0032498172 scopus 로고    scopus 로고
    • Sensitivity of CaM kinase II to the frequency of Ca2+ oscillations
    • De Koninck, P.; Schulman, H. Sensitivity of CaM kinase II to the frequency of Ca2+ oscillations.Science 1998, 279, 227-230.
    • (1998) Science , vol.279 , pp. 227-230
    • de Koninck, P.1    Schulman, H.2
  • 74
    • 26944451290 scopus 로고    scopus 로고
    • CaMK-II oligomerization potential determined using CFP/YFPFRET
    • Lantsman, K.; Tombes, R. M. CaMK-II oligomerization potential determined using CFP/YFPFRET. Biochim. Biophys. Acta 2005, 1746, 45-54.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 45-54
    • Lantsman, K.1    Tombes, R.M.2
  • 75
    • 0035028435 scopus 로고    scopus 로고
    • Ca(2+)/CaM-dependent kinases: From activation to function
    • Hook, S. S.; Means, A. R. Ca(2+)/CaM-dependent kinases: From activation to function. Annu.Rev. Pharmacol. Toxicol. 2001, 41, 471-505.
    • (2001) Annu. Rev. Pharmacol. Toxicol , vol.41 , pp. 471-505
    • Hook, S.S.1    Means, A.R.2
  • 76
    • 0033781028 scopus 로고    scopus 로고
    • Calmodulin kinase determinescalcium-dependent facilitation of L-type calcium channels
    • Dzhura, I.; Wu, Y.; Colbran, R. J.; Balser, J. R.; Anderson, M. E. Calmodulin kinase determinescalcium-dependent facilitation of L-type calcium channels. Nat. Cell. Biol. 2000, 2, 173-177.
    • (2000) Nat. Cell. Biol , vol.2 , pp. 173-177
    • Dzhura, I.1    Wu, Y.2    Colbran, R.J.3    Balser, J.R.4    Anderson, M.E.5
  • 77
    • 0036702526 scopus 로고    scopus 로고
    • Calcium, calmodulin, and calcium-calmodulin kinase II: Heartbeat toheartbeat and beyond
    • Maier, L. S.; Bers, D. M. Calcium, calmodulin, and calcium-calmodulin kinase II: Heartbeat toheartbeat and beyond. J. Mol. Cell. Cardiol. 2002, 34, 919-939.
    • (2002) J. Mol. Cell. Cardiol , vol.34 , pp. 919-939
    • Maier, L.S.1    Bers, D.M.2
  • 78
    • 0028918056 scopus 로고
    • Phosphorylation modulates thefunction of the calcium release channel of sarcoplasmic reticulum from cardiac muscle
    • Hain, J.; Onoue, H.; Mayrleitner, M.; Fleischer, S.; Schindler, H. Phosphorylation modulates thefunction of the calcium release channel of sarcoplasmic reticulum from cardiac muscle. J. Biol.Chem. 1995, 270, 2074-2081.
    • (1995) J. Biol.Chem , vol.270 , pp. 2074-2081
    • Hain, J.1    Onoue, H.2    Mayrleitner, M.3    Fleischer, S.4    Schindler, H.5
  • 79
    • 0027943988 scopus 로고
    • Differential activation of CREB byCa2+/calmodulin-dependent protein kinases type II and type IV involves phosphorylation of a sitethat negatively regulates activity
    • Sun, P.; Enslen, H.; Myung, P. S.; Maurer, R. A., Differential activation of CREB byCa2+/calmodulin-dependent protein kinases type II and type IV involves phosphorylation of a sitethat negatively regulates activity. Genes Dev. 1994, 8, 2527-2539.
    • (1994) Genes Dev , vol.8 , pp. 2527-2539
    • Sun, P.1    Enslen, H.2    Myung, P.S.3    Maurer, R.A.4
  • 80
    • 0034640259 scopus 로고    scopus 로고
    • Three-dimensional reconstructionsof calcium/calmodulin-dependent (CaM) kinase II-alpha and truncated CaM kinase II-alphareveal a unique organization for its structural core and functional domains
    • Kolodziej, S. J.; Hudmon, A.; Waxham, M. N.; Stoops, J. K. Three-dimensional reconstructionsof calcium/calmodulin-dependent (CaM) kinase II-alpha and truncated CaM kinase II-alphareveal a unique organization for its structural core and functional domains. J. Biol. Chem. 2000,275, 14354-14359.
    • (2000) J. Biol. Chem , vol.275 , pp. 14354-14359
    • Kolodziej, S.J.1    Hudmon, A.2    Waxham, M.N.3    Stoops, J.K.4
  • 81
    • 1842425022 scopus 로고    scopus 로고
    • Comparative analyses of the three-dimensional structures and enzymaticproperties of alpha, beta, gamma and delta isoforms of Ca2+-calmodulin-dependent protein kinaseII
    • Gaertner, T. R.; Kolodziej, S. J.; Wang, D.; Kobayashi, R.; Koomen, J. M.; Stoops, J. K.;Waxham, M. N. Comparative analyses of the three-dimensional structures and enzymaticproperties of alpha, beta, gamma and delta isoforms of Ca2+-calmodulin-dependent protein kinaseII. J. Biol. Chem. 2004, 279, 12484-12494.
    • (2004) J. Biol. Chem , vol.279 , pp. 12484-12494
    • Gaertner, T.R.1    Kolodziej, S.J.2    Wang, D.3    Kobayashi, R.4    Koomen, J.M.5    Stoops, J.K.6    Waxham, M.N.7
  • 82
    • 0026360042 scopus 로고
    • Structural features of Ca2+/calmodulindependentprotein kinase II revealed by electron microscopy
    • Kanaseki, T.; Ikeuchi, Y.; Sugiura, H.; Yamauchi, T. Structural features of Ca2+/calmodulindependentprotein kinase II revealed by electron microscopy. J. Cell. Biol. 1991, 115,1049-1060.
    • (1991) J. Cell. Biol , vol.115 , pp. 1049-1060
    • Kanaseki, T.1    Ikeuchi, Y.2    Sugiura, H.3    Yamauchi, T.4
  • 83
    • 73349084993 scopus 로고    scopus 로고
    • Mattiazzi, A.Angiotensin II-induced oxidative stress resets the Ca2+ dependence of Ca2+-calmodulin proteinkinase II and promotes a death pathway conserved across different species
    • Palomeque, J.; Rueda, O. V.; Sapia, L.; Valverde, C. A.; Salas, M.; Petroff, M. V.; Mattiazzi, A.Angiotensin II-induced oxidative stress resets the Ca2+ dependence of Ca2+-calmodulin proteinkinase II and promotes a death pathway conserved across different species. Circ. Res. 2009, 105,1204-1212.
    • (2009) Circ. Res , vol.105 , pp. 1204-1212
    • Palomeque, J.1    Rueda, O.V.2    Sapia, L.3    Valverde, C.A.4    Salas, M.5    Petroff, M.V.6
  • 84
    • 59649127713 scopus 로고    scopus 로고
    • Oxidative-stress-inducedafterdepolarizations and calmodulin kinase II signaling
    • Xie, L. H.; Chen, F.; Karagueuzian, H. S.; Weiss, J. N. Oxidative-stress-inducedafterdepolarizations and calmodulin kinase II signaling. Circ. Res. 2009, 104, 79-86.
    • (2009) Circ. Res , vol.104 , pp. 79-86
    • Xie, L.H.1    Chen, F.2    Karagueuzian, H.S.3    Weiss, J.N.4
  • 85
    • 33846858884 scopus 로고    scopus 로고
    • Role of Ca2+/calmodulin-dependent protein kinase (CaMK) inexcitation-contraction coupling in the heart
    • Maier, L. S.; Bers, D. M. Role of Ca2+/calmodulin-dependent protein kinase (CaMK) inexcitation-contraction coupling in the heart. Cardiovasc. Res. 2007, 73, 631-640.
    • (2007) Cardiovasc. Res , vol.73 , pp. 631-640
    • Maier, L.S.1    Bers, D.M.2
  • 88
    • 33846874155 scopus 로고    scopus 로고
    • E.;Kuhn, M. CaMKII-mediated increased lusitropic responses to beta-adrenoreceptor stimulation inANP-receptor deficient mice
    • Yurukova, S.; Kilic, A.; Volker, K.; Leineweber, K.; Dybkova, N.; Maier, L. S.; Brodde, O. E.;Kuhn, M. CaMKII-mediated increased lusitropic responses to beta-adrenoreceptor stimulation inANP-receptor deficient mice. Cardiovasc. Res. 2007, 73, 678-688.
    • (2007) Cardiovasc. Res , vol.73 , pp. 678-688
    • Yurukova, S.1    Kilic, A.2    Volker, K.3    Leineweber, K.4    Dybkova, N.5    Maier, L.S.6    Brodde, O.7
  • 92
    • 0037315106 scopus 로고    scopus 로고
    • Pressure overload selectively upregulatesCa2+/calmodulin-dependent protein kinase II in vivo
    • Colomer, J. M.; Mao, L.; Rockman, H. A.; Means, A. R. Pressure overload selectively upregulatesCa2+/calmodulin-dependent protein kinase II in vivo. Mol. Endocrinol. 2003, 17,183-192.
    • (2003) Mol. Endocrinol , vol.17 , pp. 183-192
    • Colomer, J.M.1    Mao, L.2    Rockman, H.A.3    Means, A.R.4
  • 93
    • 74049097964 scopus 로고    scopus 로고
    • Cardioprotectionby CaMKII-deltaB is mediated by phosphorylation of heat shock factor 1 and subsequentexpression of inducible heat shock protein 70
    • Peng, W.; Zhang, Y.; Zheng, M.; Cheng, H.; Zhu, W.; Cao, C. M.; Xiao, R. P. Cardioprotectionby CaMKII-deltaB is mediated by phosphorylation of heat shock factor 1 and subsequentexpression of inducible heat shock protein 70. Circ. Res. 2010, 106, 102-110.
    • (2010) Circ. Res , vol.106 , pp. 102-110
    • Peng, W.1    Zhang, Y.2    Zheng, M.3    Cheng, H.4    Zhu, W.5    Cao, C.M.6    Xiao, R.P.7
  • 94
    • 0028085454 scopus 로고
    • Alternative splicing introduces a nuclearlocalization signal that targets multifunctional CaM kinase to the nucleus
    • Srinivasan, M.; Edman, C. F.; Schulman, H. Alternative splicing introduces a nuclearlocalization signal that targets multifunctional CaM kinase to the nucleus. J. Cell. Biol. 1994,126, 839-852.
    • (1994) J. Cell. Biol , vol.126 , pp. 839-852
    • Srinivasan, M.1    Edman, C.F.2    Schulman, H.3
  • 95
    • 33644865926 scopus 로고    scopus 로고
    • Increased sarcoplasmic reticulum calcium leak butunaltered contractility by acute CaMKII overexpression in isolated rabbit cardiac myocytes
    • Kohlhaas, M.; Zhang, T.; Seidler, T.; Zibrova, D.; Dybkova, N.; Steen, A.; Wagner, S.; Chen, L.;Brown, J. H.; Bers, D. M.; Maier, L. S. Increased sarcoplasmic reticulum calcium leak butunaltered contractility by acute CaMKII overexpression in isolated rabbit cardiac myocytes. Circ. Res. 2006, 98, 235-244.
    • (2006) Circ. Res , vol.98 , pp. 235-244
    • Kohlhaas, M.1    Zhang, T.2    Seidler, T.3    Zibrova, D.4    Dybkova, N.5    Steen, A.6    Wagner, S.7    Chen, L.8    Brown, J.H.9    Bers, D.M.10    Maier, L.S.11
  • 98
    • 16344367572 scopus 로고    scopus 로고
    • Morano, I.Regulation of the human atrial myosin light chain 1 promoter by Ca2+-calmodulin-dependentsignaling pathways
    • Woischwill, C.; Karczewski, P.; Bartsch, H.; Luther, H. P.; Kott, M.; Haase, H.; Morano, I.Regulation of the human atrial myosin light chain 1 promoter by Ca2+-calmodulin-dependentsignaling pathways. FASEB J. 2005, 19, 503-511.
    • (2005) FASEB J , vol.19 , pp. 503-511
    • Woischwill, C.1    Karczewski, P.2    Bartsch, H.3    Luther, H.P.4    Kott, M.5    Haase, H.6
  • 99
    • 14244258686 scopus 로고    scopus 로고
    • Signal transductionmechanisms involved in cardiac preconditioning: Role of Ras-GTPase, Ca2+/calmodulindependentprotein kinase II and epidermal growth factor receptor
    • Benter, I. F.; Juggi, J. S.; Khan, I.; Yousif, M. H.; Canatan, H.; Akhtar, S. Signal transductionmechanisms involved in cardiac preconditioning: Role of Ras-GTPase, Ca2+/calmodulindependentprotein kinase II and epidermal growth factor receptor. Mol. Cell. Biochem. 2005,268, 175-183.
    • (2005) Mol. Cell. Biochem , vol.268 , pp. 175-183
    • Benter, I.F.1    Juggi, J.S.2    Khan, I.3    Yousif, M.H.4    Canatan, H.5    Akhtar, S.6
  • 101
    • 0034677802 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum Ca(2+)/Calmodulin-dependent protein kinase is altered in heart failure
    • Netticadan, T.; Temsah, R. M.; Kawabata, K.; Dhalla, N. S. Sarcoplasmic reticulum Ca(2+)/Calmodulin-dependent protein kinase is altered in heart failure. Circ. Res. 2000, 86, 596-605.
    • (2000) Circ. Res , vol.86 , pp. 596-605
    • Netticadan, T.1    Temsah, R.M.2    Kawabata, K.3    Dhalla, N.S.4
  • 103
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • Nishizuka, Y. Studies and perspectives of protein kinase C. Science 1986, 233, 305-312.
    • (1986) Science , vol.233 , pp. 305-312
    • Nishizuka, Y.1
  • 104
    • 0027522647 scopus 로고
    • Characterization of protein kinase C isotypeexpression in adult rat heart. Protein kinase C-epsilon is a major isotype present, and it isactivated by phorbol esters, epinephrine, and endothelin
    • Bogoyevitch, M. A.; Parker, P. J.; Sugden, P. H. Characterization of protein kinase C isotypeexpression in adult rat heart. Protein kinase C-epsilon is a major isotype present, and it isactivated by phorbol esters, epinephrine, and endothelin. Circ. Res. 1993, 72, 757-767.
    • (1993) Circ. Res , vol.72 , pp. 757-767
    • Bogoyevitch, M.A.1    Parker, P.J.2    Sugden, P.H.3
  • 106
    • 0020698115 scopus 로고
    • Phorbol esters increase the amount of Ca2+, phospholipiddependentprotein kinase associated with plasma membrane
    • Kraft, A. S.; Anderson, W. B. Phorbol esters increase the amount of Ca2+, phospholipiddependentprotein kinase associated with plasma membrane. Nature 1983, 301, 621-623.
    • (1983) Nature , vol.301 , pp. 621-623
    • Kraft, A.S.1    Anderson, W.B.2
  • 107
    • 0032104245 scopus 로고    scopus 로고
    • The extended protein kinase C Superfamily
    • Mellor, H.; Parker, P. J. The extended protein kinase C superfamily. Biochem. J. 1998, 332,281-292.
    • (1998) Biochem. J , vol.332 , pp. 281-292
    • Mellor, H.1    Parker, P.J.2
  • 108
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of proteinkinase C
    • Nishizuka, Y. Intracellular signaling by hydrolysis of phospholipids and activation of proteinkinase C. Science 1992, 258, 607-614.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 109
    • 0034644523 scopus 로고    scopus 로고
    • Cellular Signaling: Pivoting around PDK-1
    • Toker, A.; Newton, A. C. Cellular Signaling: Pivoting around PDK-1. Cell 2000, 103, 185-188.
    • (2000) Cell , vol.103 , pp. 185-188
    • Toker, A.1    Newton, A.C.2
  • 111
    • 0028030002 scopus 로고
    • Increased protein kinase C and isozyme redistribution in pressure-overloadcardiac hypertrophy in the rat
    • Gu, X.; Bishop, S. P. Increased protein kinase C and isozyme redistribution in pressure-overloadcardiac hypertrophy in the rat. Circ. Res. 1994, 75, 926-931.
    • (1994) Circ. Res , vol.75 , pp. 926-931
    • Gu, X.1    Bishop, S.P.2
  • 112
    • 4344589548 scopus 로고    scopus 로고
    • Regulation of proteinkinase C isozymes in volume overload cardiac hypertrophy
    • Braun, M. U.; LaRosee, P.; Simonis, G.; Borst, M. M.; Strasser, R. H. Regulation of proteinkinase C isozymes in volume overload cardiac hypertrophy. Mol. Cell. Biochem. 2004, 262,135-143.
    • (2004) Mol. Cell. Biochem , vol.262 , pp. 135-143
    • Braun, M.U.1    Larosee, P.2    Simonis, G.3    Borst, M.M.4    Strasser, R.H.5
  • 113
    • 0030720237 scopus 로고    scopus 로고
    • Left ventricular stretch stimulatesangiotensin II-mediated phosphatidylinositol hydrolysis and protein kinase C epsilon isoformtranslocation in adult guinea pig hearts
    • Paul, K.; Ball, N. A.; Dorn, G. W.; Walsh, R. A. Left ventricular stretch stimulatesangiotensin II-mediated phosphatidylinositol hydrolysis and protein kinase C epsilon isoformtranslocation in adult guinea pig hearts. Circ. Res. 1997, 81, 643-650.
    • (1997) Circ. Res , vol.81 , pp. 643-650
    • Paul, K.1    Ball, N.A.2    Dorn, G.W.3    Walsh, R.A.4
  • 114
    • 0026078960 scopus 로고
    • Cardiac hypertrophy. Mechanical, neural, and endocrinedependence
    • Morgan, H. E.; Baker, K. M. Cardiac hypertrophy. Mechanical, neural, and endocrinedependence. Circulation 1991, 83, 13-25.
    • (1991) Circulation , vol.83 , pp. 13-25
    • Morgan, H.E.1    Baker, K.M.2
  • 115
    • 0026008492 scopus 로고
    • Mechanical loading stimulates cell hypertrophy and specific gene expression in cultured ratcardiac myocytes. Possible role of protein kinase C activation
    • Komuro, I.; Katoh, Y.; Kaida, T.; Shibazaki, Y.; Kurabayashi, M.; Hoh, E.; Takaku, F.; Yazaki, Y. Mechanical loading stimulates cell hypertrophy and specific gene expression in cultured ratcardiac myocytes. Possible role of protein kinase C activation. J. Biol. Chem. 1991, 266,1265-1268.
    • (1991) J. Biol. Chem , vol.266 , pp. 1265-1268
    • Komuro, I.1    Katoh, Y.2    Kaida, T.3    Shibazaki, Y.4    Kurabayashi, M.5    Hoh, E.6    Takaku, F.7
  • 116
    • 0026709274 scopus 로고
    • Molecular characterization of thestretch-induced adaptation of cultured cardiac cells. An in vitro model of load-induced cardiachypertrophy
    • Sadoshima, J.; Jahn, L.; Takahashi, T.; Kulik, T. J.; Izumo, S. Molecular characterization of thestretch-induced adaptation of cultured cardiac cells. An in vitro model of load-induced cardiachypertrophy. J. Biol. Chem. 1992, 267, 10551-10560.
    • (1992) J. Biol. Chem , vol.267 , pp. 10551-10560
    • Sadoshima, J.1    Jahn, L.2    Takahashi, T.3    Kulik, T.J.4    Izumo, S.5
  • 117
    • 0037281147 scopus 로고    scopus 로고
    • Isoenzyme expression and autophosphorylation during the progression ofpressure overload-induced left ventricular hypertrophy
    • Bayer, A. L.; Heidkamp, M. C.; Patel, N.; Porter, M.; Engman, S.; Samarel, A. M. Alterations inprotein kinase C isoenzyme expression and autophosphorylation during the progression ofpressure overload-induced left ventricular hypertrophy. Mol. Cell. Biochem. 2003, 242, 145-152.
    • (2003) Mol. Cell. Biochem , vol.242 , pp. 145-152
    • Bayer, A.L.1    Heidkamp, M.C.2    Patel, N.3    Porter, M.4    Engman, S.5    Samarel, A.M.6
  • 118
    • 4344692221 scopus 로고    scopus 로고
    • Diabeticcardiomyocyte dysfunction and myocyte insulin resistance: Role of glucose-induced PKCactivity
    • Davidoff, A. J.; Davidson, M. B.; Carmody, M. W.; Davis, M. E.; Ren, J. Diabeticcardiomyocyte dysfunction and myocyte insulin resistance: Role of glucose-induced PKCactivity. Mol. Cell. Biochem. 2004, 262, 155-163.
    • (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
  • 119
    • 77955707550 scopus 로고    scopus 로고
    • Breviscapine ameliorates cardiacdysfunction and regulates the myocardial Ca(2+)-cycling proteins in streptozotocin-induceddiabetic rats
    • doi:10.1007/s00592-009-0164-x
    • Wang, M.; Zhang, W. B.; Zhu, J. H.; Fu, G. S.; Zhou, B. Q. Breviscapine ameliorates cardiacdysfunction and regulates the myocardial Ca(2+)-cycling proteins in streptozotocin-induceddiabetic rats. Acta Diabetol. 2009, doi:10.1007/s00592-009-0164-x.
    • (2009) Acta Diabetol
    • Wang, M.1    Zhang, W.B.2    Zhu, J.H.3    Fu, G.S.4    Zhou, B.Q.5
  • 120
    • 0037059549 scopus 로고    scopus 로고
    • Inhibition ofprotein kinase C-beta prevents impaired endothelium-dependent vasodilation caused byhyperglycemia in humans
    • Beckman, J. A.; Goldfine, A. B.; Gordon, M. B.; Garrett, L. A.; Creager, M. A. Inhibition ofprotein kinase C-beta prevents impaired endothelium-dependent vasodilation caused byhyperglycemia in humans. Circ. Res. 2002, 90, 107-111.
    • (2002) Circ. Res , vol.90 , pp. 107-111
    • Beckman, J.A.1    Goldfine, A.B.2    Gordon, M.B.3    Garrett, L.A.4    Creager, M.A.5
  • 123
    • 0036712066 scopus 로고    scopus 로고
    • Effects of the protein kinase C beta inhibitorLY333531 on neural and vascular function in rats with streptozotocin-induced diabetes
    • Cotter, M. A.; Jack, A. M.; Cameron, N. E. Effects of the protein kinase C beta inhibitorLY333531 on neural and vascular function in rats with streptozotocin-induced diabetes. Clin.Sci. 2002, 103, 311-321.
    • (2002) Clin. Sci , vol.103 , pp. 311-321
    • Cotter, M.A.1    Jack, A.M.2    Cameron, N.E.3
  • 124
    • 33747855849 scopus 로고    scopus 로고
    • Beta inhibitorLY333531 attenuates intercellular adhesion molecule-1 and monocyte chemotactic protein-1expression in the kidney in diabetic rats
    • Wu, Y.; Wu, G.; Qi, X.; Lin, H.; Qian, H.; Shen, J.; Lin, S. Protein kinase C beta inhibitorLY333531 attenuates intercellular adhesion molecule-1 and monocyte chemotactic protein-1expression in the kidney in diabetic rats. J. Pharmacol. Sci. 2006, 101, 335-343.
    • (2006) J. Pharmacol. Sci , vol.101 , pp. 335-343
    • Wu, Y.1    Wu, G.2    Qi, X.3    Lin, H.4    Qian, H.5    Shen, J.6    Lin, S.7
  • 125
    • 77953654365 scopus 로고    scopus 로고
    • Inhibition of protein kinase C-beta by ruboxistaurin preserves cardiac function andreduces extracellular matrix production in diabetic cardiomyopathy
    • Connelly, K. A.; Kelly, D. J.; Zhang, Y.; Prior, D. L.; Advani, A.; Cox, A. J.; Thai, K.; Krum, H.;Gilbert, R. E., Inhibition of protein kinase C-beta by ruboxistaurin preserves cardiac function andreduces extracellular matrix production in diabetic cardiomyopathy. Circ. Heart Fail. 2009, 2,129-137.
    • (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
  • 127
  • 128
    • 0038104862 scopus 로고    scopus 로고
    • Increased expression of protein kinase Cisoforms in heart failure due to myocardial infarction
    • Wang, J.; Liu, X.; Sentex, E.; Takeda, N.; Dhalla, N. S. Increased expression of protein kinase Cisoforms in heart failure due to myocardial infarction. Am. J. Physiol. Heart Circ. Physiol. 2003,284, 2277-2287.
    • (2003) Am. J. Physiol. Heart Circ. Physiol , vol.284 , pp. 2277-2287
    • Wang, J.1    Liu, X.2    Sentex, E.3    Takeda, N.4    Dhalla, N.S.5
  • 129
    • 68049086486 scopus 로고    scopus 로고
    • Protein kinase Cα, but not PKCβ or PKCγ, regulates contractility and heartfailure susceptibility: Implications for ruboxistaurin as a novel therapeutic approach
    • Liu, Q.; Chen, X.; Macdonnell, S. M.; Kranias, E. G.; Lorenz, J. N.; Leitges, M.; Houser, S. R.;Molkentin, J. D., Protein kinase Cα, but not PKCβ or PKCγ, regulates contractility and heartfailure susceptibility: Implications for ruboxistaurin as a novel therapeutic approach. Circ. Res.2009, 105, 194-200.
    • (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
  • 130
    • 27644554420 scopus 로고    scopus 로고
    • Go 6983: A fast acting protein kinase C inhibitor thatattenuates myocardial ischemia/reperfusion injury
    • Young, L. H.; Balin, B. J.; Weis, M. T. Go 6983: a fast acting protein kinase C inhibitor thatattenuates myocardial ischemia/reperfusion injury. Cardiovasc. Drug Rev. 2005, 23, 255-272.
    • (2005) Cardiovasc. Drug Rev , vol.23 , pp. 255-272
    • Young, L.H.1    Balin, B.J.2    Weis, M.T.3
  • 131
    • 2042458414 scopus 로고    scopus 로고
    • Go 6983 exerts cardioprotectiveeffects in myocardial ischemia/reperfusion
    • Peterman, E. E.; Taormina, P., II; Harvey, M.; Young, L. H. Go 6983 exerts cardioprotectiveeffects in myocardial ischemia/reperfusion. J. Cardiovasc. Pharmacol. 2004, 43, 645-656.
    • (2004) J. Cardiovasc. Pharmacol , vol.43 , pp. 645-656
    • Peterman, E.E.1    Taormina, P.2    Harvey, M.3    Young, L.H.4
  • 132
    • 22944483476 scopus 로고    scopus 로고
    • Protein kinaseC βII peptide inhibitor exerts cardioprotective effects in rat cardiac ischemia/reperfusion injury
    • Omiyi, D.; Brue, R. J.; Taormina, P., II; Harvey, M.; Atkinson, N.; Young, L. H., Protein kinaseC βII peptide inhibitor exerts cardioprotective effects in rat cardiac ischemia/reperfusion injury.J. Pharmacol. Exp. Ther. 2005, 314, 542-551.
    • (2005) J. Pharmacol. Exp. Ther , vol.314 , pp. 542-551
    • Omiyi, D.1    Brue, R.J.2    Taormina, P.3    Harvey, M.4    Atkinson, N.5    Young, L.H.6
  • 135
    • 34447526639 scopus 로고    scopus 로고
    • Comparative effects of ischemic pre and postconditioning onischemia-reperfusion injury in spontaneously hypertensive rats (SHR)
    • Fantinelli, J. C.; Mosca, S. M. Comparative effects of ischemic pre and postconditioning onischemia-reperfusion injury in spontaneously hypertensive rats (SHR). Mol. Cell. Biochem. 2007,296, 45-51.
    • (2007) Mol. Cell. Biochem , vol.296 , pp. 45-51
    • Fantinelli, J.C.1    Mosca, S.M.2
  • 136
    • 0029979973 scopus 로고    scopus 로고
    • Inhibitor, abolishes preconditioninginducedprotection against contractile dysfunction in the isolated blood perfused rat heart
    • Cave, A. C.; Apstein, C. S. Polymyxin B, a protein kinase C inhibitor, abolishes preconditioninginducedprotection against contractile dysfunction in the isolated blood perfused rat heart. J. Mol. Cell. Cardiol. 1996, 28, 977-987.
    • (1996) J. Mol. Cell. Cardiol , vol.28 , pp. 977-987
    • Cave, A.C.1    Apstein, C.S.2    Polymyxin, B.3
  • 137
    • 0028914411 scopus 로고
    • Pretreatment with angiotensin II activatesprotein kinase C and limits myocardial infarction in isolated rabbit hearts
    • Liu, Y.; Tsuchida, A.; Cohen, M. V.; Downey, J. M. Pretreatment with angiotensin II activatesprotein kinase C and limits myocardial infarction in isolated rabbit hearts. J. Mol. Cell. Cardiol.1995, 27, 883-892.
    • (1995) J. Mol. Cell. Cardiol , vol.27 , pp. 883-892
    • Liu, Y.1    Tsuchida, A.2    Cohen, M.V.3    Downey, J.M.4
  • 138
    • 0034625662 scopus 로고    scopus 로고
    • Cardiotrophic effects of protein kinase C epsilon: Analysis by in vivomodulation of PKCepsilon translocation
    • Mochly-Rosen, D.; Wu, G.; Hahn, H.; Osinska, H.; Liron, T.; Lorenz, J. N.; Yatani, A.; Robbins, J.; Dorn, G. W. Cardiotrophic effects of protein kinase C epsilon: Analysis by in vivomodulation of PKCepsilon translocation. Circ. Res. 2000, 86, 1173-1179.
    • (2000) Circ. Res , vol.86 , pp. 1173-1179
    • Mochly-Rosen, D.1    Wu, G.2    Hahn, H.3    Osinska, H.4    Liron, T.5    Lorenz, J.N.6    Yatani, A.7    Robbins, J.8    Dorn, G.W.9
  • 139
    • 0033583131 scopus 로고    scopus 로고
    • Isoform-selective activation of protein kinase C by nitric oxide in theheart of conscious rabbits: A signaling mechanism for both nitric oxide-induced and ischemiainducedpreconditioning
    • Ping, P.; Takano, H.; Zhang, J.; Tang, X. L.; Qiu, Y.; Li, R. C.; Banerjee, S.; Dawn, B.;Balafonova, Z.; Bolli, R. Isoform-selective activation of protein kinase C by nitric oxide in theheart of conscious rabbits: A signaling mechanism for both nitric oxide-induced and ischemiainducedpreconditioning. Circ. Res. 1999, 84, 587-604.
    • (1999) Circ. Res , vol.84 , pp. 587-604
    • Ping, P.1    Takano, H.2    Zhang, J.3    Tang, X.L.4    Qiu, Y.5    Li, R.C.6    Banerjee, S.7    Dawn, B.8    Balafonova, Z.9    Bolli, R.10
  • 140
    • 0041932511 scopus 로고    scopus 로고
    • Additive protection of theischemic heart ex vivo by combined treatment with δ-protein kinase C inhibitor and epsilonproteinkinase C activator
    • Inagaki, K.; Hahn, H. S.; Dorn, G. W.; Mochly-Rosen, D. Additive protection of theischemic heart ex vivo by combined treatment with δ-protein kinase C inhibitor and epsilonproteinkinase C activator. Circulation 2003, 108, 869-875.
    • (2003) Circulation , vol.108 , pp. 869-875
    • Inagaki, K.1    Hahn, H.S.2    Dorn, G.W.3    Mochly-Rosen, D.4
  • 141
    • 45849123850 scopus 로고    scopus 로고
    • Mechanisms related to the cardioprotective effects of protein kinase Cepsilon (PKC epsilon) peptide activator or inhibitor in rat ischemia/reperfusion injury. NaunynSchmiedebergs
    • Teng, J. C.; Kay, H.; Chen, Q.; Adams, J. S.; Grilli, C.; Guglielmello, G.; Zambrano, C.; Krass, S.; Bell, A.; Young, L. H. Mechanisms related to the cardioprotective effects of protein kinase Cepsilon (PKC epsilon) peptide activator or inhibitor in rat ischemia/reperfusion injury. NaunynSchmiedebergs Arch. Pharmacol. 2008, 378, 1-15.
    • (2008) Arch. Pharmacol , vol.378 , pp. 1-15
    • Teng, J.C.1    Kay, H.2    Chen, Q.3    Adams, J.S.4    Grilli, C.5    Guglielmello, G.6    Zambrano, C.7    Krass, S.8    Bell, A.9    Young, L.H.10
  • 142
    • 49249102227 scopus 로고    scopus 로고
    • Differential loss of cytochrome-coxidase subunits in ischemia-reperfusion injury: Exacerbation of COI subunit loss by PKCepsiloninhibition
    • Yu, Q.; Nguyen, T.; Ogbi, M.; Caldwell, R. W.; Johnson, J. A. Differential loss of cytochrome-coxidase subunits in ischemia-reperfusion injury: Exacerbation of COI subunit loss by PKCepsiloninhibition. Am. J. Physiol. Heart Circ. Physiol. 2008, 294, H2637-2645.
    • (2008) Am. J. Physiol. Heart Circ. Physiol , vol.294
    • Yu, Q.1    Nguyen, T.2    Ogbi, M.3    Caldwell, R.W.4    Johnson, J.A.5
  • 143
    • 0034768126 scopus 로고    scopus 로고
    • Protein kinase C-epsilon is a trigger of delayedcardioprotection against myocardial ischemia of κ-opioid receptor stimulation in rat ventricularmyocytes
    • Wang, G. Y.; Zhou, J. J.; Shan, J.; Wong, T. M. Protein kinase C-epsilon is a trigger of delayedcardioprotection against myocardial ischemia of κ-opioid receptor stimulation in rat ventricularmyocytes. J. Pharmacol. Exp. Ther. 2001, 299, 603-610.
    • (2001) J. Pharmacol. Exp. Ther , vol.299 , pp. 603-610
    • Wang, G.Y.1    Zhou, J.J.2    Shan, J.3    Wong, T.M.4
  • 144
    • 14244270061 scopus 로고    scopus 로고
    • PKC-epsilon inhibits the hyperglycemiainducedapoptosis signal in adult rat ventricular myocytes
    • Malhotra, A.; Kang, B. P.; Hashmi, S.; Meggs, L. G. PKC-epsilon inhibits the hyperglycemiainducedapoptosis signal in adult rat ventricular myocytes. Mol. Cell. Biochem. 2005, 268,169-173.
    • (2005) Mol. Cell. Biochem , vol.268 , pp. 169-173
    • Malhotra, A.1    Kang, B.P.2    Hashmi, S.3    Meggs, L.G.4
  • 146
    • 34547111036 scopus 로고    scopus 로고
    • The protein kinase Cpathway mediates cardioprotection induced by cardiac-specific overexpression of fibroblastgrowth factor-2
    • House, S. L.; Melhorn, S. J.; Newman, G.; Doetschman, T.; Schultz Jel, J. The protein kinase Cpathway mediates cardioprotection induced by cardiac-specific overexpression of fibroblastgrowth factor-2. Am. J. Physiol. Heart Circ. Physiol. 2007, 293, H354-H365.
    • (2007) Am. J. Physiol. Heart Circ. Physiol , vol.293
    • House, S.L.1    Melhorn, S.J.2    Newman, G.3    Doetschman, T.4    Jel, J.S.5
  • 147
  • 150
    • 0025727594 scopus 로고
    • CDNA cloning of a novel 85 kd protein that has SH2 domains and regulates binding of PI3-kinase to the PDGF β-receptor
    • Escobedo, J. A.; Navankasattusas, S.; Kavanaugh, W. M.; Milfay, D.; Fried, V. A.; Williams, L.T. cDNA cloning of a novel 85 kd protein that has SH2 domains and regulates binding of PI3-kinase to the PDGF β-receptor. Cell 1991, 65, 75-82.
    • (1991) Cell , vol.65 , pp. 75-82
    • Escobedo, J.A.1    Navankasattusas, S.2    Kavanaugh, W.M.3    Milfay, D.4    Fried, V.A.5    Williams, L.T.6
  • 151
    • 0025755422 scopus 로고
    • Characterization of two 85 kd proteins that associate with receptortyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase
    • Otsu, M.; Hiles, I.; Gout, I.; Fry, M. J.; Ruiz-Larrea, F.; Panayotou, G.; Thompson, A.; Dhand, R.; Hsuan, J.; Totty, N.; et al. Characterization of two 85 kd proteins that associate with receptortyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase. Cell 1991, 65, 91-104.
    • (1991) Cell , vol.65 , pp. 91-104
    • Otsu, M.1    Hiles, I.2    Gout, I.3    Fry, M.J.4    Ruiz-Larrea, F.5    Panayotou, G.6    Thompson, A.7    Dhand, R.8    Hsuan, J.9    Totty, N.10
  • 152
    • 0025921611 scopus 로고
    • Cloning of PI3 kinase-associated p85 utilizing a novel method forexpression/cloning of target proteins for receptor tyrosine kinases
    • Skolnik, E. Y.; Margolis, B.; Mohammadi, M.; Lowenstein, E.; Fischer, R.; Drepps, A.; Ullrich, A.; Schlessinger, J. Cloning of PI3 kinase-associated p85 utilizing a novel method forexpression/cloning of target proteins for receptor tyrosine kinases. Cell 1991, 65, 83-90.
    • (1991) Cell , vol.65 , pp. 83-90
    • Skolnik, E.Y.1    Margolis, B.2    Mohammadi, M.3    Lowenstein, E.4    Fischer, R.5    Drepps, A.6    Ullrich, A.7    Schlessinger, J.8
  • 153
  • 154
    • 0033581886 scopus 로고    scopus 로고
    • Structural insights intophosphoinositide 3-kinase catalysis and signaling
    • Walker, E. H.; Perisic, O.; Ried, C.; Stephens, L.; Williams, R. L. Structural insights intophosphoinositide 3-kinase catalysis and signaling. Nature 1999, 402, 313-320.
    • (1999) Nature , vol.402 , pp. 313-320
    • Walker, E.H.1    Perisic, O.2    Ried, C.3    Stephens, L.4    Williams, R.L.5
  • 158
    • 37349027301 scopus 로고    scopus 로고
    • Altered heart rate and sinoatrial node function in micelacking the cAMP regulator phosphoinositide 3-kinase-γ
    • Rose, R. A.; Kabir, M. G.; Backx, P. H. Altered heart rate and sinoatrial node function in micelacking the cAMP regulator phosphoinositide 3-kinase-γ. Circ. Res. 2007, 101, 1274-1282.
    • (2007) Circ. Res , vol.101 , pp. 1274-1282
    • Rose, R.A.1    Kabir, M.G.2    Backx, P.H.3
  • 159
    • 33947371601 scopus 로고    scopus 로고
    • Differential role ofPI3K/Akt pathway in the infarct size limitation and antiarrhythmic protection in the rat heart
    • Ravingerova, T.; Matejikova, J.; Neckar, J.; Andelova, E.; Kolar, F. Differential role ofPI3K/Akt pathway in the infarct size limitation and antiarrhythmic protection in the rat heart.Mol. Cell. Biochem. 2007, 297, 111-120.
    • (2007) Mol. Cell. Biochem , vol.297 , pp. 111-120
    • Ravingerova, T.1    Matejikova, J.2    Neckar, J.3    Andelova, E.4    Kolar, F.5
  • 160
    • 77949361812 scopus 로고    scopus 로고
    • Madeddu, P.Involvement of phosphoinositide 3-kinase γ in angiogenesis and healing of experimentalmyocardial infarction in mice
    • Siragusa, M.; Katare, R.; Meloni, M.; Damilano, F.; Hirsch, E.; Emanueli, C.; Madeddu, P.Involvement of phosphoinositide 3-kinase γ in angiogenesis and healing of experimentalmyocardial infarction in mice. Circ. Res. 2010, 106, 757-768.
    • (2010) Circ. Res , vol.106 , pp. 757-768
    • Siragusa, M.1    Katare, R.2    Meloni, M.3    Damilano, F.4    Hirsch, E.5    Emanueli, C.6
  • 161
    • 33748538992 scopus 로고    scopus 로고
    • Targeted inhibition of phosphoinositide 3-kinaseactivity as a novel strategy to normalize β-adrenergic receptor function in heart failure
    • Perrino, C.; Rockman, H. A.; Chiariello, M. Targeted inhibition of phosphoinositide 3-kinaseactivity as a novel strategy to normalize β-adrenergic receptor function in heart failure. Vascul.Pharmacol. 2006, 45, 77-85.
    • (2006) Vascul. Pharmacol , vol.45 , pp. 77-85
    • Perrino, C.1    Rockman, H.A.2    Chiariello, M.3
  • 162
    • 20344402530 scopus 로고    scopus 로고
    • Targeted inhibition of β-adrenergic receptor kinase-1-associated phosphoinositide-3 kinase activity preserves β-adrenergic receptor signaling and prolongs survival in heart failure induced by calsequestrinoverexpression
    • Perrino, C.; Naga Prasad, S. V.; Patel, M.; Wolf, M. J.; Rockman, H. A. Targeted inhibition of β-adrenergic receptor kinase-1-associated phosphoinositide-3 kinase activity preserves β-adrenergic receptor signaling and prolongs survival in heart failure induced by calsequestrinoverexpression. J. Am. Coll. Cardiol. 2005, 45, 1862-1870.
    • (2005) J. Am. Coll. Cardiol , vol.45 , pp. 1862-1870
    • Perrino, C.1    Prasad, S.V.N.2    Patel, M.3    Wolf, M.J.4    Rockman, H.A.5
  • 163
    • 19644397920 scopus 로고    scopus 로고
    • A.Restoration of β-adrenergic receptor signaling and contractile function in heart failure bydisruption of the β-ARK1/phosphoinositide 3-kinase complex
    • Perrino, C.; Naga Prasad, S. V.; Schroder, J. N.; Hata, J. A.; Milano, C.; Rockman, H. A.Restoration of β-adrenergic receptor signaling and contractile function in heart failure bydisruption of the β-ARK1/phosphoinositide 3-kinase complex. Circulation 2005, 111,2579-2587.
    • (2005) Circulation , vol.111 , pp. 2579-2587
    • Perrino, C.1    Prasad, S.V.N.2    Schroder, J.N.3    Hata, J.A.4    Milano, C.5    Rockman, H.6
  • 164
    • 85047693926 scopus 로고    scopus 로고
    • Inhibition of receptor-localized PI3K preserves cardiac β-adrenergic receptor function andameliorates pressure overload heart failure
    • Nienaber, J. J.; Tachibana, H.; Naga Prasad, S. V.; Esposito, G.; Wu, D.; Mao, L.; Rockman, H.A. Inhibition of receptor-localized PI3K preserves cardiac β-adrenergic receptor function andameliorates pressure overload heart failure. J. Clin. Invest. 2003, 112, 1067-1079.
    • (2003) J. Clin. Invest , vol.112 , pp. 1067-1079
    • Nienaber, J.J.1    Tachibana, H.2    Prasad, S.V.N.3    Esposito, G.4    Wu, D.5    Mao, L.6    Rockman, H.A.7
  • 165
    • 77749254756 scopus 로고    scopus 로고
    • Tumor necrosis factor induces matrix metalloproteinases in cardiomyocytesand cardiofibroblasts differentially via superoxide production in a PI3K-gamma-dependentmanner
    • Awad, A. E.; Kandalam, V.; Chakrabarti, S.; Wang, X.; Penninger, J. M.; Davidge, S. T.; Oudit, G. Y.; Kassiri, Z. Tumor necrosis factor induces matrix metalloproteinases in cardiomyocytesand cardiofibroblasts differentially via superoxide production in a PI3K-gamma-dependentmanner. Am. J. Physiol. Cell. Physiol 2010, 298, 679-692.
    • (2010) Am. J. Physiol. Cell. Physiol , pp. 679-692
    • Awad, A.E.1    Kandalam, V.2    Chakrabarti, S.3    Wang, X.4    Penninger, J.M.5    Davidge, S.T.6    Oudit, G.Y.7    Kassiri, Z.8
  • 166
    • 33745185351 scopus 로고    scopus 로고
    • Intermittent pressure overload triggers hypertrophy-independent cardiac dysfunction andvascular rarefaction
    • Perrino, C.; Naga Prasad, S. V.; Mao, L.; Noma, T.; Yan, Z.; Kim, H. S.; Smithies, O.; Rockman, H. A. Intermittent pressure overload triggers hypertrophy-independent cardiac dysfunction andvascular rarefaction. J. Clin. Invest. 2006, 116, 1547-1560.
    • (2006) J. Clin. Invest , vol.116 , pp. 1547-1560
    • Perrino, C.1    Prasad, S.V.N.2    Mao, L.3    Noma, T.4    Yan, Z.5    Kim, H.S.6    Smithies, O.7
  • 168
    • 70350448860 scopus 로고    scopus 로고
    • Activation of a novel estrogen receptor, GPER, iscardioprotective in male and female rats
    • Deschamps, A. M.; Murphy, E. Activation of a novel estrogen receptor, GPER, iscardioprotective in male and female rats. Am. J. Physiol. Heart Circ. Physiol. 2009, 297,1806-1813.
    • (2009) Am. J. Physiol. Heart Circ. Physiol , vol.297 , pp. 1806-1813
    • Deschamps, A.M.1    Murphy, E.2
  • 169
    • 67650221165 scopus 로고    scopus 로고
    • Role of B-type natriuretic peptide in epoxyeicosatrienoic acid-mediatedimproved post-ischaemic recovery of heart contractile function
    • Chaudhary, K. R.; Batchu, S. N.; Das, D.; Suresh, M. R.; Falck, J. R.; Graves, J. P.; Zeldin, D.C.; Seubert, J. M. Role of B-type natriuretic peptide in epoxyeicosatrienoic acid-mediatedimproved post-ischaemic recovery of heart contractile function. Cardiovasc. Res. 2009, 83,362-370.
    • (2009) Cardiovasc. Res , vol.83 , pp. 362-370
    • Batchu, S.N.1    Das, D.2    Suresh, M.R.3    Falck, J.R.4    Graves, J.P.5    Zeldin, D.C.6    Seubert, J.M.7
  • 174
    • 0142027759 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase(p110-α) plays a critical role for the induction of physiological, but notpathological, cardiac hypertrophy
    • McMullen, J. R.; Shioi, T.; Zhang, L.; Tarnavski, O.; Sherwood, M. C.; Kang, P. M.; Izumo, S.Phosphoinositide 3-kinase(p110-α) plays a critical role for the induction of physiological, but notpathological, cardiac hypertrophy. Proc. Natl. Acad. Sci. USA 2003, 100, 12355-12360.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12355-12360
    • McMullen, J.R.1    Shioi, T.2    Zhang, L.3    Tarnavski, O.4    Sherwood, M.C.5    Kang, P.M.6
  • 176
    • 48849088862 scopus 로고    scopus 로고
    • Darbepoetin alfa exerts acardioprotective effect in autoimmune cardiomyopathy via reduction of ER stress and activationof the PI3K/Akt and STAT3 pathways
    • Mao, W.; Iwai, C.; Liu, J.; Sheu, S. S.; Fu, M.; Liang, C. S. Darbepoetin alfa exerts acardioprotective effect in autoimmune cardiomyopathy via reduction of ER stress and activationof the PI3K/Akt and STAT3 pathways. J. Mol. Cell. Cardiol. 2008, 45, 250-260.
    • (2008) J. Mol. Cell. Cardiol , vol.45 , pp. 250-260
    • Mao, W.1    Iwai, C.2    Liu, J.3    Sheu, S.S.4    Fu, M.5    Liang, C.S.6
  • 177
    • 33749438378 scopus 로고    scopus 로고
    • Competitive displacement of phosphoinositide 3-kinase from β-adrenergicreceptor kinase-1 improves postinfarction adverse myocardial remodeling
    • Curcio, A.; Noma, T.; Naga Prasad, S. V.; Wolf, M. J.; Lemaire, A.; Perrino, C.; Mao, L.;Rockman, H. A. Competitive displacement of phosphoinositide 3-kinase from β-adrenergicreceptor kinase-1 improves postinfarction adverse myocardial remodeling. Am. J. Physiol. HeartCirc. Physiol. 2006, 291, H1754-H1760.
    • (2006) Am. J. Physiol. HeartCirc. Physiol , vol.291
    • Curcio, A.1    Noma, T.2    Prasad, S.V.N.3    Wolf, M.J.4    Lemaire, A.5    Perrino, C.6    Mao, L.7    Rockman, H.A.8
  • 178
    • 77955704300 scopus 로고    scopus 로고
    • The anti-apoptotic effect of heat shockprotein 90 on hypoxia-mediated cardiomyocyte damage through the Pi3k/Akt pathway
    • Wang, W.; Peng, Y.; Wang, Y.; Zhao, X.; Yuan, Z. The anti-apoptotic effect of heat shockprotein 90 on hypoxia-mediated cardiomyocyte damage through the Pi3k/Akt pathway. Clin.Exp. Pharmacol. Physiol. 2009.
    • (2009) Clin. Exp. Pharmacol. Physiol
    • Wang, W.1    Peng, Y.2    Wang, Y.3    Zhao, X.4    Yuan, Z.5
  • 179
    • 65949097056 scopus 로고    scopus 로고
    • Estrogen receptor beta mediates increased activation of PI3K/Akt signaling and improvedmyocardial function in female hearts following acute ischemia
    • Wang, M. J.; Wang, Y.; Weil, B.; Abarbanell, A.; Herrmann, J.; Tan, J. N.; Kelly, M.; Meldrum, D. R. Estrogen receptor beta mediates increased activation of PI3K/Akt signaling and improvedmyocardial function in female hearts following acute ischemia. Am. J. Physiol. Regul. Integr. Compar. Physiol. 2009, 296, R972-R978.
    • (2009) Am. J. Physiol. Regul. Integr. Compar. Physiol , vol.296
    • Wang, M.J.1    Wang, Y.2    Weil, B.3    Abarbanell, A.4    Herrmann, J.5    Tan, J.N.6    Kelly, M.7
  • 180
    • 64049095859 scopus 로고    scopus 로고
    • PPAR-αactivation protects the type 2 diabetic myocardium against ischemia-reperfusion injury: Involvement of the PI3-Kinase/Akt and NO pathway
    • Bulhak, A. A.; Jung, C.; Ostenson, C. G.; Lundberg, J. O.; Sjoquist, P. O.; Pernow, J. PPAR-αactivation protects the type 2 diabetic myocardium against ischemia-reperfusion injury: Involvement of the PI3-Kinase/Akt and NO pathway. Am. J. Physiol. Heart Circ. Physiol. 2009,296, H719-727.
    • (2009) Am. J. Physiol. Heart Circ. Physiol , vol.296
    • Bulhak, A.A.1    Jung, C.2    Ostenson, C.G.3    Lundberg, J.O.4    Sjoquist, P.O.5    Pernow, J.6
  • 181
    • 23644447741 scopus 로고    scopus 로고
    • Preconditioning thediabetic heart: The importance of Akt phosphorylation
    • Tsang, A.; Hausenloy, D. J.; Mocanu, M. M.; Carr, R. D.; Yellon, D. M. Preconditioning thediabetic heart: The importance of Akt phosphorylation. Diabetes 2005, 54, 2360-2364.
    • (2005) Diabetes , vol.54 , pp. 2360-2364
    • Tsang, A.1    Hausenloy, D.J.2    Mocanu, M.M.3    Carr, R.D.4    Yellon, D.M.5
  • 182
    • 0032787638 scopus 로고    scopus 로고
    • Myocardial protection by insulin isdependent on phospatidylinositol 3-kinase but not protein kinase C or KATP channels in theisolated rabbit heart
    • Baines, C. P.; Wang, L.; Cohen, M. V.; Downey, J. M. Myocardial protection by insulin isdependent on phospatidylinositol 3-kinase but not protein kinase C or KATP channels in theisolated rabbit heart. Basic Res. Cardiol. 1999, 94, 188-198.
    • (1999) Basic Res. Cardiol , vol.94 , pp. 188-198
    • Baines, C.P.1    Wang, L.2    Cohen, M.V.3    Downey, J.M.4
  • 183
    • 37349123107 scopus 로고    scopus 로고
    • Erythropoietin protects against doxorubicin-inducedcardiomyopathy via a phosphatidylinositol 3-kinase-dependent pathway
    • Kim, K. H.; Oudit, G. Y.; Backx, P. H. Erythropoietin protects against doxorubicin-inducedcardiomyopathy via a phosphatidylinositol 3-kinase-dependent pathway. J. Pharmacol. Exp.Ther. 2008, 324, 160-169.
    • (2008) J. Pharmacol. Exp.Ther , vol.324 , pp. 160-169
    • Kim, K.H.1    Oudit, G.Y.2    Backx, P.H.3
  • 184
    • 36348963739 scopus 로고    scopus 로고
    • S.Cardioprotection induced by hydrogen sulfide preconditioning involves activation of ERK andPI3K/Akt pathways
    • Hu, Y.; Chen, X.; Pan, T. T.; Neo, K. L.; Lee, S. W.; Khin, E. S.; Moore, P. K.; Bian, J. S.Cardioprotection induced by hydrogen sulfide preconditioning involves activation of ERK andPI3K/Akt pathways. Pflugers Arch. 2008, 455, 607-616.
    • (2008) Pflugers Arch , vol.455 , pp. 607-616
    • Hu, Y.1    Chen, X.2    Pan, T.T.3    Neo, K.L.4    Lee, S.W.5    Khin, E.S.6    Moore, P.K.7    Bian, J.8
  • 186
    • 11444267248 scopus 로고    scopus 로고
    • Isoflurane protects against myocardial infarction during early reperfusion by activation ofphosphatidylinositol-3-kinase signal transduction: Evidence for anesthetic-inducedpostconditioning in rabbits
    • Chiari, P. C.; Bienengraeber, M. W.; Pagel, P. S.; Krolikowski, J. G.; Kersten, J. R.; Warltier, D.C. Isoflurane protects against myocardial infarction during early reperfusion by activation ofphosphatidylinositol-3-kinase signal transduction: Evidence for anesthetic-inducedpostconditioning in rabbits. Anesthesiology 2005, 102, 102-109.
    • (2005) Anesthesiology , vol.102 , pp. 102-109
    • Chiari, P.C.1    Bienengraeber, M.W.2    Pagel, P.S.3    Krolikowski, J.G.4    Kersten, J.R.5    Warltier, D.C.6
  • 187
    • 4043060632 scopus 로고    scopus 로고
    • Postconditioning: A form ofmodified reperfusion protects the myocardium by activating the phosphatidylinositol 3-kinase-Akt pathway
    • Tsang, A.; Hausenloy, D. J.; Mocanu, M. M.; Yellon, D. M. Postconditioning: A form ofmodified reperfusion protects the myocardium by activating the phosphatidylinositol 3-kinase-Akt pathway. Circ. Res. 2004, 95, 230-232.
    • (2004) Circ. Res , vol.95 , pp. 230-232
    • Tsang, A.1    Hausenloy, D.J.2    Mocanu, M.M.3    Yellon, D.M.4
  • 188
    • 70449518977 scopus 로고    scopus 로고
    • Wan, Y.Vascular endothelial growth factor promotes cardiac stem cell migration via the PI3K/Aktpathway
    • Tang, J.; Wang, J.; Kong, X.; Yang, J.; Guo, L.; Zheng, F.; Zhang, L.; Huang, Y.; Wan, Y.Vascular endothelial growth factor promotes cardiac stem cell migration via the PI3K/Aktpathway. Exp. Cell Res. 2009, 315, 3521-3531.
    • (2009) Exp. Cell Res , vol.315 , pp. 3521-3531
    • Tang, J.1    Wang, J.2    Kong, X.3    Yang, J.4    Guo, L.5    Zheng, F.6    Zhang, L.7    Huang, Y.8
  • 189
    • 0032881288 scopus 로고    scopus 로고
    • AKT/PKB and other D3 phosphoinositideregulatedkinases: Kinase activation by phosphoinositide-dependent phosphorylation
    • Chan, T. O.; Rittenhouse, S. E.; Tsichlis, P. N. AKT/PKB and other D3 phosphoinositideregulatedkinases: Kinase activation by phosphoinositide-dependent phosphorylation. Annu. Rev. Biochem. 1999, 68, 965-1014.
    • (1999) Annu. Rev. Biochem , vol.68 , pp. 965-1014
    • Chan, T.O.1    Rittenhouse, S.E.2    Tsichlis, P.N.3
  • 192
    • 34548800403 scopus 로고    scopus 로고
    • P38 pathway kinases as anti-inflammatory drugtargets
    • Schindler, J. F.; Monahan, J. B.; Smith, W. G. p38 pathway kinases as anti-inflammatory drugtargets. J. Dent. Res. 2007, 86, 800-811.
    • (2007) J. Dent. Res , vol.86 , pp. 800-811
    • Schindler, J.F.1    Monahan, J.B.2    Smith, W.G.3
  • 193
    • 33748331228 scopus 로고    scopus 로고
    • Activation and apoptoticalterations in hearts subjected to calcium paradox are attenuated by taurine
    • Xu, Y. J.; Saini, H. K.; Zhang, M.; Elimban, V.; Dhalla, N. S. MAPK activation and apoptoticalterations in hearts subjected to calcium paradox are attenuated by taurine. Cardiovasc. Res.2006, 72, 163-174.
    • (2006) Cardiovasc. Res , vol.72 , pp. 163-174
    • Xu, Y.J.1    Saini, H.K.2    Zhang, M.3    Elimban, V.4    Dhalla, N.S.5
  • 194
    • 0031939753 scopus 로고    scopus 로고
    • Cardiac musclecell hypertrophy and apoptosis induced by distinct members of the p38 mitogen-activated proteinkinase family
    • Wang, Y.; Huang, S.; Sah, V. P.; Ross, J., Jr.; Brown, J. H.; Han, J.; Chien, K. R. Cardiac musclecell hypertrophy and apoptosis induced by distinct members of the p38 mitogen-activated proteinkinase family. J. Biol. Chem. 1998, 273, 2161-2168.
    • (1998) J. Biol. Chem , vol.273 , pp. 2161-2168
    • Wang, Y.1    Huang, S.2    Sah, V.P.3    Ross Jr., J.4    Brown, J.H.5    Han, J.6    Chien, K.R.7
  • 195
    • 5644285411 scopus 로고    scopus 로고
    • P38mitogen-activated protein kinase inhibition improves cardiac function and attenuates leftventricular remodeling following myocardial infarction in the rat
    • See, F.; Thomas, W.; Way, K.; Tzanidis, A.; Kompa, A.; Lewis, D.; Itescu, S.; Krum, H. p38mitogen-activated protein kinase inhibition improves cardiac function and attenuates leftventricular remodeling following myocardial infarction in the rat. J. Am. Coll. Cardiol. 2004, 44,1679-1689.
    • (2004) J. Am. Coll. Cardiol , vol.44 , pp. 1679-1689
    • See, F.1    Thomas, W.2    Way, K.3    Tzanidis, A.4    Kompa, A.5    Lewis, D.6    Itescu, S.7    Krum, H.8
  • 196
    • 0033998888 scopus 로고    scopus 로고
    • Inhibition of the cardiac p38-MAPKpathway by SB203580 delays ischemic cell death
    • Barancik, M.; Htun, P.; Strohm, C.; Kilian, S.; Schaper, W. Inhibition of the cardiac p38-MAPKpathway by SB203580 delays ischemic cell death. J. Cardiovasc. Pharmacol. 2000, 35, 474-483.
    • (2000) J. Cardiovasc. Pharmacol , vol.35 , pp. 474-483
    • Barancik, M.1    Htun, P.2    Strohm, C.3    Kilian, S.4    Schaper, W.5
  • 197
    • 0027946514 scopus 로고
    • Thestress-activated protein kinases are major c-Jun amino-terminal kinases activated by ischemiaand reperfusion
    • Pombo, C. M.; Bonventre, J. V.; Avruch, J.; Woodgett, J. R.; Kyriakis, J. M.; Force, T. Thestress-activated protein kinases are major c-Jun amino-terminal kinases activated by ischemiaand reperfusion. J. Biol. Chem. 1994, 269, 26546-26551.
    • (1994) J. Biol. Chem , vol.269 , pp. 26546-26551
    • Pombo, C.M.1    Bonventre, J.V.2    Avruch, J.3    Woodgett, J.R.4    Kyriakis, J.M.5    Force, T.6
  • 198
    • 0032142853 scopus 로고    scopus 로고
    • Role of p38 MAP kinase in myocardial stress
    • Nagarkatti, D. S.; Sha'afi, R. I. Role of p38 MAP kinase in myocardial stress. J. Mol. Cell.Cardiol. 1998, 30, 1651-1664.
    • (1998) J. Mol. Cell.Cardiol , vol.30 , pp. 1651-1664
    • Nagarkatti, D.S.1    Sha'afi, R.I.2
  • 199
    • 0033748263 scopus 로고    scopus 로고
    • The role of differential activation of p38-mitogen-activated protein kinase inpreconditioned ventricular myocytes
    • Saurin, A. T.; Martin, J. L.; Heads, R. J.; Foley, C.; Mockridge, J. W.; Wright, M. J.; Wang, Y.;Marber, M. S. The role of differential activation of p38-mitogen-activated protein kinase inpreconditioned ventricular myocytes. FASEB J. 2000, 14, 2237-2246.
    • (2000) FASEB J , vol.14 , pp. 2237-2246
    • Saurin, A.T.1    Martin, J.L.2    Heads, R.J.3    Foley, C.4    Mockridge, J.W.5    Wright, M.J.6    Wang, Y.7    Marber, M.S.8
  • 200
    • 0033528695 scopus 로고    scopus 로고
    • Inhibition of p38 mitogen-activated protein kinase decreasescardiomyocyte apoptosis and improves cardiac function after myocardial ischemia andreperfusion
    • Ma, X. L.; Kumar, S.; Gao, F.; Louden, C. S.; Lopez, B. L.; Christopher, T. A.; Wang, C.; Lee, J.C.; Feuerstein, G. Z.; Yue, T. L. Inhibition of p38 mitogen-activated protein kinase decreasescardiomyocyte apoptosis and improves cardiac function after myocardial ischemia andreperfusion. Circulation 1999, 99, 1685-1691.
    • (1999) Circulation , vol.99 , pp. 1685-1691
    • Ma, X.L.1    Kumar, S.2    Gao, F.3    Louden, C.S.4    Lopez, B.L.5    Christopher, T.A.6    Wang, C.7    Lee, J.C.8    Feuerstein, G.Z.9    Yue, T.L.10
  • 201
    • 0033525760 scopus 로고    scopus 로고
    • An inhibitor of p38 mitogen-activated protein kinase protectsneonatal cardiac myocytes from ischemia
    • Mackay, K.; Mochly-Rosen, D. An inhibitor of p38 mitogen-activated protein kinase protectsneonatal cardiac myocytes from ischemia. J. Biol. Chem. 1999, 274, 6272-6279.
    • (1999) J. Biol. Chem , vol.274 , pp. 6272-6279
    • Mackay, K.1    Mochly-Rosen, D.2
  • 202
    • 0035955751 scopus 로고    scopus 로고
    • Antiischemic effects ofSB203580 are mediated through the inhibition of p38-α mitogen-activated protein kinase:Evidence from ectopic expression of an inhibition-resistant kinase
    • Martin, J. L.; Avkiran, M.; Quinlan, R. A.; Cohen, P.; Marber, M. S. Antiischemic effects ofSB203580 are mediated through the inhibition of p38-α mitogen-activated protein kinase:Evidence from ectopic expression of an inhibition-resistant kinase. Circ. Res. 2001, 89, 750-752.
    • (2001) Circ. Res , vol.89 , pp. 750-752
    • Martin, J.L.1    Avkiran, M.2    Quinlan, R.A.3    Cohen, P.4    Marber, M.S.5
  • 206
    • 40749144924 scopus 로고    scopus 로고
    • P38 mitogen-activated proteinkinase inhibition decreases TNF-α secretion and protects against left ventricular remodeling inrats with myocardial ischemia
    • Yin, H.; Zhang, J.; Lin, H.; Wang, R.; Qiao, Y.; Wang, B.; Liu, F. p38 mitogen-activated proteinkinase inhibition decreases TNF-α secretion and protects against left ventricular remodeling inrats with myocardial ischemia. Inflammation 2008, 31, 65-73.
    • (2008) Inflammation , vol.31 , pp. 65-73
    • Yin, H.1    Zhang, J.2    Lin, H.3    Wang, R.4    Qiao, Y.5    Wang, B.6    Liu, F.7
  • 207
    • 65549171108 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase: A critical node linking insulin resistanceand cardiovascular diseases in type 2 diabetes mellitus
    • Liu, Z.; Cao, W. p38 mitogen-activated protein kinase: A critical node linking insulin resistanceand cardiovascular diseases in type 2 diabetes mellitus. Endocr. Metab. Immune Disord. Drug Targets 2009, 9, 38-46.
    • (2009) Endocr. Metab. Immune Disord. Drug Targets , vol.9 , pp. 38-46
    • Liu, Z.1    Cao, W.2
  • 208
    • 27744475493 scopus 로고    scopus 로고
    • No correlation between the p38 MAPK pathway andthe contractile dysfunction in diabetic cardiomyocytes: Hyperglycaemia-induced signaling andcontractile function
    • Wenzel, S.; Soltanpour, G.; Schluter, K. D. No correlation between the p38 MAPK pathway andthe contractile dysfunction in diabetic cardiomyocytes: Hyperglycaemia-induced signaling andcontractile function. Pflugers Arch. 2005, 451, 328-337.
    • (2005) Pflugers Arch , vol.451 , pp. 328-337
    • Wenzel, S.1    Soltanpour, G.2    Schluter, K.D.3
  • 209
    • 57149129986 scopus 로고    scopus 로고
    • The potential role of MLC phosphatase and MAPK signaling in thepathogenesis of vascular dysfunction in heart failure
    • Ogut, O.; Brozovich, F. V. The potential role of MLC phosphatase and MAPK signaling in thepathogenesis of vascular dysfunction in heart failure. J. Cell. Mol. Med. 2008, 12, 2158-2164.
    • (2008) J. Cell. Mol. Med , vol.12 , pp. 2158-2164
    • Ogut, O.1    Brozovich, F.V.2
  • 210
    • 59149107397 scopus 로고    scopus 로고
    • Chronic cocaineinducedcardiac oxidative stress and mitogen-activated protein kinase activation: The role ofNox2 oxidase
    • Fan, L.; Sawbridge, D.; George, V.; Teng, L.; Bailey, A.; Kitchen, I.; Li, J. M. Chronic cocaineinducedcardiac oxidative stress and mitogen-activated protein kinase activation: The role ofNox2 oxidase. J. Pharmacol. Exp. Ther. 2009, 328, 99-106.
    • (2009) J. Pharmacol. Exp. Ther , vol.328 , pp. 99-106
    • Fan, L.1    Sawbridge, D.2    George, V.3    Teng, L.4    Bailey, A.5    Kitchen, I.6    Li, J.M.7
  • 211
    • 53449097061 scopus 로고    scopus 로고
    • Mapk signaling in cardiovascular health and disease: Molecular mechanisms andtherapeutic targets
    • Muslin, A. J. Mapk signaling in cardiovascular health and disease: Molecular mechanisms andtherapeutic targets. Clin. Sci. 2008, 115, 203-218.
    • (2008) Clin. Sci , vol.115 , pp. 203-218
    • Muslin, A.J.1
  • 213
    • 34548016354 scopus 로고    scopus 로고
    • Role of p38 mitogen-activated proteinkinase on cardiac dysfunction after hemorrhagic shock in rats
    • Sato, H.; Tanaka, T.; Kasai, K.; Kita, T.; Tanaka, N. Role of p38 mitogen-activated proteinkinase on cardiac dysfunction after hemorrhagic shock in rats. Shock 2007, 28, 291-299.
    • (2007) Shock , vol.28 , pp. 291-299
    • Sato, H.1    Tanaka, T.2    Kasai, K.3    Kita, T.4    Tanaka, N.5
  • 214
    • 33748515649 scopus 로고    scopus 로고
    • Inhibition of p38 mitogen-activatedprotein kinase attenuates left ventricular dysfunction by mediating pro-inflammatory cardiaccytokine levels in a mouse model of diabetes mellitus
    • Westermann, D.; Rutschow, S.; Van Linthout, S.; Linderer, A.; Bucker-Gartner, C.; Sobirey, M.;Riad, A.; Pauschinger, M.; Schultheiss, H. P.; Tschope, C. Inhibition of p38 mitogen-activatedprotein kinase attenuates left ventricular dysfunction by mediating pro-inflammatory cardiaccytokine levels in a mouse model of diabetes mellitus. Diabetologia 2006, 49, 2507-2513.
    • (2006) Diabetologia , vol.49 , pp. 2507-2513
    • Westermann, D.1    Rutschow, S.2    van Linthout, S.3    Linderer, A.4    Bucker-Gartner, C.5    Sobirey, M.6    Riad, A.7    Pauschinger, M.8    Schultheiss, H.P.9    Tschope, C.10
  • 216
    • 33747879777 scopus 로고    scopus 로고
    • Selectiveinhibition of p38-alpha MAPK improves cardiac function and reduces myocardial apoptosis inrat model of myocardial injury
    • Li, Z.; Ma, J. Y.; Kerr, I.; Chakravarty, S.; Dugar, S.; Schreiner, G.; Protter, A. A. Selectiveinhibition of p38-alpha MAPK improves cardiac function and reduces myocardial apoptosis inrat model of myocardial injury. Am. J. Physiol. Heart Circ. Physiol. 2006, 291, H1972-H1977.
    • (2006) Am. J. Physiol. Heart Circ. Physiol , vol.291
    • Li, Z.1    Ma, J.Y.2    Kerr, I.3    Chakravarty, S.4    Dugar, S.5    Schreiner, G.6    Protter, A.A.7
  • 218
    • 1642305705 scopus 로고    scopus 로고
    • Inhibition of p38 MAPK decreases myocardialTNF-alpha expression and improves myocardial function and survival in endotoxemia
    • Peng, T.; Lu, X.; Lei, M.; Moe, G. W.; Feng, Q. Inhibition of p38 MAPK decreases myocardialTNF-alpha expression and improves myocardial function and survival in endotoxemia. Cardiovasc. Res. 2003, 59, 893-900.
    • (2003) Cardiovasc. Res , vol.59 , pp. 893-900
    • Peng, T.1    Lu, X.2    Lei, M.3    Moe, G.W.4    Feng, Q.5
  • 219
    • 0033134116 scopus 로고    scopus 로고
    • P38 MAPK inhibition decreases TNF-α production and enhances postischemic humanmyocardial function
    • Cain, B. S.; Meldrum, D. R.; Meng, X.; Dinarello, C. A.; Shames, B. D.; Banerjee, A.; Harken, A. H. p38 MAPK inhibition decreases TNF-α production and enhances postischemic humanmyocardial function. J. Surg. Res. 1999, 83, 7-12.
    • (1999) J. Surg. Res , vol.83 , pp. 7-12
    • Cain, B.S.1    Meldrum, D.R.2    Meng, X.3    Dinarello, C.A.4    Shames, B.D.5    Banerjee, A.6
  • 220
    • 38149051354 scopus 로고    scopus 로고
    • Insulin-induced myocardial protection in isolated ischemic rathearts requires p38 MAPK phosphorylation of Hsp27
    • Li, G.; Ali, I. S.; Currie, R. W. Insulin-induced myocardial protection in isolated ischemic rathearts requires p38 MAPK phosphorylation of Hsp27. Am. J. Physiol. Heart Circ. Physiol. 2008,294, H74-H87.
    • (2008) Am. J. Physiol. Heart Circ. Physiol , vol.294
    • Li, G.1    Ali, I.S.2    Currie, R.W.3
  • 221
    • 16844385112 scopus 로고    scopus 로고
    • The p38MAPK inhibitor SB203580 blocks adenosine A(1) receptor-induced attenuation of in vivomyocardial stunning
    • Yoshimura, Y.; Kristo, G.; Keith, B. J.; Jahania, S. A.; Mentzer, R. M., Jr.; Lasley, R. D. The p38MAPK inhibitor SB203580 blocks adenosine A(1) receptor-induced attenuation of in vivomyocardial stunning. Cardiovasc. Drugs Ther. 2004, 18, 433-440.
    • (2004) Cardiovasc. Drugs Ther , vol.18 , pp. 433-440
    • Yoshimura, Y.1    Kristo, G.2    Keith, B.J.3    Jahania, S.A.4    Mentzer Jr., R.M.5    Lasley, R.D.6
  • 224
    • 0034806269 scopus 로고    scopus 로고
    • Alterations of load-induced p38 MAP kinase activation in failing rathearts
    • Yasaka, A.; Hayashida, W. Alterations of load-induced p38 MAP kinase activation in failing rathearts. Biochem. Biophys. Res. Commun. 2001, 285, 503-507.
    • (2001) Biochem. Biophys. Res. Commun , vol.285 , pp. 503-507
    • Yasaka, A.1    Hayashida, W.2
  • 227
    • 0034537885 scopus 로고    scopus 로고
    • The p38 MAPK inhibitor, SB203580, abrogates ischaemic preconditioning in rat heart but timing of administration iscritical
    • Mocanu, M. M.; Baxter, G. F.; Yue, Y.; Critz, S. D.; Yellon, D. M. The p38 MAPK inhibitor, SB203580, abrogates ischaemic preconditioning in rat heart but timing of administration iscritical. Basic. Res. Cardiol. 2000, 95, 472-478.
    • (2000) Basic. Res. Cardiol , vol.95 , pp. 472-478
    • Mocanu, M.M.1    Baxter, G.F.2    Yue, Y.3    Critz, S.D.4    Yellon, D.M.5
  • 229
    • 38149108156 scopus 로고    scopus 로고
    • Role of p38-mitogen-activated protein kinase in ischaemicpreconditioning in rat heart
    • Bell, J. R.; Eaton, P.; Shattock, M. J. Role of p38-mitogen-activated protein kinase in ischaemicpreconditioning in rat heart. Clin. Exp. Pharmacol. Physiol. 2008, 35, 126-134.
    • (2008) Clin. Exp. Pharmacol. Physiol , vol.35 , pp. 126-134
    • Bell, J.R.1    Eaton, P.2    Shattock, M.J.3
  • 230
    • 34547872783 scopus 로고    scopus 로고
    • Inhibition of p38 MAPKand AMPK restores adenosine-induced cardioprotection in hearts stressed by antecedentischemia by altering glucose utilization
    • Jaswal, J. S.; Gandhi, M.; Finegan, B. A.; Dyck, J. R.; Clanachan, A. S. Inhibition of p38 MAPKand AMPK restores adenosine-induced cardioprotection in hearts stressed by antecedentischemia by altering glucose utilization. Am. J. Physiol. Heart Circ. Physiol. 2007, 293, H1107-H1114.
    • (2007) Am. J. Physiol. Heart Circ. Physiol , vol.293
    • Jaswal, J.S.1    Gandhi, M.2    Finegan, B.A.3    Dyck, J.R.4    Clanachan, A.S.5
  • 231
    • 34247266120 scopus 로고    scopus 로고
    • Hypoxic preconditioning induces delayed cardioprotectionthrough p38 MAPK-mediated calreticulin upregulation
    • Wu, X.; Liu, X.; Zhu, X.; Tang, C. Hypoxic preconditioning induces delayed cardioprotectionthrough p38 MAPK-mediated calreticulin upregulation. Shock 2007, 27, 572-577.
    • (2007) Shock , vol.27 , pp. 572-577
    • Wu, X.1    Liu, X.2    Zhu, X.3    Tang, C.4
  • 232
    • 34250311614 scopus 로고    scopus 로고
    • Myocardial protection evoked byhyperoxic exposure involves signaling through nitric oxide and mitogen activated proteinkinases
    • Ruusalepp, A.; Czibik, G.; Flatebo, T.; Vaage, J.; Valen, G. Myocardial protection evoked byhyperoxic exposure involves signaling through nitric oxide and mitogen activated proteinkinases. Basic Res. Cardiol. 2007, 102, 318-326.
    • (2007) Basic Res. Cardiol , vol.102 , pp. 318-326
    • Ruusalepp, A.1    Czibik, G.2    Flatebo, T.3    Vaage, J.4    Valen, G.5
  • 233
    • 27144502042 scopus 로고    scopus 로고
    • Cardioprotection inducedby cardiac-specific overexpression of fibroblast growth factor-2 is mediated by the MAPKcascade
    • House, S. L.; Branch, K.; Newman, G.; Doetschman, T.; Schultz Jel, J. Cardioprotection inducedby cardiac-specific overexpression of fibroblast growth factor-2 is mediated by the MAPKcascade. Am. J. Physiol. Heart Circ. Physiol. 2005, 289, H2167-H2175.
    • (2005) Am. J. Physiol. Heart Circ. Physiol , vol.289
    • House, S.L.1    Branch, K.2    Newman, G.3    Doetschman, T.4    Jel, J.S.5
  • 234
    • 13444256258 scopus 로고    scopus 로고
    • E.;Carretero, O. A. Inhibition of p38 mitogen-activated protein kinase protects the heart againstcardiac remodeling in mice with heart failure resulting from myocardial infarction
    • Liu, Y. H.; Wang, D.; Rhaleb, N. E.; Yang, X. P.; Xu, J.; Sankey, S. S.; Rudolph, A. E.;Carretero, O. A. Inhibition of p38 mitogen-activated protein kinase protects the heart againstcardiac remodeling in mice with heart failure resulting from myocardial infarction. J. Card. Fail.2005, 11, 74-81.
    • (2005) J. Card. Fail , vol.11 , pp. 74-81
    • Liu, Y.H.1    Wang, D.2    Rhaleb, N.E.3    Yang, X.P.4    Xu, J.5    Sankey, S.S.6    Rudolph, A.7
  • 235
    • 0031239584 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 182 ofp38 mitogen-activated protein kinase correlates with the protection of preconditioning in therabbit heart
    • Weinbrenner, C.; Liu, G. S.; Cohen, M. V.; Downey, J. M. Phosphorylation of tyrosine 182 ofp38 mitogen-activated protein kinase correlates with the protection of preconditioning in therabbit heart. J. Mol. Cell. Cardiol. 1997, 29, 2383-2391.
    • (1997) J. Mol. Cell. Cardiol , vol.29 , pp. 2383-2391
    • Weinbrenner, C.1    Liu, G.S.2    Cohen, M.V.3    Downey, J.M.4
  • 236
    • 0030051750 scopus 로고    scopus 로고
    • The role of protein kinases in adaptational growth of theheart
    • Bogoyevitch, M. A.; Sugden, P. H. The role of protein kinases in adaptational growth of theheart. Int. J. Biochem. Cell Biol. 1996, 28, 1-12.
    • (1996) Int. J. Biochem. Cell Biol , vol.28 , pp. 1-12
    • Bogoyevitch, M.A.1    Sugden, P.H.2
  • 238
    • 0036683691 scopus 로고    scopus 로고
    • Structural insight into substrate specificity and regulatorymechanisms of phosphoinositide 3-kinases
    • Djordjevic, S.; Driscoll, P. C. Structural insight into substrate specificity and regulatorymechanisms of phosphoinositide 3-kinases. Trends Biochem. Sci. 2002, 27, 426-432.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 426-432
    • Djordjevic, S.1    Driscoll, P.C.2
  • 239
    • 56549091431 scopus 로고    scopus 로고
    • The complexity of mitogen-activated protein kinases (MAPKs) madesimple
    • Krishna, M.; Narang, H. The complexity of mitogen-activated protein kinases (MAPKs) madesimple. Cell. Mol. Life Sci. 2008, 65, 3525-3544.
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 3525-3544
    • Krishna, M.1    Narang, H.2
  • 240
    • 12844256390 scopus 로고    scopus 로고
    • Overexpression of mitogen-activated protein kinase kinase 6 in theheart improves functional recovery from ischemia in vitro and protects against myocardialinfarction in vivo
    • Martindale, J. J.; Wall, J. A.; Martinez-Longoria, D. M.; Aryal, P.; Rockman, H. A.; Guo, Y.;Bolli, R.; Glembotski, C. C. Overexpression of mitogen-activated protein kinase kinase 6 in theheart improves functional recovery from ischemia in vitro and protects against myocardialinfarction in vivo. J. Biol. Chem. 2005, 280, 669-676.
    • (2005) J. Biol. Chem , vol.280 , pp. 669-676
    • Martindale, J.J.1    Wall, J.A.2    Martinez-Longoria, D.M.3    Aryal, P.4    Rockman, H.A.5    Guo, Y.6    Bolli, R.7    Glembotski, C.C.8
  • 241
  • 242
    • 76649085797 scopus 로고    scopus 로고
    • Alterations of cardiacERK1/2 expression and activity due to volume overload were attenuated by the blockade ofRAS
    • Zhang, W.; Elimban, V.; Xu, Y. J.; Zhang, M.; Nijjar, M. S.; Dhalla, N. S. Alterations of cardiacERK1/2 expression and activity due to volume overload were attenuated by the blockade ofRAS. J. Cardiovasc. Pharmacol. Ther 2010, 15, 84-92.
    • (2010) J. Cardiovasc. Pharmacol. Ther , vol.15 , pp. 84-92
    • Zhang, W.1    Elimban, V.2    Xu, Y.J.3    Zhang, M.4    Nijjar, M.S.5    Dhalla, N.S.6
  • 243
    • 77949655389 scopus 로고    scopus 로고
    • Functional effects of proteinkinases and peroxynitrite on cardiac carnitine palmitoyltransferase-1 in isolated mitochondria
    • Sharma, V.; Abraham, T.; So, A.; Allard, M. F.; McNeill, J. H. Functional effects of proteinkinases and peroxynitrite on cardiac carnitine palmitoyltransferase-1 in isolated mitochondria.Mol. Cell. Biochem. 2010, 337, 223-237.
    • (2010) Mol. Cell. Biochem , vol.337 , pp. 223-237
    • Sharma, V.1    Abraham, T.2    So, A.3    Allard, M.F.4    McNeill, J.H.5
  • 244
    • 0034740521 scopus 로고    scopus 로고
    • Dependence of β1-opioid receptorinducedcardioprotection on a tyrosine kinase-dependent but not a Src-dependent pathway
    • Fryer, R. M.; Wang, Y.; Hsu, A. K.; Nagase, H.; Gross, G. J. Dependence of β1-opioid receptorinducedcardioprotection on a tyrosine kinase-dependent but not a Src-dependent pathway. J.Pharmacol. Exp. Ther. 2001, 299, 477-482.
    • (2001) J. Pharmacol. Exp. Ther , vol.299 , pp. 477-482
    • Fryer, R.M.1    Wang, Y.2    Hsu, A.K.3    Nagase, H.4    Gross, G.J.5
  • 245
    • 0032951513 scopus 로고    scopus 로고
    • Importance of PKC and tyrosine kinase insingle or multiple cycles of preconditioning in rat hearts
    • Fryer, R. M.; Schultz, J. E.; Hsu, A. K.; Gross, G. J. Importance of PKC and tyrosine kinase insingle or multiple cycles of preconditioning in rat hearts. Am. J. Physiol. Cell. Physiol. 1999,276, H1229-H1235.
    • (1999) Am. J. Physiol. Cell. Physiol , vol.276
    • Fryer, R.M.1    Schultz, J.E.2    Hsu, A.K.3    Gross, G.J.4
  • 246
    • 3042785147 scopus 로고    scopus 로고
    • Pretreatment with tyrosine kinase inhibitor attenuates the reduction of apoptosis 24 h afterischemic preconditioning
    • Okubo, S.; Tanabe, Y.; Takeda, K.; Kitayama, M.; Kanemitsu, S.; Kukreja, R. C.; Takekoshi, N.Pretreatment with tyrosine kinase inhibitor attenuates the reduction of apoptosis 24 h afterischemic preconditioning. Jpn. J. Physiol. 2004, 54, 143-151.
    • (2004) Jpn. J. Physiol , vol.54 , pp. 143-151
    • Okubo, S.1    Tanabe, Y.2    Takeda, K.3    Kitayama, M.4    Kanemitsu, S.5    Kukreja, R.C.6    Takekoshi, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.