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Volumn 272, Issue 2 41-2, 1997, Pages

β-Adrenergic regulation of cAMP and protein phosphorylation in phospholamban-knockout mouse hearts

Author keywords

C protein; troponin I; agonist

Indexed keywords

CYCLIC AMP; ISOPRENALINE; PHOSPHOLAMBAN;

EID: 33750879037     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.1997.272.2.h785     Document Type: Article
Times cited : (49)

References (28)
  • 1
    • 0023459463 scopus 로고
    • Regulation of cardiac sarcoplasmic reticulum function by phospholamban
    • Edes, I., and E. G. Kranias. Regulation of cardiac sarcoplasmic reticulum function by phospholamban. Membr. Biochem. 7: 175-192, 1989.
    • (1989) Membr. Biochem. , vol.7 , pp. 175-192
    • Edes, I.1    Kranias, E.G.2
  • 2
    • 0025315239 scopus 로고
    • Phospholamban and troponin I are substrates for protein kinase C in vitro but not in intact beating guinea pig hearts
    • Edes, I., and E. G. Kranias. Phospholamban and troponin I are substrates for protein kinase C in vitro but not in intact beating guinea pig hearts. Circ. Res. 67: 394-400, 1990.
    • (1990) Circ. Res. , vol.67 , pp. 394-400
    • Edes, I.1    Kranias, E.G.2
  • 3
    • 0024432512 scopus 로고
    • Changes in phosphoinositide turnover in isolated guinea pig hearts stimulated with isoproterenol
    • Edes, I., R. J. Solaro, and E. G. Kranias. Changes in phosphoinositide turnover in isolated guinea pig hearts stimulated with isoproterenol. Circ. Res. 65: 989-996, 1989.
    • (1989) Circ. Res. , vol.65 , pp. 989-996
    • Edes, I.1    Solaro, R.J.2    Kranias, E.G.3
  • 4
    • 0025835948 scopus 로고
    • The effect of α-adrenergic agents and phorbol esters on the phosphorylation of sarcolemmal proteins in beating guinea pig hearts
    • Edes, I., L. Talosi, and E. G. Kranias. The effect of α-adrenergic agents and phorbol esters on the phosphorylation of sarcolemmal proteins in beating guinea pig hearts. Cardiovasc. Res. 25: 510-515, 1991.
    • (1991) Cardiovasc. Res. , vol.25 , pp. 510-515
    • Edes, I.1    Talosi, L.2    Kranias, E.G.3
  • 5
    • 0027519404 scopus 로고
    • 2-adrenergic receptor within the fourth transmembrane domain alters ligand binding and functional properties of the receptor
    • 2-adrenergic receptor within the fourth transmembrane domain alters ligand binding and functional properties of the receptor. J. Biol. Chem. 268: 23116-23121, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23116-23121
    • Green, S.A.1    Cole, G.2    Jacinto, M.3    Innis, M.4    Liggett, S.B.5
  • 6
    • 0022358078 scopus 로고
    • Effects of phosphorylated and unphosphorylated C-protein on cardiac actomyosin ATPase
    • Hartzell, H. C. Effects of phosphorylated and unphosphorylated C-protein on cardiac actomyosin ATPase. J. Mol. Biol. 186: 185-195, 1985.
    • (1985) J. Mol. Biol. , vol.186 , pp. 185-195
    • Hartzell, H.C.1
  • 7
    • 0029154871 scopus 로고
    • In vivo echocardiographic detection of enhanced left ventricular function in gene-targeted mice with phospholamban deficiency
    • Hoit, B. D., S. F. Khoury, E. G. Kranias, N. Ball, and R. A. Walsh. In vivo echocardiographic detection of enhanced left ventricular function in gene-targeted mice with phospholamban deficiency. Circ. Res. 77: 632-637, 1995.
    • (1995) Circ. Res. , vol.77 , pp. 632-637
    • Hoit, B.D.1    Khoury, S.F.2    Kranias, E.G.3    Ball, N.4    Walsh, R.A.5
  • 9
    • 0018615366 scopus 로고
    • Phosphorylation of the 19,000 dalton light chain of myosin in perfused rat heart under the influence of negative and positive inotropic agents
    • Kopp, S. J., and M. Barany. Phosphorylation of the 19,000 dalton light chain of myosin in perfused rat heart under the influence of negative and positive inotropic agents. J. Biol. Chem. 254: 12007-12012, 1979.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12007-12012
    • Kopp, S.J.1    Barany, M.2
  • 10
    • 0021992245 scopus 로고
    • Phosphorylation and functional modifications of sarcoplasmic reticulum and myofibrils in isolated rabbit hearts stimulated with isoprenaline
    • Kranias, E. G., J. L. Garvey, R. D. Srivastava, and R. J. Solaro. Phosphorylation and functional modifications of sarcoplasmic reticulum and myofibrils in isolated rabbit hearts stimulated with isoprenaline. Biochem. J. 226: 113-121, 1985.
    • (1985) Biochem. J. , vol.226 , pp. 113-121
    • Kranias, E.G.1    Garvey, J.L.2    Srivastava, R.D.3    Solaro, R.J.4
  • 11
    • 0020477578 scopus 로고
    • Phosphorylation of troponin I and phospholamban during catecholamine stimulation of rabbit heart
    • Kranias, E. G., and R. J. Solaro. Phosphorylation of troponin I and phospholamban during catecholamine stimulation of rabbit heart. Nature Lond. 298: 182-184, 1982.
    • (1982) Nature Lond. , vol.298 , pp. 182-184
    • Kranias, E.G.1    Solaro, R.J.2
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature Lond. 227: 680-685, 1970.
    • (1970) Nature Lond. , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0023028739 scopus 로고
    • α-Adrenergic stimulation of sarcolemmal protein phosphorylation and slow response in intact myocardium
    • Lindemann, J. P. α-Adrenergic stimulation of sarcolemmal protein phosphorylation and slow response in intact myocardium. J. Biol. Chem. 261: 4860-4867, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4860-4867
    • Lindemann, J.P.1
  • 15
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of β-agonist stimulation
    • Luo, W., I. L. Grupp, J. Harrer, S. Ponniah, G. Grupp, J. J. Duffy, T. Doetschman, and E. G. Kranias. Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of β-agonist stimulation. Circ. Res. 75: 401-409, 1994.
    • (1994) Circ. Res. , vol.75 , pp. 401-409
    • Luo, W.1    Grupp, I.L.2    Harrer, J.3    Ponniah, S.4    Grupp, G.5    Duffy, J.J.6    Doetschman, T.7    Kranias, E.G.8
  • 16
    • 0025848016 scopus 로고
    • Purification and complete sequence determination of the major plasma membrane substrate for cAMP-dependent protein kinase and protein kinase C in myocardium
    • Palmer, C. J., B. T. Scott, and L. R. Jones. Purification and complete sequence determination of the major plasma membrane substrate for cAMP-dependent protein kinase and protein kinase C in myocardium. J. Biol. Chem. 266: 11126-11130, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11126-11130
    • Palmer, C.J.1    Scott, B.T.2    Jones, L.R.3
  • 17
    • 0021987578 scopus 로고
    • Isoproterenol-induced phosphorylation of a 15-kilodalton sarcolemmal protein in intact myocardium
    • Presti, C. F., L. R. Jones, and J. P. Lindemann. Isoproterenol-induced phosphorylation of a 15-kilodalton sarcolemmal protein in intact myocardium. J. Biol. Chem. 260: 3860-3867, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3860-3867
    • Presti, C.F.1    Jones, L.R.2    Lindemann, J.P.3
  • 18
    • 0022402480 scopus 로고
    • Identification of an endogenous protein kinase C activity and its intrinsic 15 kDa substrate in purified canine cardiac sarcolemmal vesicles
    • Presti, C. F., B. T. Scott, and L. R. Jones. Identification of an endogenous protein kinase C activity and its intrinsic 15 kDa substrate in purified canine cardiac sarcolemmal vesicles. J. Biol. Chem. 260: 13879-13889, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13879-13889
    • Presti, C.F.1    Scott, B.T.2    Jones, L.R.3
  • 20
    • 0015716692 scopus 로고
    • A rapid, sensitive and specific method for the determination of protein in dilute solution
    • Schaffner, W., and C. Weisman. A rapid, sensitive and specific method for the determination of protein in dilute solution. Anal. Biochem. 56: 502-514, 1973.
    • (1973) Anal. Biochem. , vol.56 , pp. 502-514
    • Schaffner, W.1    Weisman, C.2
  • 21
    • 0015213029 scopus 로고
    • The purification of cardiac myofibrils with Triton X-100
    • Solaro, R. J., D. C. Pang, and F. N. Briggs. The purification of cardiac myofibrils with Triton X-100. Biochim. Biophys. Acta 245: 259-262, 1971.
    • (1971) Biochim. Biophys. Acta , vol.245 , pp. 259-262
    • Solaro, R.J.1    Pang, D.C.2    Briggs, F.N.3
  • 22
    • 0026089312 scopus 로고
    • Regulation of the cardiac ryanodine receptor by protein kinase-dependent phosphorylation
    • Takasago, T., T. Imagawa, K. Furukawa, T. Orgurusu, and M. Shigekawa. Regulation of the cardiac ryanodine receptor by protein kinase-dependent phosphorylation. J. Biochem. 109: 163-170, 1991.
    • (1991) J. Biochem. , vol.109 , pp. 163-170
    • Takasago, T.1    Imagawa, T.2    Furukawa, K.3    Orgurusu, T.4    Shigekawa, M.5
  • 23
    • 0027480875 scopus 로고
    • Intracellular mechanism mediating the reversal of β-adrenergic stimulation in beating hearts
    • Heart Circ. Physiol. 33
    • Talosi, L., I. Edes, and E. G. Kranias. Intracellular mechanism mediating the reversal of β-adrenergic stimulation in beating hearts. Am. J. Physiol. 264 (Heart Circ. Physiol. 33): H791-H797, 1993.
    • (1993) Am. J. Physiol. , vol.264
    • Talosi, L.1    Edes, I.2    Kranias, E.G.3
  • 25
    • 0025273128 scopus 로고
    • Regulation of cardiac L-type calcium current by phosphorylation and G proteins
    • Trautwein, W., and J. Hescheler. Regulation of cardiac L-type calcium current by phosphorylation and G proteins. Annu. Rev. Physiol. 52: 257-274, 1990.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 257-274
    • Trautwein, W.1    Hescheler, J.2
  • 28
    • 0029037870 scopus 로고
    • Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation
    • Zhang, R., J. Zhao, A. Mandveno, and J. D. Potter. Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation. Circ. Res. 76: 1028-1035, 1995.
    • (1995) Circ. Res. , vol.76 , pp. 1028-1035
    • Zhang, R.1    Zhao, J.2    Mandveno, A.3    Potter, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.