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Volumn 97, Issue 2, 1996, Pages 533-539

Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice

Author keywords

cardiomyocyte; left ventricular function; overexpression; phospholamban; transgenic

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM ION; ISOPRENALINE; PHOSPHOLAMBAN;

EID: 0030032378     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI118446     Document Type: Article
Times cited : (283)

References (34)
  • 1
    • 0018758359 scopus 로고
    • Mechanism by which cyclic adenosine 3′:'5′-monophosphate-dependent protein kinase stimulates calcium transport in cardiac sarcoplasmic reticulum
    • Hicks, M. J., M. Shigekawa, and A. M. Katz. 1979. Mechanism by which cyclic adenosine 3′:'5′-monophosphate-dependent protein kinase stimulates calcium transport in cardiac sarcoplasmic reticulum. Circ. Res. 44:384-391.
    • (1979) Circ. Res. , vol.44 , pp. 384-391
    • Hicks, M.J.1    Shigekawa, M.2    Katz, A.M.3
  • 3
    • 0016199158 scopus 로고
    • Adenosine 3′:5′: Monophosphate dependent protein kinase-catalyzed phosphorylation reaction and its relationship to calcium-transport in cardiac sarcoplasmic reticulum
    • Kirchberger, M A , M Tada, and A. M. Katz. 1974. Adenosine 3′:5′: monophosphate dependent protein kinase-catalyzed phosphorylation reaction and its relationship to calcium-transport in cardiac sarcoplasmic reticulum. J Biol. Chem. 249:6166-6173
    • (1974) J Biol. Chem. , vol.249 , pp. 6166-6173
    • Kirchberger, M.A.1    Tada, M.2    Katz, A.M.3
  • 4
    • 0018674267 scopus 로고
    • Concerted regulation of cardiac sarcoplasmic reticulum calcium transport by cyclic adenosine monophosphate-dependent and calcium-calmodulin-dependent phosphorylation
    • LePeuch, C. L , J. Haiech, and J G. Demaille. 1979. Concerted regulation of cardiac sarcoplasmic reticulum calcium transport by cyclic adenosine monophosphate-dependent and calcium-calmodulin-dependent phosphorylation Biochemistry. 18.5150-5157.
    • (1979) Biochemistry , vol.18 , pp. 5150-5157
    • LePeuch, C.L.1    Haiech, J.2    Demaille, J.G.3
  • 5
    • 0021279643 scopus 로고
    • Phosphorylation of phospholamban by calcium-activated phospholipid-dependent protein kinase
    • Movsesian, M A., M. Nishikawa, and R. S. Adelstein. 1984. Phosphorylation of phospholamban by calcium-activated phospholipid-dependent protein kinase. J. Biol. Chem. 259:8029-8032.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8029-8032
    • Movsesian, M.A.1    Nishikawa, M.2    Adelstein, R.S.3
  • 7
    • 0022196729 scopus 로고
    • 2+ transport by phosphoprotein phosphatase activity associated with cardiac sarcoplasmic reticulum
    • 2+ transport by phosphoprotein phosphatase activity associated with cardiac sarcoplasmic reticulum. J Biol. Chem 260:11006-11010
    • (1985) J Biol. Chem , vol.260 , pp. 11006-11010
    • Kranias, E.G.1
  • 8
    • 0020477578 scopus 로고
    • Phosphorylation of troponin 1 and phospholamban during catecholamine stimulation of rabbit heart
    • Kranias, E. G , and R. J. Solaro. 1982. Phosphorylation of troponin 1 and phospholamban during catecholamine stimulation of rabbit heart. Nature (Lond.), 298.182-184
    • (1982) Nature (Lond.) , vol.298 , pp. 182-184
    • Kranias, E.G.1    Solaro, R.J.2
  • 11
    • 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. 1994. 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) 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
  • 12
    • 0020637196 scopus 로고
    • Effects of phospholamban phosphorylation catalyzed by adenosine 3′:5′-monophosphate and calmodulin-dependent protein kinases on calcium transport ATPase of cardiac sarcoplasmic reticulum
    • Tada, M., M. Inui, M. Yamada, M. A. Kadoma, T. Kuzuya, H Abe, and S Kakiuchi. 1983. Effects of phospholamban phosphorylation catalyzed by adenosine 3′:5′-monophosphate and calmodulin-dependent protein kinases on calcium transport ATPase of cardiac sarcoplasmic reticulum. J MoL Cell. Cardiol. 15:335-346.
    • (1983) J MoL Cell. Cardiol. , vol.15 , pp. 335-346
    • Tada, M.1    Inui, M.2    Yamada, M.3    Kadoma, M.A.4    Kuzuya, T.5    Abe, H.6    Kakiuchi, S.7
  • 13
    • 0025947645 scopus 로고
    • Dependence of cardiac sarcoplasmic reticulum calcium pump activity on the phosphorylation status of phospholamban
    • Colyer, J., and J H. Wang. 1991. Dependence of cardiac sarcoplasmic reticulum calcium pump activity on the phosphorylation status of phospholamban. J. Biol. Chem. 266:17486-17493
    • (1991) J. Biol. Chem. , vol.266 , pp. 17486-17493
    • Colyer, J.1    Wang, J.H.2
  • 14
    • 0023635288 scopus 로고
    • Phospholamban stoichiometry in canine cardiac muscle sarcoplasmic reticulum
    • Louis, C F., J. Turnquist, and B. Jarvis. 1987. Phospholamban stoichiometry in canine cardiac muscle sarcoplasmic reticulum. Neurosci. Res. 12:937-941.
    • (1987) Neurosci. Res. , vol.12 , pp. 937-941
    • Louis, C.F.1    Turnquist, J.2    Jarvis, B.3
  • 16
    • 0027940368 scopus 로고
    • Myocardial expression of a constitutively active alpha 1B-adrenergic receptor in transgenic mice induces cardiac hypertrophy
    • Milano, C. A., P. C. Dolber, H. A Rockman, R. A Bond, M. E. Venable, L. F. Allen, and R. J. Lefkowitz 1994. Myocardial expression of a constitutively active alpha 1B-adrenergic receptor in transgenic mice induces cardiac hypertrophy. Proc. Natl. Acad Sci. USA 91:10109-10113.
    • (1994) Proc. Natl. Acad Sci. USA , vol.91 , pp. 10109-10113
    • Milano, C.A.1    Dolber, P.C.2    Rockman, H.A.3    Bond, R.A.4    Venable, M.E.5    Allen, L.F.6    Lefkowitz, R.J.7
  • 18
    • 0026342911 scopus 로고
    • Tissue-specific regulation of the α-myosin heavy chain gene promoter in transgenic mice
    • Subramaniam, A., W K. Jones, J. Gulick, S. Wert, J. Neumann, and J. Robbins. 1991. Tissue-specific regulation of the α-myosin heavy chain gene promoter in transgenic mice. J Biol. Chem. 266:24613-24620.
    • (1991) J Biol. Chem. , vol.266 , pp. 24613-24620
    • Subramaniam, A.1    Jones, W.K.2    Gulick, J.3    Wert, S.4    Neumann, J.5    Robbins, J.6
  • 21
    • 0024792640 scopus 로고
    • Identification of transgenic mice carrying the CAT gene with PCR amplification
    • Walter, C. A., D. Nasr-Schirf. and V. J. Luna. 1989 Identification of transgenic mice carrying the CAT gene with PCR amplification. Biotechniques 7:1065-1067.
    • (1989) Biotechniques , vol.7 , pp. 1065-1067
    • Walter, C.A.1    Nasr-Schirf, D.2    Luna, V.J.3
  • 22
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid quanidium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid quanidium thiocyanate-phenol-chloroform extraction. Anal Biochem. 162:156-159.
    • (1987) Anal Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 23
    • 0029076693 scopus 로고
    • Application of the immunoblot technique for quantitation of protein levels in cardiac homogenates
    • Harrer, J. M., E. Kiss, and E. G. Kranias. 1995. Application of the immunoblot technique for quantitation of protein levels in cardiac homogenates. Biotechnigues. 18.995-997.
    • (1995) Biotechnigues , vol.18 , pp. 995-997
    • Harrer, J.M.1    Kiss, E.2    Kranias, E.G.3
  • 24
    • 0028067513 scopus 로고
    • Myosin heavy chain regulation and myocyte contractile depression after LV hypertrophy in aortic-banded mice
    • Dorn, II, G. W., J. Robbins, N. Ball, and R. A. Walsh. 1994. Myosin heavy chain regulation and myocyte contractile depression after LV hypertrophy in aortic-banded mice. Am. J. Physiol. 267.H400-H405.
    • (1994) Am. J. Physiol. , vol.267
    • Dorn II, G.W.1    Robbins, J.2    Ball, N.3    Walsh, R.A.4
  • 26
    • 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. 1995. In vivo echocardiographic detection of enhanced left ventricular function in gene-targeted mice with phospholamban deficiency. Circ Res 77:632-637.
    • (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
  • 27
    • 0016193316 scopus 로고
    • Estimating the functional capabilities of sarcoplasmic reticulum in cardiac muscle
    • Solaro, R. J., and F. N. Briggs. 1974. Estimating the functional capabilities of sarcoplasmic reticulum in cardiac muscle. Circ. Res 34:531-540.
    • (1974) Circ. Res , vol.34 , pp. 531-540
    • Solaro, R.J.1    Briggs, F.N.2
  • 28
    • 0029091777 scopus 로고
    • Differential phospholamban gene expression in murine cardiac compartment: Molecular and physiological analyses
    • Koss, K. L , S Ponniah, W K. Jones, I. L. Grupp, and E. G. Kranias. 1995 Differential phospholamban gene expression in murine cardiac compartment: molecular and physiological analyses Circ. Res. 77:342-353.
    • (1995) Circ. Res. , vol.77 , pp. 342-353
    • Koss, K.L.1    Ponniah, S.2    Jones, W.K.3    Grupp, I.L.4    Kranias, E.G.5
  • 30
    • 0029074341 scopus 로고
    • Mechanisms, diagnosis, and treatment of diastolic heart failure
    • Lenihan, D J., M. C. Gerson, B. D. Hoit, and R. A Walsh, 1995. Mechanisms, diagnosis, and treatment of diastolic heart failure. Am. Heart J. 130: 153-156.
    • (1995) Am. Heart J. , vol.130 , pp. 153-156
    • Lenihan, D.J.1    Gerson, M.C.2    Hoit, B.D.3    Walsh, R.A.4
  • 31
    • 0023957833 scopus 로고
    • Phosphorylation of C-protein. troponin I and phospholamban in isolated rabbit hearts
    • Garvey, J. L , E. G Kranias, and R. J Solaro. 1988. Phosphorylation of C-protein. troponin I and phospholamban in isolated rabbit hearts. Biochem. J. 249:709-714.
    • (1988) Biochem. J. , vol.249 , pp. 709-714
    • Garvey, J.L.1    Kranias, E.G.2    Solaro, R.J.3
  • 32
    • 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. 1985. Isoproterenol-induced phosphorylation of a 15-kilodalton sarcolemmal protein in intact myocardium. J. Biol Chem. 260.3860-3867.
    • (1985) J. Biol Chem. , vol.260 , pp. 3860-3867
    • Presti, C.F.1    Jones, L.R.2    Lindemann, J.P.3
  • 33
    • 0028088886 scopus 로고
    • Role of sarcoplasmic reticulum in loss of load-sensitive relaxation in pressure overload cardiac hypertrophy
    • Cory, C. R., R. W. Grange, and M. E. Houston 1994. Role of sarcoplasmic reticulum in loss of load-sensitive relaxation in pressure overload cardiac hypertrophy. Am J Physiol. 266:H68-H78.
    • (1994) Am J Physiol. , vol.266
    • Cory, C.R.1    Grange, R.W.2    Houston, M.E.3


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