Phospholamban: A major determinant of the cardiac force-frequency relationship

American Journal of Physiology - Heart and Circulatory Physiology

Volumn 278, Issue 1 47-1, 2000, Pages

  Bluhm, Wolfgang F ^a   Kranias, Evangelia G ^b   Dillmann, Wolfgang H ^a   Meyer, Markus ^a,c  

^a UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

^b UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Knockout mice; Papillary muscles; Rapid cooling contractures; Twitch acceleration

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CYCLOPIAZONIC ACID; PHOSPHOLAMBAN;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; HEART MUSCLE CONTRACTILE FORCE; HEART MUSCLE CONTRACTILITY; HEART PAPILLARY MUSCLE; HEART RATE; KNOCKOUT MOUSE; MOUSE; MUSCLE LENGTH; MUSCLE TWITCH; NONHUMAN; PRIORITY JOURNAL; SARCOPLASMIC RETICULUM;

EID: 0033969489     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.2000.278.1.h249     Document Type: Article

References (33)

1. 2+ release in cardiac muscle activation during postrest recovery. Am. J. Physiol. Heart Circ. Physiol. 248: H366-H381, 1985.
2. 2+ loading in cardiac muscle preparations based on rapid-cooling contractures. Am. J. Physiol. Cell Physiol. 256: C109-C0120, 1989.
3. Bers, D. M., R. A. Bassani, J. W. Bassani, S. Baudet, and L. V. Hryshko. Paradoxical twitch potentiation after rest in cardiac muscle: increased fractional release of SR calcium. J. Mol. Cell. Cardiol. 25: 1047-1057, 1993.
4. Bluhm, W. F., and W. Y. W. Lew. Sarcoplasmic reticulum in cardiac length-dependent activation in rabbits. Am. J. Physiol. Heart Circ. Physiol. 269: H965-H972, 1995.
5. Bluhm, W. F., M. Meyer, E. A. Swanson, and W. H. Dillmann. Postrest potentiation of active force in mouse papillary muscles is greatly accelerated by increased stimulus frequency. Ann. NY Acad. Sci. 853: 304-307, 1998.
6. Bowditch, H. P. Über die Eigentümlichkeiten der Reizbarkeit, welche die Muskelfasern des Herzens zeigen. Ber. Sächs. Akad. Wiss. 23: 652-689, 1871.
7. Cohen, C. J., H. A. Fozzard, and S. S. Sheu. Increase in intracellular sodium ion activity during stimulation in mammalian cardiac muscle. Circ. Res. 50: 651-662, 1982.
8. Gwathmey, J. K., M. T. Slawsky, R. J. Hajjar, G. M. Briggs, and J. P. Morgan. Role of intracellular calcium handling in force-interval relationships of human ventricular myocardium. J. Clin. Invest. 85: 1599-1613, 1990.
9. 2+-ATPaSe in failing and nonfailing human myocardium. Circ. Res. 75: 434-442, 1994.
10. 2+ ATPase gene in the heart of transgenic mice accelerates calcium transients and cardiac relaxation. J. Clin. Invest. 100: 380-389, 1997.
11. 2+ transient in rat heart is independent of phospholamban phosphorylation. Am. J. Physiol. Heart Circ. Physiol. 273: H695-H706, 1997.
12. 2+ pump of sarcoplasmic reticulum. Nature 342: 90-92, 1989.
13. Kiss, E., I. Edes, Y. Sato, W. Luo, S. B. Liggett, and E. G. Kranias. β-Adrenergic regulation of cAMP and protein phosphorylation in phospholamban-knockout mouse hearts. Am. J. Physiol. Heart Circ. Physiol. 272: H785-H790, 1997.
14. Koch-Weser, J., and J. R. Blinks. The influence of the interval between beats on myocardial contractility. Pharmocol. Rev. 15: 601-652, 1963.
15. Koss, K. L., I. L. Grupp, and E. G. Kranias. The relative phospholamban and SERCA2 ratio: a critical determinant of myocardial contractility. Basic Res. Cardiol. 92: 17-24, 1997.
16. Koss, K. L., and E. G. Kranias. Phospholamban: a prominent regulator of myocardial contractility. Circ. Res. 79: 1059-1063, 1996.
17. 2+ transients and relaxation in mammalian cardiac muscle. Jpn. Circ. J. 46: 39-43, 1982.
18. 2+]i-frequency relationships in rat ventricular trabeculae at physiological frequencies. Am. J. Physiol. Heart Circ. Physiol. 276: H9-H18, 1999.
19. Lewartowski, B., and B. Pytkowski. Cellular mechanism of the relationship between myocardial force and frequency of contractions. Prog. Biophys. Mol. Biol. 50: 97-120, 1987.
20. Li, L., G. Chu, E. G. Kranias, and D. M. Bers. Cardiac myocyte calcium transport in phospholamban knockout mouse: relaxation and endogenous CaMKII effects. Am. J. Physiol. Heart Circ. Physiol. 274: H1335-H1347, 1998.
21. Lompré, A. M., M. Anger, and D. Levitsky. Sarco(endo)plasmic reticulum calcium pumps in the cardiovascular system: function and gene expression. J. Mol. Cell. Cardiol. 26: 1109-1121, 1994.
22. Lorenz, J. N., and E. G. Kranias. Regulatory effects of phospholamban on cardiac function in intact mice. Am. J. Physiol. Heart Circ. Physiol. 273: H2826-H2831, 1997.
23. 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 beta-agonist stimulation. Circ. Res. 75: 401-409, 1994.
24. Luo, W., B. M. Wolska, I. L. Grupp, J. M. Harrer, K. Haghighi, D. G. Ferguson, J. P. Slack, G. Grupp, T. Doetschman, R. J. Solaro, and E. G. Kranias. Phospholamban gene dosage effects in the mammalian heart. Circ. Res. 78: 839-847, 1996.
25. Lüss, I., P. Boknik, L. R. Jones, U. Kirchhefer, J. Knapp, B. Linck, H. Lüss, A. Meissner, F. U. Müller, W. Schmitz, U. Vahlensieck, and J. Neumann. Expression of cardiac calcium regulatory proteins in atrium v ventricle in different species. J. Mol. Cell. Cardiol. 31: 1299-1314, 1999.
26. 2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature 316: 696-700, 1985.
27. Meyer, M., W. F. Bluhm, H. He, S. R. Post, F. J. Giordano, W. Y. W. Lew, and W. H. Dillmann. Phospholamban-to-SERCA2 ratio controls the force-frequency relationship. Am. J. Physiol. Heart Circ. Physiol. 276: H779-H785, 1999.
28. Mulieri, L. A., G. Hasenfuss, B. Leavitt, P. D. Allen, and N. R. Alpert. Altered myocardial force-frequency relation in human heart failure. Circulation 85: 1743-1750, 1992.
29. Ross, J., Jr., T. Miura, M. Kambayashi, G. P. Eising, and K. H. Ryu. Adrenergic control of the force-frequency relation. Circulation 92: 2327-2332, 1995.
30. Santana, L. F., E. G. Kranias, and W. J. Lederer. Calcium sparks and excitation-contraction coupling in phospholamban-deficient mouse ventricular myocytes. J. Physiol. (Lond.) 503: 21-29, 1997.
31. Simmerman, H. K., J. H. Collins, J. L. Theibert, A. D. Wegener, and L. R. Jones. Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains. J. Biol. Chem. 261: 13333-13341, 1986.
32. Tada, M., M. A. Kirchberger, D. I. Repke, and A. M. Katz. The stimulation of calcium transport in cardiac sarcoplasmic reticulum by adenosine 3′:5′-monophosphate-dependent protein kinase. J. Biol. Chem. 249: 6174-6180, 1974.
33. 2+. Am. J. Physiol. Cell Physiol. 271: C391-C397, 1996.