|
|
||||||||
AJP - Heart and Circulatory Physiology, Vol 264, Issue 3 791-H797, Copyright © 1993 by American Physiological Society
ARTICLES |
L. Talosi, I. Edes and E. G. Kranias
Department of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, Ohio 45267-0575.
The changes in 32P labeling of phosphoproteins were studied in Langendorff-perfused guinea pig hearts during reversal of the stimulatory effects of isoproterenol. Exposure of the hearts to isoproterenol was associated with significant increases in adenosine 3',5'-cyclic monophosphate (cAMP) levels and in the phosphate incorporation into phospholamban in sarcoplasmic reticulum, the 15-kDa protein in the sarcolemma, and troponin I in the myofibrils. Phospholamban was phosphorylated on serine and threonine residues, both of which are sites for cAMP-dependent and Ca(2+)-calmodulin-dependent protein kinases, respectively. Termination of isoproterenol infusion was associated with reversal of the mechanical effects of isoproterenol stimulation and reversal of the increases in tissue cAMP levels. However, the decreases in cAMP levels correlated only with dephosphorylation of phosphoserine in phospholamban. Dephosphorylation of phosphothreonine in phospholamban, the 15-kDa sarcolemmal protein, and troponin I occurred at a slower rate. These findings suggest that cAMP-dependent phosphorylation of phospholamban (phosphoserine) may play a prominent role during beta-adrenergic stimulation of intact hearts.
This article has been cited by other articles:
![]() |
A. G. Brittsan, A. N. Carr, A. G. Schmidt, and E. G. Kranias Maximal Inhibition of SERCA2 Ca2+ Affinity by Phospholamban in Transgenic Hearts Overexpressing a Non-phosphorylatable Form of Phospholamban J. Biol. Chem., April 14, 2000; 275(16): 12129 - 12135. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. Li, J. Desantiago, G. Chu, E. G. Kranias, and D. M. Bers Phosphorylation of phospholamban and troponin I in beta -adrenergic-induced acceleration of cardiac relaxation Am J Physiol Heart Circ Physiol, March 1, 2000; 278(3): H769 - H779. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Kuschel, P. Karczewski, P. Hempel, W.-P. Schlegel, E.-G. Krause, and S. Bartel Ser16 prevails over Thr17 phospholamban phosphorylation in the beta -adrenergic regulation of cardiac relaxation Am J Physiol Heart Circ Physiol, May 1, 1999; 276(5): H1625 - H1633. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. K. B. SIMMERMAN and L. R. JONES Phospholamban: Protein Structure, Mechanism of Action, and Role in Cardiac Function Physiol Rev, October 1, 1998; 78(4): 921 - 947. [Abstract] [Full Text] [PDF] |
||||
![]() |
W. Luo, G. Chu, Y. Sato, Z. Zhou, V. J. Kadambi, and E. G. Kranias Transgenic Approaches to Define the Functional Role of Dual Site Phospholamban Phosphorylation J. Biol. Chem., February 20, 1998; 273(8): 4734 - 4739. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. Chu, G. W. Dorn II, W. Luo, J. M. Harrer, V. J. Kadambi, R. A. Walsh, and E. G. Kranias Monomeric Phospholamban Overexpression in Transgenic Mouse Hearts Circ. Res., October 19, 1997; 81(4): 485 - 492. [Abstract] [Full Text] |
||||
![]() |
K. L. Koss and E. G. Kranias Phospholamban: A Prominent Regulator of Myocardial Contractility Circ. Res., December 1, 1996; 79(6): 1059 - 1063. [Full Text] |
||||
![]() |
I. Edes, E. Kiss, Y. Kitada, F. M. Powers, J. G. Papp, E. G. Kranias, and R. J. Solaro Effects of Levosimendan, a Cardiotonic Agent Targeted to Troponin C, on Cardiac Function and on Phosphorylation and Ca2+ Sensitivity of Cardiac Myofibrils and Sarcoplasmic Reticulum in Guinea Pig Heart Circ. Res., July 1, 1995; 77(1): 107 - 113. [Abstract] [Full Text] |
||||
![]() |
R. Zhang, J. Zhao, A. Mandveno, and J. D. Potter Cardiac Troponin I Phosphorylation Increases the Rate of Cardiac Muscle Relaxation Circ. Res., June 1, 1995; 76(6): 1028 - 1035. [Abstract] [Full Text] |
||||
![]() |
D. Hagemann, M. Kuschel, T. Kuramochi, W. Zhu, H. Cheng, and R.-P. Xiao Frequency-encoding Thr17 Phospholamban Phosphorylation Is Independent of Ser16 Phosphorylation in Cardiac Myocytes J. Biol. Chem., July 14, 2000; 275(29): 22532 - 22536. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. Chu, J. W. Lester, K. B. Young, W. Luo, J. Zhai, and E. G. Kranias A Single Site (Ser16) Phosphorylation in Phospholamban Is Sufficient in Mediating Its Maximal Cardiac Responses to beta -Agonists J. Biol. Chem., December 1, 2000; 275(49): 38938 - 38943. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Visit Other APS Journals Online |