AJP - Heart Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Heart Circ Physiol 264: H791-H797, 1993;
0363-6135/93 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Talosi, L.
Right arrow Articles by Kranias, E. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Talosi, L.
Right arrow Articles by Kranias, E. G.

AJP - Heart and Circulatory Physiology, Vol 264, Issue 3 791-H797, Copyright © 1993 by American Physiological Society


ARTICLES

Intracellular mechanisms mediating reversal of beta-adrenergic stimulation in intact beating hearts

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:


Home page
J. Biol. Chem.Home page
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]


Home page
Am. J. Physiol. Heart Circ. Physiol.Home page
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]


Home page
Am. J. Physiol. Heart Circ. Physiol.Home page
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]


Home page
Physiol. Rev.Home page
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]


Home page
J. Biol. Chem.Home page
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]


Home page
Circ. Res.Home page
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]


Home page
Circ. Res.Home page
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]


Home page
Circ. Res.Home page
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]


Home page
Circ. Res.Home page
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]


Home page
J. Biol. Chem.Home page
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]


Home page
J. Biol. Chem.Home page
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