Skip Navigation

European Heart Journal 1991 12(Supplement F):143-144; doi:10.1093/eurheartj/12.suppl_F.143
Copyright © 1991 by the European Society of Cardiology.
This Article
Right arrow Full Text (PDF)
Right arrow E-letters: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when E-letters are posted
Right arrow Alert me if a correction is posted
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Edes, I.
Right arrow Articles by Kranias, E. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Edes, I.
Right arrow Articles by Kranias, E. G.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 1991 The European Society of Cardiology

The effect of {alpha}-adrenergic agents and protein kinase C activators on protein phosphorylation in isolated guinea pig hearts

I. Edes*, L. Talosi{dagger} and E. G. Kranias{dagger}

* 2nd Department of Medicine, Albert Szent-Gyorgyi Medical University Szeged, Hungary
{dagger} Department of Pharmacology and Cell Biophysics, University of Cincinnati, College of Medicine Cincinnati, Ohio, U.S.A.

Correspondence: Istvan Edes MD 2nd Department of Medicine, Albert Szent-Gyorgyi Medical University H-6701 Szeged, P.O. Box 480, Hungary

The incorporation of [32P]Pi into sarcolcmmal, sarcoplasmic reticular and myofibrillar proteins was studied in Langendorff-perfused guinea pig hearts treated with the {alpha}-agonist norepinephrine or with protein kinase C activators (phorbol 12-myristate 13-acetate (PMA) or 1,2-dioctanoylglycerol (D8G)). Norepinephrine was administered in the presence of propranolol and atropine, while the protein kinase C activators (PMA and D8G) were infused in the presence of propranolol, atropine and prazosin. Examination of 32P-incorporation into the various cardiac proteins revealed that there were no significant increases in the degree of phosphorylation of the: (1) 15kDa sarcolemmal protein; (2) phospholamban in sarcoplasmic reticulum; and (3) troponin I and C protein in the myofibrib. In parallel control studies, stimulation of beating guinea pig hearts by isoproterenol was associated with a 4–5-fold increase in 32P-incorporation into phospholamban and troponin I and about a 2-fold increase in 32P-incorporation into C protein and the 15kDa sarcolemmal protein. These findings indicate that the major cardiac regulatory phosphoproteins, which have been reported to serve as substrates for protein kinase C in vitro, are not phosphorylated by the same enzyme in perfused, beating guinea pig hearts.

Key Words: Protein phosphorylation • adrenergic receptors • protein kinase C


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Cardiovasc ResHome page
S. T Rapundalo
Cardiac protein phosphorylation: functional and pathophysiological correlates
Cardiovasc Res, June 1, 1998; 38(3): 559 - 588.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.