Document Detail

Cyclic AMP-dependent phosphorylation of a 16 kDa protein in a plasma membrane-enriched fraction of rat aortic myocytes.
MedLine Citation:
PMID:  4065343     Owner:  NLM     Status:  MEDLINE    
Phosphorylation induced by cAMP-dependent protein kinase was examined in a plasma membrane-enriched fraction from control and beta-adrenergic-stimulated rat aortic myocytes. Phosphorylation of a 16 kDa protein which copurified with the plasma membrane marker (Na+ + K+)-ATPase was most prominent. It was decreased by pretreatment of the myocytes with isoproterenol and the effect of isoproterenol was inhibited by propranolol. Both phosphorylation induced by cAMP-dependent protein kinase and its inhibition by isoproterenol pretreatment declined in preparations exposed to endogenous phosphatase. These results provide strong evidence that beta-adrenergic stimulation of aortic myocytes induces in situ phosphorylation of a 16 kDa plasma membrane protein.
C Boulanger-Saunier; D M Kattenburg; J C Stoclet
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  193     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1985 Dec 
Date Detail:
Created Date:  1986-01-21     Completed Date:  1986-01-21     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  283-8     Citation Subset:  IM    
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MeSH Terms
Aorta / metabolism
Cell Membrane / metabolism
Isoproterenol / antagonists & inhibitors,  pharmacology
Membrane Proteins / metabolism*
Muscle, Smooth, Vascular / metabolism*
Propranolol / pharmacology
Protein Kinases / metabolism*
Rats, Inbred Strains
Reg. No./Substance:
0/Membrane Proteins; 525-66-6/Propranolol; 7683-59-2/Isoproterenol; EC 2.7.-/Protein Kinases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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