Document Detail


Phosphorylation of high-Mr caldesmon by protein kinase C modulates the regulatory function of this protein on the interaction between actin and myosin.
MedLine Citation:
PMID:  2139605     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
High-Mr caldesmon, which is involved in smooth muscle contraction, was phosphorylated by protein kinase C. By chymotryptic digestion, actin- and calmodulin-binding assays and immunoprecipitation with the antibody to the C-terminal 35-kDa fragment, we have identified that all phosphate groups are incorporated exclusively into this fragment, which is the functional domain for binding actin and calmodulin. Phosphorylation of high-Mr caldesmon and its C-terminal 35-kDa fragment reduced their binding abilities to both F-actin and calmodulin. Further, their inhibitory effects on the actin-activated ATPase activity of gizzard myosin were also reversed in proportion to the degree of phosphorylation. These results suggest that phosphorylation of high-Mr caldesmon by protein kinase C, which is restricted within the C-terminal 35-kDa domain, results in the modulation of its activity in the smooth muscle actin--myosin interaction.
Authors:
T Tanaka; H Ohta; K Kanda; T Tanaka; H Hidaka; K Sobue
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  188     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1990 Mar 
Date Detail:
Created Date:  1990-06-01     Completed Date:  1990-06-01     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  495-500     Citation Subset:  IM    
Affiliation:
Department of Neuropharmacology and Neurochemistry, Osaka University Medical School, Japan.
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MeSH Terms
Descriptor/Qualifier:
Actins / metabolism,  pharmacology
Animals
Binding Sites / drug effects
Calmodulin / metabolism,  pharmacology
Calmodulin-Binding Proteins / metabolism*,  pharmacology,  physiology
Chickens
Chymotrypsin / pharmacology
Enzyme Activation / drug effects
Gizzard
Myosins / antagonists & inhibitors,  metabolism*
Phosphopeptides / analysis
Phosphorylation
Protein Kinase C / metabolism*
Tropomyosin / pharmacology
Chemical
Reg. No./Substance:
0/Actins; 0/Calmodulin; 0/Calmodulin-Binding Proteins; 0/Phosphopeptides; 0/Tropomyosin; EC 2.7.11.13/Protein Kinase C; EC 3.4.21.1/Chymotrypsin; EC 3.6.4.1/Myosins

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


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