Document Detail

Alterations in protein kinase C isoenzyme expression and autophosphorylation during the progression of pressure overload-induced left ventricular hypertrophy.
MedLine Citation:
PMID:  12619877     Owner:  NLM     Status:  MEDLINE    
Cardiomyocytes express several isoenzymes of protein kinase C (PKC), which as a group have been implicated in the induction of left ventricular hypertrophy (LVH) and its transition to heart failure. Individual PKC isoenzymes also require transphosphorylation and autophosphorylation for enzymatic activity. To determine whether PKC isoenzyme expression and autophosphorylation are altered during LVH progression in vivo, suprarenal abdominal aortic coarctation was performed in Sprague-Dawley rats. Quantitative Western blotting was performed on LV tissue 1, 8 and 24 weeks after aortic banding, using antibodies specific for total PKCalpha, PKCdelta and PKCepsilon, and their C-terminal autophosphorylation sites. Aortic banding produced sustained hypertension and gradually developing LVH that progressed to diastolic heart failure over time. PKCepsilon levels and autophosphorylation were not significantly different from sham-operated controls during any stage of LVH progression. PKCalpha expression levels were also unaffected during the induction of LVH, but increased 3.2 +/- 0.8 fold during the transition to heart failure. In addition, there was a high degree of correlation between PKCalpha levels and the degree of LVH in 24 week banded animals. However, autophosphorylated PKCalpha was not increased at any time point. In contrast, PKCdelta autophosphorylation was increased prior to the development of LVH, and also during the transition to heart failure. The increased PKCdelta autophosphorylation in 1 week banded rats was not accompanied by an increase in total PKCdelta, whereas total PKCdelta levels were markedly increased (6.0 +/- 1.7 fold) in 24 week banded animals. Furthermore, both phosphorylated and total PKCdelta levels were highly correlated with the degree of LVH in 24 week banded rats. In summary, we provide indirect evidence to indicate that PKCdelta may be involved in the induction of pressure overload LVH, whereas both PKCdelta and PKCalpha may be involved in the transition to heart failure.
Allison L Bayer; Maria C Heidkamp; Nehu Patel; Michael Porter; Steve Engman; Allen M Samarel
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular and cellular biochemistry     Volume:  242     ISSN:  0300-8177     ISO Abbreviation:  Mol. Cell. Biochem.     Publication Date:  2003 Jan 
Date Detail:
Created Date:  2003-03-06     Completed Date:  2003-10-15     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0364456     Medline TA:  Mol Cell Biochem     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  145-52     Citation Subset:  IM    
The Cardiovascular Institute and Department of Physiology, Loyola University Chicago Stritch School of Medicine, Maywood, IL 60153, USA.
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MeSH Terms
Disease Models, Animal
Disease Progression
Electrophoresis, Polyacrylamide Gel
Gene Expression Regulation, Enzymologic*
Hypertension / complications,  enzymology
Hypertrophy, Left Ventricular / complications,  enzymology*,  etiology*
Isoenzymes / metabolism
Myocardial Contraction
Pressure / adverse effects*
Protein Kinase C / metabolism*
Protein Kinase C-alpha
Protein Kinase C-delta
Protein Kinase C-epsilon
Rats, Sprague-Dawley
Grant Support
Reg. No./Substance:
0/Isoenzymes; EC 2.7.1.-/Prkcd protein, rat; EC 2.7.1.-/Prkce protein, rat; EC Kinase C; EC Kinase C-alpha; EC Kinase C-delta; EC Kinase C-epsilon

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