Protein Kinase C- α and - ϵ Modulate Connexin-43 Phosphorylation in Human Heart

We have previously demonstrated that protein kinase C (PKC)- α expression is significantly elevated in failing human left ventricle, with immunostaining showing increased PKC- α localization at the intercalated disks of cardiomyocytes. In the present study we sought to determine, in the failing hear...

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Bibliographic Details
Published in:Journal of molecular and cellular cardiology 2001-04, Vol.33 (4), p.789-798
Main Authors: Bowling, Nancy, Huang, Xiao-di, Sandusky, George E., Fouts, Rebecca L., Mintze, Karen, Esterman, Michail, Allen, Paul D., Maddi, Rosemarie, McCall, Eileen, Vlahos, Chris J.
Format: Article
Language:English
Subjects:
Blotting, Western - methods
Cardiomyopathy
Connexin 43 - metabolism
Female
Gap junctions
Heart
Heart Failure - metabolism
Heart Failure - pathology
Heart Ventricles - metabolism
Heart Ventricles - pathology
Humans
Isoenzymes - metabolism
Male
Microscopy, Confocal - methods
Middle Aged
Phosphoprotein
Phosphorylation
Precipitin Tests - methods
Protein kinase
Protein Kinase C - metabolism
Protein Kinase C-alpha
Protein Kinase C-epsilon
Signal transduction
Ventricular Dysfunction, Left - metabolism
Ventricular Dysfunction, Left - pathology
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Summary:We have previously demonstrated that protein kinase C (PKC)- α expression is significantly elevated in failing human left ventricle, with immunostaining showing increased PKC- α localization at the intercalated disks of cardiomyocytes. In the present study we sought to determine, in the failing heart, if PKC- α interacted with connexin-43 (Cx-43) both spatially and functionally, and to compare the association of PKC-α /Cx-43 with that of PKC- ϵ, a PKC isozyme that does not significantly increase in failing hearts. The possibility of a PKC- α or PKC- ϵ/Cx-43 association in non-failing hearts was also investigated. Co-immunoprecipitation of PKC- α or PKC- ϵ and Cx-43 in non-failing and failing left ventricle was achieved using antibodies to PKC- α or Cx-43. Confocal microscopy confirmed that PKC- α distribution within the cardiomyocyte included co-localization with connexin-43 in both failing and non-failing myocardium. In a similar manner, confocal imaging of PKC- ϵ showed cardiomyocyte distribution in both cytosol and membrane, and colocalization of PKC-ϵ with Cx-43. Recombinant PKC- α or - ϵ increased PKC activity significantly above endogenous levels in the co-immunoprecipitated Cx-43 complexes (P
ISSN:0022-2828
1095-8584
DOI:10.1006/jmcc.2000.1349