Enhanced PKCε mediated phosphorylation of connexin43 at serine 368 by a carboxyl-terminal mimetic peptide is dependent on injury

The gap junction (GJ) protein connexin (Cx43) is important for organized action potential propagation between mammalian cardiomyocytes. Disruption of the highly ordered distribution of Cx43 GJs is characteristic of cardiac tissue after ischemic injury. We recently demonstrated that epicardial admini...

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Bibliographic Details
Published in:Channels (Austin, Tex.) Tex.), 2011-05, Vol.5 (3), p.236-240
Main Authors: Palatinus, Joseph A., Rhett, Joshua M., Gourdie, Robert G.
Format: Article
Language:English
Subjects:
Addendum
Animals
Binding
Biology
Biomimetic Materials - pharmacology
Bioscience
Calcium
Cancer
Cell
Connexin 43 - genetics
Connexin 43 - metabolism
Cycle
Female
HeLa Cells
Humans
Landes
Mice
Myocardial Ischemia - genetics
Myocardial Ischemia - metabolism
Myocardium - metabolism
Organogenesis
Peptides - pharmacology
Phosphorylation - drug effects
Phosphorylation - genetics
Protein Kinase C-epsilon - genetics
Protein Kinase C-epsilon - metabolism
Proteins
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Summary:The gap junction (GJ) protein connexin (Cx43) is important for organized action potential propagation between mammalian cardiomyocytes. Disruption of the highly ordered distribution of Cx43 GJs is characteristic of cardiac tissue after ischemic injury. We recently demonstrated that epicardial administration of a peptide mimetic of the Cx43 carboxyl-terminus reduced pathologic remodeling of Cx43 GJs and protected against induced arrhythmias following ventricular injury. Treatment of injuries with the carboxyl-terminal peptide was associated with an increase in phosphorylation at serine 368 of the Cx43 carboxyl-terminus. Here, we report that Cx43 peptide treatment of uninjured hearts does not prompt a similar increase in phosphorylation. Moreover, we show that peptide treatment of undisturbed cultured HeLa cells expressing a Cx43 construct also exhibit no changes in Cx43 phosphorylation at serine 368. However, in parallel with the results in vivo, a trend of increasing phosphorylation at serine 368 was observed in Cx43-expressing HeLa cells following scratch wounding of cultured monolayers. These results suggest that peptide-enhanced phosphorylation of the Cx43 carboxyl-terminus is dependent on injury-mediated cellular responses.
ISSN:1933-6950
1933-6969
DOI:10.4161/chan.5.3.15834