Overexpression of heat shock proteins differentially modulates protein kinase C expression in rat neonatal cardiomyocytes.
Previous studies have suggested that protein kinase C (PKC) is involved in heat shock protein (Hsp)-mediated cardioprotection. Therefore, we wanted to determine whether overexpression of Hsps modulates PKC expression, which will give us further insight into understanding the mechanism by which Hsps and PKC interact to protect cells from stress-induced injury. Specifically, we overexpressed the inducible form of Hsp70 (Hsp70i) or Hsp90 in rat neonatal cardiomyocytes and evaluated PKCdelta or PKCepsilon expression by immunoblotting and immunofluorescent confocal microscopy. Western analysis showed that overexpression of Hsp70i or Hsp90 decreased PKCepsilon expression. However, overexpression of Hsp70i or Hsp90 did not modify PKCdelta expression over control levels. Overexpression of constitutively active PKCdelta or PKCepsilon increased Hsp70i expression over control levels. The data suggest that overexpression of Hsps differentially modulates expression of PKC isoforms in rat neonatal cardiomyocytes. Furthermore, PKC may directly play a role in Hsp-mediated cardioprotection by upregulating Hsp70i expression.
Coaxum
Sonya D
SD
Department of Physiology, Loyola University Medical Center, Maywood, IL 60153, USA.
Martin
Jody L
JL
Mestril
Ruben
R
D000256:Adenoviridae; D000818:Animals; D005822:Genetic Vectors; D006360:Heat-Shock Proteins / Q000378:metabolism*; D032383:Myocytes, Cardiac / Q000378:metabolism*; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D014161:Transduction, Genetic
D006360:Heat-Shock Proteins; D011493:Protein Kinase C