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and -
, which
mediate functional protection in isolated rat heart
Departments of 1 Internal Medicine and 2 Legal Medicine, Yamaguchi University School of Medicine, Yamaguchi 755-8505, Japan
Protein kinase C
(PKC) plays an important role in mediating ischemic
preconditioning (PC). However, the relationship between PKC isoforms
and PC is still uncertain. We analyzed subcellular localization of PKC
isoforms by Western blot analysis in isolated rat heart and demonstrate
that PKC-
, -
, and -
were translocated to the membrane fraction
associated with the improvement of cardiac function. Translocation of
PKC- and - persisted after a 30-min period following PC, but the
translocation of PKC- was transient. Under low
Ca2+ perfusion (0.2 mmol/l), PC
improved the cardiac function associated with the translocation of
PKC-. Chelerythrine (1.0 µmol/l) suppressed the translocation of
all PKC isoforms associated with the loss of improvement of the cardiac
function. On the other hand, bisindolylmaleimide (0.1 µmol/l) did not
inhibit the improvement of cardiac function induced by PC, which was
associated with the translocation of PKC-. These results indicate
that the effect of PC on cardiac function is mediated by the
translocation of either PKC- or - independently in rat hearts.
ischemia; protein kinase C isoforms; contractile function; low calcium perfusion; protein kinase C inhibitors
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