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Department of Biochemistry and Molecular Biology, St. Louis University Health Sciences Center, St. Louis, Missouri 63104
The present study demonstrates that
the
,
, and
isozymes of protein kinase C (PKC) are
translocated to particulate fractions from the cytosol during brief
intervals of global ischemia as well as reperfusion of ischemic
rat myocardium. In contrast, phorbol ester treatment of perfused hearts
resulted in the translocation of the
,
, and
isozymes of PKC
to particulate fractions. Additionally, the
,
, and
isozymes
of PKC are translocated to particulate fractions in phorbol
ester-stimulated, isolated adult rat cardiac myocytes. Concomitant with
the translocation of PKC isozymes to particulate fractions during
myocardial ischemia, increased protein phosphorylation was
observed, which was blocked by pretreatment of hearts with the
selective PKC inhibitor bisindolylmaleimide I (50 nM). In particular,
ischemia resulted in the phosphorylation of 26-, 20-, and
17-kDa particulate-associated proteins. Taken together, the present
findings are the first to demonstrate that specific PKC isozymes are
translocated to particulate fractions in the ischemic and the
reperfused ischemic rat heart, resulting in the phosphorylation of
specific particulate-associated proteins.
heart; reperfusion; myocytes; phorbol esters
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