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Obesity Research Center (G.C.Y., B.E.C.), Evans Department of Medicine, Boston University School of Medicine, Boston, Massachusetts 02118; and Immunology Division (H.M.K.), Children’s Hospital of Philadelphia, University of Pennsylvania, Philadelphia, Pennsylvania 19104
Address all correspondence and requests for reprints to: Gordon C. Yaney, Ph.D., Boston Medical Center, Obesity Research Center, 88 E. Newton Street, Boston, Massachusetts 02118. E-mail: gyaney{at}acs.bu.edu
Pancreatic ß-cells contain protein kinase C (PKC) isoforms that may
play a role in insulin secretion. Activity of PKC classes (cPKC, nPKC,
aPKC) and their regulation by acyl-CoA derivatives was examined in
extracts of clonal pancreatic ß-cells (HIT) by protein
phosphorylation. PKC classes were distinguished based on their
previously defined cofactor requirements. Down-regulation of PKC by
phorbol esters was confirmed by Western blotting and resulted in the
complete loss of cPKC activity, partial loss of nPKC activity and
preservation of aPKC activity and glucose-stimulated insulin secretion.
aPKC activity was potentiated 4- to 8-fold by the CoA esters of
myristate, palmitate, and oleate with a half-maximal value of 3
µM. Both oleoyl- and myristol-CoA, but not palmitoyl-CoA,
caused inhibition of nPKC activity. Oleoyl-CoA inhibited nPKC activity
up to 75% with a half-maximal effect at 10 µM. This
value was independent of the concentration of diacylglycerol used. The
addition of exogenous oleate or palmitate potentiated
glucose-stimulated insulin secretion 2-fold and was unaffected by
PMA-induced down-regulation. Stimulation by glucose or glucose and
oleate also increased the mass of PKC-
found in the particulate
fraction. These data are consistent with increased cytosolic long-chain
acylCoA-activating aPKC isoforms resulting in stimulation and/or
potentiation of glucose-induced insulin secretion.
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