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(Received for publication, March 11, 1997, and in revised form, August 12, 1997)
From the An understanding of the role of CaM kinase II in
the pancreatic
Volume 272, Number 43,
Issue of October 24, 1997
pp. 27464-27469
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Calcium-stimulated Phosphorylation of MAP-2 in Pancreatic
TC3-cells Is Mediated by
Ca2+/Calmodulin-dependent Kinase II
,
,
Department of Biochemistry and Molecular
Biology, University of North Texas Health Science Center, Fort
Worth, Texas 76107-2699 and § Department of Pediatrics,
Washington University School of Medicine,
St. Louis, Missouri 63110
-cell is dependent on the identification of its
cellular targets. One of the best substrates of CaM kinase II in
vitro that could function in secretory events is the
microtubule-associated protein, MAP-2. By immunoblot analysis, a high
molecular weight protein with electrophoretic properties characteristic
of MAP-2, was identified in rat insulinoma TC3 cells and isolated
rat islets. In immunoprecipitation experiments employing
-toxin-permeabilized TC3 cells, elevation of intracellular
Ca2+ or addition of forskolin, an adenylate cyclase
activator, induced significant phosphorylation of MAP-2 in
situ. The effect of Ca2+ was rapid,
concentration-dependent and closely correlated with activation of CaM kinase II under similar experimental conditions. H-89, a specific and potent inhibitor of cAMP-dependent
protein kinase (PKA), prevented forskolin-induced MAP-2 phosphorylation but had little effect on MAP-2 phosphorylation stimulated by elevated Ca2+. Phosphopeptide mapping revealed that the
phosphorylation pattern observed in situ upon incubation of
the TC3 cells with increased free Ca2+, was strikingly
similar to that generated in vitro by CaM kinase II, most
notably with regard to the increased phosphate incorporated into one
prominent site. These data provide evidence that MAP-2 is
phosphorylated by CaM kinase II in the pancreatic -cell in situ, and that this event may provide an important link in the mediation of Ca2+-dependent insulin
secretion.
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