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J Biol Chem, Vol. 273, Issue 18, 10914-10918, May 1, 1998
From the Angiogenesis Research Center, Cardiovascular Division,
Department of Medicine, Beth Israel Deaconess Medical Center,
Harvard Medical School, Boston, Massachusetts 02215
Recent studies suggest that some of the heparan
sulfate-carrying proteoglycans may directly participate in signaling
via their cytoplasmic tail. The present investigation addresses the
potential involvement of syndecan-4, a widely expressed transmembrane
proteoglycan, in this process. We found that the cytoplasmic tail of
syndecan-4 is phosphorylated on a single serine residue
(Ser183) in growth-arrested NIH 3T3 fibroblasts, with
a stoichiometry of 0.3 mol Pi/mol syndecan-4. Treatment of
the cells with a protein kinase C (PKC)-activating phorbol ester lead
to a 2.5-fold increase in Ser183 phosphorylation. This
increase was inhibited by a generic PKC inhibitor but not by an
inhibitor specific to the calcium-dependent conventional
PKCs, suggesting that the cytoplasmic tail of syndecan-4 is
phosphorylated by a calcium-independent novel PKC isozyme. Application
of 10-30 ng/ml basic fibroblast growth factor (bFGF) produced a
2-3-fold reduction in the phosphorylation of syndecan-4. Because
treatment with the phosphatase inhibitor calyculin prevented the
bFGF-induced decrease in syndecan-4 phosphorylation, the effect of bFGF
appears to be mediated by a protein serine/threonine phosphatase type 1 or 2A. We conclude that the cytoplasmic tail of syndecan-4 is subject
to in vivo phosphorylation on Ser183, which is
regulated by the activities of a novel PKC isozyme and a
bFGF-dependent serine/threonine phosphatase.
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