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J Biol Chem, Vol. 273, Issue 48, 32288-32296, November 27, 1998
From the Expression of syndecan-1, a cell-surface heparan
sulfate proteoglycan, is down-regulated during skeletal muscle
differentiation (Larraín, J., Cizmeci-Smith, G., Troncoso, V.,
Stahl, R. C., Carey, D. J., and Brandan, E. (1997)
J. Biol. Chem. 272, 18418-18424). We examined the
role of syndecan-1 in basic fibroblast growth factor
(bFGF)-dependent inhibition of myogenesis.
C2C12 myoblasts were stably transfected with an
expression plasmid containing the rat syndecan-1 coding region
cDNA. Constitutive syndecan-1 expression resulted in a strongly
diminished capacity of the transfected clones to differentiate and to
express skeletal muscle-specific markers such as fusion, creatine
kinase, and myosin. The expression of myogenin, a master transcription
factor for muscle differentiation, was also reduced and delayed.
Analysis of the induction of a myogenin promoter-driven reporter
revealed that syndecan-1 expression resulted in a 6-7-fold increase in
sensitivity to bFGF-dependent inhibition of myogenin
expression. Transfecting the cells with a plasmid containing myogenin
cDNA reversed the inhibition of myogenin transcriptional activation
and myosin expression in syndecan-1-transfected cells; however, cell
fusion was not observed. These results demonstrate that syndecan-1
expression enhances cell responsiveness to bFGF and inhibits myoblast
fusion and suggest that muscle terminal differentiation is regulated by
syndecan-1 expression.
Syndecan-1 Expression Inhibits Myoblast Differentiation through a
Basic Fibroblast Growth Factor-dependent Mechanism
,
Department of Cell and Molecular Biology,
Faculty of Biological Sciences, Catholic University of Chile,
Santiago, Chile and ¶ Henry Hood M.D. Research Program, Sigfried
and Janet Weis Center for Research, Pennsylvania State College of
Medicine, Danville, Pennsylvania 17822-2613
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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