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J Biol Chem, Vol. 274, Issue 14, 9169-9174, April 2, 1999
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From the Three members of the family of protease-activated
receptors (PARs), PARs-1, -3 and -4, have been identified as thrombin
receptors. PAR-1 is expressed by primary myoblast cultures, and
expression is repressed once myoblasts fuse to form myotubes. The
current study was undertaken to investigate the hypothesis that
thrombin inhibits myoblast fusion. Primary rodent myoblast cultures
were deprived of serum to promote myoblast fusion and then cultured in
the presence or absence of thrombin. Thrombin inhibited myoblast fusion, but another notable effect was observed; 50% of control cells
were apoptotic within 24 h of serum deprivation, whereas less than
15% of thrombin-treated cells showed signs of apoptosis. Proteolysis
was required for the effect of thrombin, but no other serine protease
tested mimicked the action of thrombin. Neither a PAR-1- nor a
PAR-4-activating peptide inhibited apoptosis or fusion, and myoblast
cultures were negative for PAR-3 expression. Myoblasts exposed to
thrombin for 1 h and then changed to medium without thrombin
accumulated apoptosis inhibitory activity in their medium over the
subsequent 20 h. Thus the protective action of thrombin appears to
be effected through cleavage of an unidentified thrombin receptor,
leading to secretion of a downstream apoptosis inhibitory factor. These
results demonstrate that thrombin functions as a survival factor for
myoblasts and is likely to play an important role in muscle development
and repair.
Department of Biochemistry and Molecular
Biology, Monash University, Clayton, Victoria 3168, Australia and
the ¶ School of Veterinary Science, University of Melbourne,
Parkville, Victoria 3052, Australia
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