Hs. Suidan et al., THE THROMBIN RECEPTOR IS PRESENT IN MYOBLASTS AND ITS EXPRESSION IS REPRESSED UPON FUSION, The Journal of biological chemistry, 271(46), 1996, pp. 29162-29169
Cultured myoblasts derived from limb muscle of newborn rats express th
rombin receptor immunoreactivity on their surface. Receptor expression
is repressed upon myoblast fusion. This is due at least in part to a
decrease in the amount of the thrombin receptor mRNA. Addition of thro
mbin triggers calcium transients only in mono- but not multinucleated
muscle cells. Furthermore, thrombin increases the rate of myoblast pro
liferation that coincides with an activation of mitogen-activated prot
ein kinase. Northern analysis of thrombin receptor mRNA expression in
skeletal muscle showed that the transcript is present at a relatively
high level at birth, but is almost undetectable in the adult. By in si
tu hybridization, the mRNA at birth appeared to be present mostly in m
ononucleated cells grouped in clusters, but not in muscle fibers. Very
few nuclei surrounded by a mRNA signal were present on muscle section
s of rats 24 days postnatally. These results suggest that the thrombin
receptor plays a role in muscle development.