A unique subset of developmentally regulated surface proteins turns over rapidly during fusion of the L6 rat myoblast cell line.

We have previously identified several developmentally regulated surface polypeptides in the L6 rat myoblast cell line, on the basis of their susceptibility to lactoperoxidase catalyzed iodination. An analysis of the turnover rates of these polypeptides now indicates that while the bulk of the iodinated polypeptides have a half-life of 20-30 h, four low-molecular-weight polypeptides have half lives of 2-7 h. The half-lives of all of the rapid turnover class surface polypeptides were greatly increased in cultures where fusion was inhibited by chloroquine and in nonfusing variants of the L6 cell line. In contrast, inhibition of fusion by the metalloendoprotease inhibitor 1, 10-phenanthroline did not alter the turnover of any iodinatable surface proteins. We propose that some or all of the rapid turnover class of polypeptides may be surface receptors which control cell surface alterations involved in the acquisition of fusion competence or in fusion itself.