ENHANCED MYOGENESIS IN NCAM-TRANSFECTED MOUSE MYOBLASTS

THE fusion of mononucleate precursor myoblasts to form the multinucleated skeletal muscle fibre is proceeded by a series of complex cell-cell interactions1-5 but the cell-surface molecules involved in these events have not been characterized. During myogenesis in vivo and in vitro, expression of the neural cell adhesion molecule (NCAM) undergoes an isoform transition that precisely correlates with terminal myoblast differentiation and myotube formation6,7. Altered processing of RNA results in the replacement of the transmembrane NCAM (relative molecular mass, 145,000 (145K)) in proliferating myoblasts by a predominant 125K NCAM form linked to glycosyl phosphatidylinositol in myotubes8,9. We now report that mouse myoblasts transfected to constitutively express the human muscle-specific 125K glycosyl-phosphatidylinositol-linked NCAM isoform more readily fuse to form myotubes. This suggests that NCAM plays a part in myoblast fusion and that the isoform switch may promote this function. © 1990 Nature Publishing Group.