Possible involvement of a cell surface glycoprotein in the differentiation of skeletal myoblasts (original) (raw)

The Journal of biological chemistry, 1984

Abstract

From a highly myogenic permanent line of rat skel-myoblasts (L6), we have isolated two classes of single step concanavalin A-resistant mutants. The RI class is about 2-fold and RII about 5-fold more resistant than the parental cells to the lethal action of concanavalin A. In all of the mutants, both the morphological differentiation (i.e. fusion to form myotubes) and biochemical differentiation, measured by the appearance of creatine kinase and acetylcholine receptors, are absent. The biochemical lesion in the RI type of mutants is not known, but RII type of mutants is unable to catalyze transfer of mannose from GDP-mannose into a lipid-linked form. Concanavalin A binding to separated membrane proteins from RII type of mutants on polyacrylamide gels is reduced 80% compared to wild type cells. In the RI type of mutants, however, only one major band, approximately 46,000 daltons, does not bind concanavalin A to the same extent as the wild type cells. In somatic cell hybridizations, RI...

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