Endogenous lectin from chick embryo skeletal muscle is not involved in myotube formation in vitro.

Antisera against a beta-D-galactoside-specific lectin purified to homogeneity from embryonic chick thigh muscle and from adult chicken livers were raised in rabbits. The sera contained antibodies which strongly inhibited the hemagglutinin activity of the lectin. Immune and preimmune [125I]IgG and [125I]Fab preparations were tested for ability to bind to monolayers of cultured chick myoblasts and showed no significant differences in binding. Thus, we were unable to detect the lectin on the cell surface. When added to myoblast cultures, the purified lectin had no influence on the process of myoblast fusion. Furthermore, neither anti-lectin IgG nor Fab fragments interfered with myotube formation when present at high concentration in fusing cultures. On the basis of these results, we conclude that intercellular interactions between the lectin and complementary cell surface receptors do not play a role in myoblast adhesion and fusion in vitro.