Cell surface proteins of differentiating rat cerebellar cells maintained in dispersed cell culture.

The complement of cell surface proteins of differentiating rat cerebellar neurons maintained in dispersed cell cultures was evaluated by the combined methods of lactoperoxidase-catalyzed radioiodination and miniature sodium dodecyl sulfate polyacrylamide gel electrophoresis. Pure neuronal cell samples were obtained by direct dissection of such cells from the surfaces of the culture vessels. The electrophoretic profiles of cell surface proteins (CSP) from neurons maintained for 1, 7, 14, 21 and 28 days in vitro (DIV) were compared. It could be seen that while the pattern was relatively constant between 7 and 28 DIV, several differences existed between profiles from 1 and 7 DIV. The earliest stage was characterized by a prominent polypeptide triplet having molecular weight of approximately 48,000, 56,000 and 71,000 daltons. Later stages of development (7-28 DIV) were characterized by a greater number of high molecular weight surface polypeptides relative to the earliest stage. Comparison of electrophoretic profiles of CSPs of neurons and nonneuronal cells indicated that a number of polypeptides were not shared by these classes of cells.