Rat oligodendrocytes have cell adhesion molecules.

The researchers isolated oligodendrocytes and observed their aggregation behavior. They treated the cells with trypsin to assess its effect on adhesion. To test protein synthesis, they used inhibitors like cycloheximide. Glycosylation inhibitors were also applied to study their role. An immunological assay was developed to detect adhesion molecules. This assay used rabbit immunoglobulins against conditioned medium. The team tested if these antibodies could prevent cell aggregation. They also incubated antibodies with the medium to see if they could neutralize their effect.

Trypsin treatment reduced the aggregation of oligodendrocytes. This suggests that cell adhesion molecules are sensitive to this enzyme. Protein synthesis inhibitors prevented the regeneration of these molecules. Glycosylation inhibitors also blocked the recovery of adhesion. The immunological assay successfully detected the presence of these molecules. Rabbit immunoglobulins against conditioned medium inhibited aggregation. Incubation of these antibodies with the medium neutralized their effect. These findings support the role of specific molecules in cell adhesion.

The study supports the idea that cell adhesion molecules mediate oligodendrocyte aggregation. These molecules are inactivated by trypsin and require protein synthesis and glycosylation. The immunological assay effectively measures their presence. The findings suggest that these molecules are crucial for cell adhesion. The study provides a method to quantify these proteins. It highlights the importance of post-translational modifications. The results align with the authors' hypothesis. The work contributes to understanding glial cell interactions.