Microheterogeneity ("neurotypy") of neurofilament proteins.

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Abstract
Neurofilaments purified from adult rat brainstem by 2 methods were electrophoresed on NaDodSO4[sodium dodecyl sulfate]/polyacrylamide gels to separate the triplet proteins (approximate MW of 200,000, 155,000 and 68,000) which were electroblotted onto nitrocellulose paper. On Coomassie blue-stained gels that were not electroblotted, the same banding pattern was seen with both methods of preparation. Immunocytochemical staining of the electroblots with each of 5 monoclonal antibodies revealed that 3 of the monoclonal antibodies were specific for the MW 200,000 neurofilament protein and 2, for both the MW 200,000 and 155,000 neurofilament proteins. None of the antibodies reacted with the MW 68,000 band. The MW 200,000 band could be resolved into doublet bands. Individual monoclonal antibodies reacted with either 1 or both of the MW 200,000 doublets. The immunocytochemical staining of the neurofilament triplets on electroblots was compared to that of adult rat cerebellar paraffin sections. Each monoclonal antibody had a unique pattern of staining, reacting only with certain subpopulations of neurons or their processes. Correlation of the staining patterns in cerebellar tissue sections with those of neurofilament polypeptides on electroblots, suggested that different neurofilament polypeptides can be localized to different structures and subpopulations of neurons and that molecular heterogeneity (neurotypy) may be revealed within the MW 200,000 and 155,000 neurofilament polypeptides.