Developmentally regulated epitopes on a neurofilament protein visualized by monoclonal antibodies
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1Department of Neurobiologie, Max-Planck-Institut für Biophysikalische Chemie, Göttingen F.R.G.
Two monoclonal antibodies (mabs) which recognized the 68 kDa subunit of the rat neurofilament triplet were isolated. In immunoblots with SDS-solubilized and reduced proteins, these mabs recognized their epitopes equally well in embryonic and in adult tissue. However, these epitopes were developmentally regulated in paraformaldehyde-fixed rat brain sections. They were abundant in all compartments of differentiating neurons, whereas in mature neurons their presence was markedly attenuated, with a moderate abundance in perikarya and larger dendrites and low concentrations in axons. Thus, a differential developmental modification, possibly involving the masking of an epitope, is demonstrated for the small neurofilament polypeptide in rat and monkey brain tissue.
Two monoclonal antibodies (mabs) which recognized the 68 kDa subunit of the rat neurofilament triplet were isolated. In immunoblots with SDS-solubilized and reduced proteins, these mabs recognized their epitopes equally well in embryonic and in adult tissue. However, these epitopes were developmentally regulated in paraformaldehyde-fixed rat brain sections. They were abundant in all compartments of differentiating neurons, whereas in mature neurons their presence was markedly attenuated, with a moderate abundance in perikarya and larger dendrites and low concentrations in axons. Thus, a differential developmental modification, possibly involving the masking of an epitope, is demonstrated for the small neurofilament polypeptide in rat and monkey brain tissue.