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Cross‐reactivity between gfa and neurofilament (nf) proteins not revealed by immunohistology
Author(s) -
Dahl D.,
Grossi M.,
Bignami A.
Publication year - 1985
Publication title -
international journal of developmental neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.761
H-Index - 88
eISSN - 1873-474X
pISSN - 0736-5748
DOI - 10.1016/0736-5748(85)90173-x
Subject(s) - administration (probate law) , medical school , center (category theory) , medicine , gerontology , library science , political science , law , medical education , chemistry , computer science , crystallography
Antisera raised to a chicken brain cytoskeletal preparation selectively decorated neurof[laments in tissue sections. Glial filaments were not stained. However, the antisera were adsorbed on columns prepared with purified GFA, the subunit of glial filaments. Fractions adsorbed and eluted from GFA columns decorated neurofilaments with identical pattern. By the immunoblotting procedure the antisera reacted with the polypeptides of the neurofilament triplet and GFA. A 61K 5.6 component of brain cytoskeleton disappearing in Wallerian degeneration (Dahl, et al.; 22:185, 1982) was also decorated. Similar results were obtained with a monoclonal antibody isolated from the fusion of mouse myeloma cells with spleen cells from mice immunized with the same chicken brain antigen. Monoclonal and polyclonal antibodies decorated axonal and perikaryal neurofilaments with identical pattern. By the immunoblotting procedure the monoclonal reacted neurofilament 150K and GFA. Furthermore, both monoclonal and polyclonal antibodies reacted with a 18K cyanogen bromide peptide of GFA. It is suggested that neurofilament proteins and GFA share immunoreactlve sites and that the conunon epitope recognized by the monoclonal is exposed on neurofi[aments but masked on glial filaments in tissue sections. Supported by NIH grant NS 13034 and the Veterans Administration.