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Differential expression of gangliosides on the surfaces of myelinated nerve fibers
Author(s) -
Ganser A. L.,
Kirschner D. A.
Publication year - 1984
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490120212
Subject(s) - axolemma , node of ranvier , receptor , microbiology and biotechnology , ganglioside , schwann cell , proteases , chemistry , axon , cholera toxin , protease , biology , biochemistry , biophysics , myelin , enzyme , neuroscience , central nervous system
The binding of cholera and tetanus toxins to receptors on the surfaces of teased nerve fibers was used to localize G M1 and G 1b ‐series gangliosides, respectively, by immunocytochemical methods. Native fibers and fibers treated with various hydrolytic enzymes to degrade specific surface components were studied. With native fibers, both toxins bound abundantly to nodes of Ranvier and poorly to the most external, internodal Schwann cell surfaces. Treatment of the fibers with proteases, hyaluronidase, and chondroitin ABC lyase neither eliminated receptors at the nodes nor unmasked receptors over the internodes. The axolemma underlying the paranodal or internodal myelin, exposed by extensive treatment with protease, bound both toxins in large amounts. Neuraminidase action induced cholera toxin receptors on the Schwann cell surface; these receptors were insensitive to protease. The results indicate that G M1 and G 1b ‐series gangliosides are predominantly localized to axonal and glial structures of the node of Ranvier and to paranodal/internodal axolemma, and that polysialogangliosides not of the G 1b ‐series are present on the internodal Schwann cell surface.