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CERAMIDE GLYCOSYLTRANSFERASES IN CULTURED RAT CEREBELLUM: CHANGES WITH AGE, WITH DEMYELINATION, AND WITH INHIBITION OF MYELINATION BY 5‐BROMO‐2′‐DEOXYURIDINE OR EXPERIMENTAL ALLERGIC ENCEPHALOMYELITIS SERUM
Author(s) -
Latovitzki N.,
Silberberg D. H.
Publication year - 1975
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1975.tb03671.x
Subject(s) - encephalomyelitis , in vivo , in vitro , cerebellum , galactosyltransferase , glycosyltransferase , biology , biochemistry , chemistry , medicine , endocrinology , microbiology and biotechnology , immunology , enzyme , central nervous system
—UDP‐galactose:ceramide galactosyltransferase (CGalT) (E.C. 2.4.1.62) and UDP‐glucose:ceramide glucosyltransferase (CGlcT) activities were measured in myelinating cultures of newborn rat cerebellum. Specific activities were measured at various days in vitro and the pattern of activities compared with that reported for in vivo tissue. Cultures demyelinated by incubation with media containing 22% serum from rabbits in which experimental allergic encephalomyelitis (EAE) was induced by injection with whole guinea‐pig spinal cord, had 28% of CGalT specific activity and 86% of CGlcT specific activity measured in control cultures. Cultures in which myelination was inhibited by maintenance on media containing 0.15 m m ‐5‐bromo‐2′‐deoxyuridine (BUdR) had 10% of CGalT specific activity and 118% of CGlcT specific activity of control cultures. Cultures in which myelination was inhibited by maintenance on media containing 2% EAE serum had 12% of the CGalT specific activity of control cultures. The data suggest that in vitro CGalT is predominantly a glial enzyme while CGlcT occurs primarily in neurons, and that the reduced CGalT activity may be involved in the mechanism of myelination inhibition by BUdR and by EAE serum.