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Gangliosides inhibit phospholipid‐sensitive Ca 2+ ‐dependent kinase phosphorylation of rat myelin basic proteins
Author(s) -
Kim J. Y. H.,
Goldenring J. R.,
DeLorenzo R. J.,
Yu R. K.
Publication year - 1986
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.490150205
Subject(s) - phosphorylation , biochemistry , phospholipid , myelin , ganglioside , sialic acid , protein kinase a , kinase , protein kinase c , sphingolipid , myelin basic protein , ceramide , in vitro , endogeny , chemistry , biology , microbiology and biotechnology , membrane , central nervous system , apoptosis , neuroscience
Gangliosides inhibit the phosphorylation of both small and large rat myelin basic proteins (SMBP, LMBP) by an endogenous phospholipid‐sensitive Ca 2+ ‐dependent protein kinase (C‐Kinase). Using a rat brain myelin preparation in an in vitro phosphorylation assay system, we determined the inhibition constants (IC 50 's) of the gangliosides G M1 , G D1a , G D1b , and G T1b to be approximately 160 μM, 65 μM, 65 μM, and 40 μM, respectively. Asialoganglioside G A1 , ceramide, and Nacetylneuraminic acid (NANA, sialic acid) failed to produce similar inhibition, suggesting that both the lipid and the sialic acid moieties are necessary, but neither alone is sufficient to produce inhibition. The results indicate that gangliosides may regulate protein kinase C activities in the nervous system.