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Gangliosides inhibit phospholipid-sensitive Ca2+-dependent kinase phosphorylation of rat myelin basic proteins

✍ Scribed by J. Y. H. Kim; J. R. Goldenring; R. J. DeLorenzo; R. K. Yu

Publisher: John Wiley and Sons
Year: 1986
Tongue: English
Weight: 590 KB
Volume: 15
Category: Article
ISSN: 0360-4012
DOI: 10.1002/jnr.490150205

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✦ Synopsis

Gangliosides inhibit the phosphorylation of both small and large rat myelin basic proteins (SMBP, LMBP) by an endogenous phospholipid-sensitive Ca*+-dependent protein kinase (C-kinase). Using a rat brain myelin preparation in an in vitro phosphorylation assay system, we determined the inhibition constants (ICs0's) of the gangliosides GMI, GDI,, GDlb, and GTlb to be approximately 160 pM, 65 pM, 65 pM, and 40 pM, respectively. Asialoganglioside G A ~, 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.

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