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

J. Y.H. Kim, J. R. Goldenring, R. J. DeLorenzo, R. K. Yu

Research output: Contribution to journalArticlepeer-review

55 Scopus citations


Gangliosides inhibit the phosphorylation of both small and large rat myelin basic proteins (SMBP, LMBP) by an endogenous phospholipid‐sensitive Ca2+‐dependent protein kinase (C‐Kinase). Using a rat brain myelin preparation in an in vitro phosphorylation assay system, we determined the inhibition constants (IC50's) of the gangliosides GM1, GD1a, GD1b, and GT1b to be approximately 160 μM, 65 μM, 65 μM, and 40 μM, respectively. Asialoganglioside GA1, 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.

Original languageEnglish (US)
Pages (from-to)159-166
Number of pages8
JournalJournal of Neuroscience Research
Issue number2
StatePublished - 1986
Externally publishedYes


  • ganglioside
  • myelin basic protein
  • phospholipid‐sensitive Ca‐dependent protein kinase
  • protein C‐kinase

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience


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