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

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

Research output: Contribution to journalArticle

55 Citations (Scopus)

Abstract

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
Volume15
Issue number2
DOIs
StatePublished - Jan 1 1986
Externally publishedYes

Fingerprint

Gangliosides
N-Acetylneuraminic Acid
Phosphotransferases
Phosphorylation
G(M1) Ganglioside
Glycosphingolipids
Ceramides
Myelin Sheath
Protein Kinases
Protein Kinase C
Nervous System
Inhibitory Concentration 50
Lipids
Acids
Brain
rat Mbp protein
M40
In Vitro Techniques

Keywords

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

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience

Cite this

Gangliosides inhibit phospholipid‐sensitive Ca2+‐dependent kinase phosphorylation of rat myelin basic proteins. / Kim, J. Y.H.; Goldenring, J. R.; DeLorenzo, R. J.; Yu, Robert K.

In: Journal of Neuroscience Research, Vol. 15, No. 2, 01.01.1986, p. 159-166.

Research output: Contribution to journalArticle

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