Gangliosides inhibit phospholipid-sensitive Ca2+-dependent kinase phosphorylation of rat myelin basic proteins.
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 microM, 65 microM, 65 microM, and 40 microM, respectively. Asialoganglioside GA1, ceramide, and N-acetylneuraminic 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.
J Y
JY
Kim
J R
JR
Goldenring
R J
RJ
DeLorenzo
R K
RK
Yu
D000818:Animals; D001345:Autoradiography; D001921:Brain / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005732:Gangliosides / Q000494:pharmacology*; D004676:Myelin Basic Protein / Q000378:metabolism*; D010743:Phospholipids / Q000494:pharmacology*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000037:antagonists & inhibitors* / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
D005732:Gangliosides; D004676:Myelin Basic Protein; D010743:Phospholipids; D011493:Protein Kinase C