Is acetylation of protein involved in membrane function?
Berl, S.; Clarke, D.D.; Colon, A.D.; Nunez, R.
Journal of Neural Transmission. Supplementum 19: 105-119
1983
ISSN/ISBN: 0303-6995 PMID: 6321644 Document Number: 197567
[3H]-acetate is rapidly incorporated as the acetyl moiety into synaptosomal protein and the apparent rate appears to decrease after approximately 1-2 minutes. A second dose of labeled acetate given 6 minutes after the first shows the same time dependent process suggesting that the protein substrate is not depleted. The apparent fall-off in the rate may represent the approach to a steady state of the mixing of the added acetate with internal cold acetate. Veratridine or batrachotoxin appears to stimulate a deacetylation process and tetrodotoxin blocks the effect of veratridine. Several proteins are acetylated at least one of which appears to be a glycoprotein of relatively low molecular weight. The presence of cold pyruvate or glucose competes with the incorporation of labeled acetate; the implication is that glucose and pyruvate can serve as a source of acetyl CoA for protein acetylation. The studies suggest that acetylation-deacetylation processes may be involved in membrane function, possibly in ion and/or transmitter channels.