Inhibition of acyl coenzyme A:Lysolecithin acyltransferases by local anesthetics, detergents and inhibitors of cyclic nucleotide phosphodiesterases

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Abstract

Acyl coenzyme A:lysolecithin acyltransferase plays a major role in regulating the amount of lysolecithin in cell membranes. The acyltransferase activity in microsomal preparations from rat liver, rat heart and rabbit gastric mucosa is inhibited by a series of tertiary amine local anesthetics, detergents, and some inhibitors of cyclic nucleotide phosphodiesterases. Aspirin and indomethacin cause elevated lysolecithin/lecithin ratios in the stomachs of mice after oral administration. Inhibition of acyltransferase activity in microsomal preparations by local anesthetics correlates with reported anesthetic potencies at approximately 1 100 reported therapeutic dosages. In BHK-13 cells acyltransferase activity is inhibited at 1 3 to 1 10 the concentrations that have been reported to cause alterations in the mobility and topography of cell surface receptors.

Original languageEnglish (US)
Pages (from-to)186-193
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume75
Issue number1
DOIs
StatePublished - Mar 7 1977

Bibliographical note

Funding Information:
* This work was supported by the Theodore Gildred Foundation and U. S. Public Health Service Grants CA16123and CA14195 from the National Cancer Institute.

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