Inhibition of liver microsomal carnitine acyltransferases by sulphonylurea drugs
- 4 September 1995
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 371 (2) , 137-139
- https://doi.org/10.1016/0014-5793(95)00877-c
Abstract
The sulphonylureas glibenclamide and tolbutamide inhibited carnitine acyltransferase activities in rat liver microsomes. Glibenclamide was a more potent inhibitor than tolbutamide. The effect of tolbutamide on the malonyl-CoA-inhibitable transferase was influenced by the phospholipid/detergent environment whereas the effect of glibenclamide was not. Glibenclamide was a more potent inhibitor of the malonyl-CoA-inhibitable transferase than of the malonyl-CoA-insensitive enzyme. The extent of inhibition of the malonyl-CoA-inhibitable transferase by tolbutamide was similar to its effect on VLDL triacylglycerol secretion as reported by Wiggins and Gibbons [Biochem. J. 284 (1992) 457–462] possibly supporting the suggestion that microsomal carnitine acyltransferases are involved in VLDL triacylglycerol assembly/secretionKeywords
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