Inhibition of liver microsomal carnitine acyltransferases by sulphonylurea drugs
| Autor: | E.David Saggerson, N. M. Broadway |
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| Rok vydání: | 1995 |
| Předmět: |
Male
medicine.medical_specialty Tolbutamide Biophysics Phospholipid macromolecular substances Lipoproteins VLDL Biochemistry Rats Sprague-Dawley Glibenclamide chemistry.chemical_compound Structural Biology Internal medicine Glyburide Genetics medicine Animals Transferase Secretion Molecular Biology Triglycerides chemistry.chemical_classification Microsome Carnitine Acyltransferases Cell Biology Sulphonylureas Rats Malonyl Coenzyme A enzymes and coenzymes (carbohydrates) Enzyme Endocrinology Liver chemistry Liposomes Microsomes Liver lipids (amino acids peptides and proteins) medicine.drug |
| Zdroj: | FEBS Letters. 371:137-139 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(95)00877-c |
| Popis: | 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/secretion. |
| Databáze: | OpenAIRE |
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