Altered activity of lecithin cholesterol ACYL transferase enzyme and high density lipoprotein in type 2 diabetes mellitus
Journal Title: Medpulse International Journal of Biochemistry - Year 2017, Vol 4, Issue 1
Abstract
An important enzyme in modulating plasma HDL levels is cholesterol acyl transferase (LCAT) which is responsible for the formation of most of the cholesterol esters (CE) present in human plasma. This enzyme catalyses the transfer of fatty acid from the Sn-2 position of the lecithin to the free hydroxyl group of cholesterol. It utilizes linoleate for the esterification of cholesterol in preference to the other fatty acids. Thus the enrichment of the linoleate content of plasma lecithin which accompanies ingestion of a poly unsaturated fat diet leads to an increase in the proportion of cholesterol linoleate in plasma. The physiological substrate for LCAT is probably nascent HDL. The enzyme activity is dependent on apoA-1 and in inhibited by apoA-2. Thus the maturing HDL particles contain mainly esterified cholesterol which having been rendered non diffusible are trapped in the HDL and then are transferred to the liver to undergo catabolism. Present studies have been carried out on diabetic patients with good glycaemic control and diabetics with poor glycaemic control and compared with normal control group. HDL cholesterol levels in diabetic patients with good and poor glycaemic control were significantly lower than the normal control group. LCAT in diabetic patients with good and poor glycaemic control were significantly lower than the normal control group. However HDL cholesterol level and LCAT activity in diabetic patients with poor glycaemic control was still lower this supports the observation that coronary artery disease (CAD) is 2-4 times higher in diabetes than non diabetes.
Authors and Affiliations
Tahmeen Jameel, Raisa Faheem, Aiman Mahmood, Afnan Ali Afrooz
Keywords
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