Lcat Structure and Function
نویسندگان
چکیده
Journal of Lipid Research Volume 53, 2012 1783 Copyright © 2012 by the American Society for Biochemistry and Molecular Biology, Inc. removal of excess cholesterol from macrophages in the arterial wall and subsequent delivery to the liver for biliary excretion. Interest in the enzyme increased even further when in 1967 the fi rst family with three sisters with familial LCAT defi ciency was described ( 4 ). To date, approximately 60 isolated cases and 70 small families with partial or complete LCAT defi ciency have been described with 86 different molecular defects in the LCAT gene ( 5 ) (http:// www.hgmd.org). In addition, numerous animal models lacking or overexpressing LCAT, including mice ( 6–10 ), hamsters ( 11 ), rabbits ( 12 ), and monkeys ( 13 ) have been generated to gain better insight in the complex role of LCAT in modulating lipoprotein metabolism, RCT, and atherosclerosis.
منابع مشابه
Distant Homology Modeling of LCAT and Its Validation through In Silico Targeting and In Vitro and In Vivo Assays
LCAT (lecithin:cholesterol acyltransferase) catalyzes the transacylation of a fatty acid of lecithin to cholesterol, generating a cholesteryl ester and lysolecithin. The knowledge of LCAT atomic structure and the identification of the amino acids relevant in controlling its structure and function are expected to be very helpful to understand the enzyme catalytic mechanism, as involved in HDL ch...
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Lysosomal phospholipase A2 (LPLA2) and lecithin:cholesterol acyltransferase (LCAT) belong to a structurally uncharacterized family of key lipid-metabolizing enzymes responsible for lung surfactant catabolism and for reverse cholesterol transport, respectively. Whereas LPLA2 is predicted to underlie the development of drug-induced phospholipidosis, somatic mutations in LCAT cause fish eye diseas...
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We established five monoclonal antibodies that reacted with human LCAT and recognized different epitopes on LCAT. These are mouse anti-human LCAT monoclonal antibodies designated 36487, 36454, 36442, 36405, and 36486, which react with the peptides corresponding to human LCAT amino acid residues R159-E179, M258-S273, S274-S294, D352-S376, and N415-E440, respectively. We also successfully used tw...
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The enzymatic and interfacial binding activity of lecithin-cholesterol acyltransferase (LCAT) is affected differentially by the location and extent of its glycosylation. Two LCAT glycosylation-deficient mutants, N84Q and N384Q, were constructed, permanently expressed in Chinese hamster ovary cells, and purified to determine the effects of deleting individual glycan chains on its stability, stru...
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The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT). The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase. T...
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