Phospholipid hydrolysis with phospholipases A2 and C impairs apolipoprotein B-100 conformation on the surface of low density lipoproteins by reducing their association resistance.

作者信息

Aksenov D V, Mel'nichenko A A, Suprun I V, Yanushevskaya E V, Vlasik T N, Sobenin I A, Panasenko O M, Orekhov A N

机构信息

Laboratory of Cell-to-Cell Interactions, Institute of General Pathology and Pathophysiology, Russian Academy of Medical Sciences, Moscow.

出版信息

Bull Exp Biol Med. 2005 Oct;140(4):419-22. doi: 10.1007/s10517-005-0508-7.

DOI:10.1007/s10517-005-0508-7

PMID:16671570

Abstract

Modification of apolipoprotein B-100 conformation on the surface of LDL isolated from human blood was demonstrated by enzyme immunoassay with a panel of monoclonal antibodies to this protein. The study by the light transmission fluctuation method showed that incubation of LDL with phospholipases A2 or C led to association of LDL particles. This lipolytic modification seems to impair LDL surface properties inducing association of these particles, which can play an important role in lipid accumulation in the vascular wall and at early stages promote the development of atherosclerosis.

摘要