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

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

doi:10.1007/s10517-005-0508-7

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

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

Authors

D V Aksenov¹, A A Mel'nichenko, I V Suprun, E V Yanushevskaya, T N Vlasik, I A Sobenin, O M Panasenko, A N Orekhov

Affiliation

¹ Laboratory of Cell-to-Cell Interactions, Institute of General Pathology and Pathophysiology, Russian Academy of Medical Sciences, Moscow. denaks@newmail.ru

PMID: 16671570
DOI: 10.1007/s10517-005-0508-7

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.

MeSH terms

Apolipoprotein B-100
Apolipoproteins B / chemistry*
Humans
Hydrolysis
Lipoproteins, LDL / chemistry*
Phospholipases A / chemistry
Phospholipases A / metabolism*
Phospholipids / chemistry*
Phospholipids / metabolism
Protein Conformation
Type C Phospholipases / chemistry
Type C Phospholipases / metabolism*

Substances

Apolipoprotein B-100
Apolipoproteins B
Lipoproteins, LDL
Phospholipids
Phospholipases A
Type C Phospholipases