Proteolysis of apoprotein B-100 impairs its topography on LDL surface and reduces LDL association resistance.

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

Journal: Bulletin of experimental biology and medicine 2006;140(5):521-5

PMID: 16758614

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Abstract

Serine proteinases (trypsin and chymotrypsin) cause destruction of apolipoprotein B-100 on the surface of human blood LDL. Incubation of LDL with these enzymes increases the mean size of LDL particles. Proteolysis of apolipoprotein B-100 induces changes in surface structure, destabilizes LDL particles, and reduces their association resistance. Presumably, this proteolytic modification of LDL with subsequent association of these particles plays an important role in accumulation of cholesterol in the vascular wall and in the development of early stages of atherosclerosis.

Address: Laboratory of Atherogenesis Mechanisms, Institute of Experimental Cardiology, National Center of Cardiology, Ministry of Health of the Russian Federation, Moscow. [email protected]

DOI: 10.1007/s10517-006-0013-7

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MeSH Terms: Agglutinins, Apolipoprotein B-100, Apolipoproteins B, Atherosclerosis, Cholesterol, Chromatography, Chymotrypsin, Dose-Response Relationship, Drug, Humans, Lectins, Lipoproteins, LDL, Surface Properties, Time Factors, Trypsin