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.
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Translated from Byulleten' Eksperimental'noi Biologii i Meditsiny, Vol. 140, No. 11, pp. 530–534, November, 2005
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Panasenko, O.M., Aksenov, D.V., Mel'nichenko, A.A. et al. Proteolysis of Apoprotein B-100 Impairs Its Topography on LDL Surface and Reduces LDL Association Resistance. Bull Exp Biol Med 140, 521–525 (2005). https://doi.org/10.1007/s10517-006-0013-7
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DOI: https://doi.org/10.1007/s10517-006-0013-7