Phospholipid Hydrolysis with Phospholipases A2 and C Impairs Apolipoprotein B-100 Conformation on the Surface of Low Density Lipoproteins by Reducing Their Association Resistance |
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| Authors: | 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 |
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| Affiliation: | (1) Laboratory of Cell-to-Cell Interactions, Institute of General Pathology and Pathophysiology, Russian Academy of Medical Sciences, Russia;(2) Laboratory of Physicochemical Methods of Investigation and Analysis, Institute of Physicochemical Medicine, Ministry of Health of the Russian Federation, Russia;(3) Laboratory of Atherogenesis Mechanisms, Institute of Experimental Cardiology, Ministry of Health of the Russian Federation, Russia;(4) Laboratory of Cell Engineering, Institute of Experimental Cardiology, Ministry of Health of the Russian Federation, Russia;(5) Institute of Atherosclerosis, Russian Academy of Natural Sciences, Moscow, Russia |
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| 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. __________ Translated from Byulleten' Eksperimental'noi Biologii i Meditsiny, Vol. 140, No. 10, pp. 418–422, October, 2005 |
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| Keywords: | low density lipoproteins phospholipase A2 phospholipase C lipoprotein aggregation atherosclerosis |
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