Key result
Apo B-100 deglycosylation increases lipoprotein aggregation and intracellular cholesterol accumulation in human aortic intima cells.
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Sub-fractions of all apo B-100 containing lipoproteins (low density lipoproteins, very low density lipoproteins and intermediate density lipoproteins) with reduced contents of sialic acid were found in vivo in human blood. These lipoproteins were inclined to spontaneously form aggregates and were able to stimulate accumulation of cholesterol in cells cultured from human aortic intima. In vitro treatment of apo B-containing lipoproteins with 2,6- and 2,3-specific sialidases, alpha-mannosidase, endoglycosidases F1 or F2 or peptide-N-glycanase F also stimulated aggregation and increased the ability of these particles to potentiate cholesterol accumulation in cells of the intact human aortic intima. So, deglycosylation of various apo B-containing lipoproteins possibly occurs in the blood, decreases their resistance to aggregation and increases the ability of these particles to stimulate accumulation of cholesterol in human aortic intima cells, thereby increasing their atherogenic potential.
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Аксенов et al. (2008) studied Atherosclerosis. In vitro enzymatic deglycosylation of apo B-containing lipoproteins (with 2,6- and 2,3-specific sialidases, alpha-mannosidase, endoglycosidases F1 or F2, or peptide-N-glycanase F) vs. Untreated apo B-containing lipoproteins was evaluated on Lipoprotein aggregation and intracellular cholesterol accumulation in human aortic intima cells. Deglycosylation of apo B-100 lipoproteins with 2,6- and 2,3-specific sialidases or endoglycosidases F1/F2 increased particle aggregation and cholesterol accumulation in human aortic intima cells.
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