Lipoprotein desialylation simultaneously enhances the cell cholesterol uptake and impairs the reverse cholesterol transport system: in vitro evidences utilizing neuraminidase-treated lipoproteins and mouse peritoneal macrophages

• Published in: Atherosclerosis Vol. 139; no. 1; pp. 65 - 75
• Main Authors: Harada, Lila M, Carvalho, Márcia D.T, Passarelli, Marisa, Quintão, Eder C.R
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Ireland Ltd 01.07.1998; Elsevier
• Subjects: Animals; Atherosclerosis; Atherosclerosis (general aspects, experimental research); Biological and medical sciences; Biological Transport; Blood and lymphatic vessels; Cardiology. Vascular system; Carrier Proteins - metabolism; Cells, Cultured; Cholesterol - metabolism; Cholesterol efflux; Cholesterol Ester Transfer Proteins; Cholesterol Esters - metabolism; Cholesteryl ester transfer protein (CETP); Desialylation; Glycoproteins; Humans; Lecithin:cholesterol acyltransferase (LCAT); Lipoproteins - metabolism; Macrophages, Peritoneal - metabolism; Medical sciences; Mice; Neuraminidase - metabolism; Phosphatidylcholine-Sterol O-Acyltransferase - metabolism; Reverse cholesterol transport; Sialic Acids - metabolism; Lecithin:cholesterol acyltransferase (LCAT); Cholesteryl ester transfer protein (CETP); Reverse cholesterol transport; Desialylation; Atherosclerosis; Cholesterol efflux; Cell culture; Pathophysiology; Rodentia; Cardiovascular disease; Exploration; Lipoprotein; In vitro; Accumulation; Cholesterol; Vascular disease; Vertebrata; Mammalia; Mouse; Animal; Intracellular; Macrophage
• ISSN: 0021-9150; 1879-1484
• DOI: 10.1016/S0021-9150(98)00057-4

Desialylation of low density lipoprotein (LDL) brings about accumulation of cholesterol in cultured cells. The influence of the neuraminidase-treated lipoprotein (LP) on the reverse cholesterol transport system was investigated in vitro utilizing very low density lipoprotein (VLDL), LDL, total high density lipoprotein (HDL) and its subfractions, HDL 2 and HDL 3, isolated from healthy donor plasma and mouse peritoneal macrophages. It was found that LP desialylation significantly: (1) decreased the capacity of total HDL and of HDL 2, but not of HDL 3, to efflux cellular cholesterol; (2) lowered the cholesterol esterification rate by lecithin:cholesterol acyltransferase (LCAT) without modifying the intrinsic LCAT activity of HDL; (3) increased the cholesteryl ester transfer from HDL to apo B-containing LP mediated by cholesteryl ester transfer protein (CETP); (4) enhanced the uptake by macrophages of cholesterol from HDL and LDL, although the amount of cholesterol taken up by the cells was much greater from the desialylated LDL than from desialylated HDL. Taken together, these in vitro evidences indicate that, in addition to enhancing the cell cholesterol LP uptake, desialylation may contribute to the premature development of atherosclerosis by impairing the reverse cholesterol transport system.