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• W2022698642 abstract "Chronic alcohol exposure leads to the appearance of carbohydrate-deficient transferrin (CDT), a N-glycosylated protein and sialic acid-deficient apolipoprotein E (apoE), an O-glycosylated protein. We show that chronic ethanol treatment destabilizes sialyltransferase (ST) mRNA resulting in a concomitant decreased steady-state level of ST mRNA. As a result, alcohol markedly decreases the hepatic synthetic rate of ST. This leads to impaired sialylation of transferrin and apoE. Consequently, apoE content in plasma high-density lipoproteins (HDL) is decreased. ApoE plays a significant role in the delivery of HDL cholesterol to the liver via apo B/E receptor, a process called reverse cholesterol transport (RCT). Desialylation of apoE results in its decreased association with HDL. Thus, the dissociation constant of HDL for binding to sialo-apoE is 90 +/- 35 nM, whereas that for desialo-apoE is 1010 +/- 250 nM. More importantly, the uptake of labeled cholesterol by human HepG2 cells is decreased by 30-40% from reconstituted HDL particles (rHDL)-containing desialo-apoE compared to rHDL with sialo-apoE. We conclude that chronic alcohol exposure down-regulates the expression of sialyltransferase genes resulting in impaired sialylation of apoE. This leads to its decreased binding to plasma HDL and thereby, impairs the RCT function of HDL." @default.
• W2022698642 created "2016-06-24" @default.
• W2022698642 creator A5021652778 @default.
• W2022698642 creator A5069628391 @default.
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• W2022698642 date "1999-11-01" @default.
• W2022698642 modified "2023-10-16" @default.
• W2022698642 title "Alcohol and Molecular Regulation of Protein Glycosylation and Function" @default.
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• W2022698642 doi "https://doi.org/10.1016/s0741-8329(99)00041-5" @default.
• W2022698642 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10580514" @default.
• W2022698642 hasPublicationYear "1999" @default.
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