Profiling impaired hepatic endoplasmic reticulum glycosylation as a consequence of ethanol ingestion.

ABSTRACT: Alcoholic liver disease (ALD) is a prominent cause of morbidity and mortality in the United States. Alterations in protein folding occur in numerous disease states, including ALD. The endoplasmic reticulum (ER) is the primary site of post-translational modifications (PTM) within the cell. Glycosylation, the most abundant PTM, affects protein stability, structure, localization, and activity. Decreases in hepatic glycosylation machinery have been observed in rodent models of ALD, but specific protein targets have not been identified. Utilizing two-dimensional gel electrophoresis and liquid chromatography-tandem mass spectrometry, glycoproteins were identified in hepatic microsomal fractions from control and ethanol-fed mice. This study reports for the first time a global decrease in ER glyco

SUBMITTER: Galligan JJ 

PROVIDER: S-EPMC3501204 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature