Proteins Differentially Expressed in the Pancreas of Hepatic Alcohol Dehydrogenase-Deficient Deer Mice Fed Ethanol For 3 Months

• Published in: Pancreas Vol. 46; no. 6; p. 806
• Main Authors: Bhopale, Kamlesh K, Amer, Samir M, Kaphalia, Lata, Soman, Kizhake V, Wiktorowicz, John E, Shakeel Ansari, Ghulam A, Kaphalia, Bhupendra S
• Format: Journal Article
• Language: English
• Published: United States 01.07.2017
• Subjects: Alcohol Dehydrogenase - deficiency; Alcohol Dehydrogenase - genetics; Alcohol Drinking; Animals; Disease Models, Animal; Ethanol; Genotype; Liver - enzymology; Male; Mice, Knockout; Pancreas - metabolism; Pancreatitis, Alcoholic - genetics; Pancreatitis, Alcoholic - metabolism; Peromyscus; Phenotype; Proteins - metabolism; Proteomics - methods; Time Factors
• ISSN: 1536-4828
• DOI: 10.1097/MPA.0000000000000835

The aim of this study was to identify differentially expressed proteins in the pancreatic tissue of hepatic alcohol dehydrogenase-deficient deer mice fed ethanol to understand metabolic basis and mechanism of alcoholic chronic pancreatitis. Mice were fed liquid diet containing 3.5 g% ethanol daily for 3 months, and differentially expressed pancreatic proteins were identified by protein separation using 2-dimensional gel electrophoresis and identification by mass spectrometry. Nineteen differentially expressed proteins were identified by applying criteria established for protein identification in proteomics. An increased abundance was found for ribosome-binding protein 1, 60S ribosomal protein L31-like isoform 1, histone 4, calcium, and adenosine triphosphate (ATP) binding proteins and the proteins involved in antiapoptotic processes and endoplasmic reticulum function, stress, and/or homeostasis. Low abundance was found for endoA cytokeratin, 40S ribosomal protein SA, amylase 2b isoform precursor, serum albumin, and ATP synthase subunit β and the proteins involved in cell motility, structure, and conformation. Chronic ethanol feeding in alcohol dehydrogenase-deficient deer mice differentially expresses pancreatic functional and structural proteins, which can be used to develop biomarker(s) of alcoholic chronic pancreatitis, particularly amylase 2b precursor, and 60 kDa heat shock protein and those involved in ATP synthesis and blood osmotic pressure.