Proteome analysis of rat pancreatic acinar cells: Implication for cerulein‐induced acute pancreatitis

Abstract

Cerulein pancreatitis was shown to be one of the best characterized models for acute pancreatitis. High doses of cerulein induce a dysregulation of the digestive enzyme production and cytoplasmic vacuolization and the death of acinar cells, edema formation, and an infiltration of inflammatory cells into the pancreas, which are similar symptoms shown in human acute pancreatitis. The present study aims to determine the differentially expressed proteins in cerulein‐treated pancreatic acinar cells as an in vitro model for acute pancreatitis. Pancreatic acinar AR42J cells were treated with 10⁻⁸ M cerulein for 24 h. The changed protein patterns separated by two‐dimensional electrophoresis using pH gradients of 5–8 were conclusively identified by matrix‐assisted laser desorption/ionization‐time of flight mass spectrometry analysis of the peptide digests. Five differentially expressed proteins (heat shock protein 90, mitochondrial ATP synthase beta chain precursor, tubulin beta chain, 3‐mercaptopyruvate sulfurtransferase, mitochondrial ATP synthase subunit D) were identified in cerulein‐treated AR42J cells. These proteins are related to cellular stress such as reactive oxygen species, cytoskeletal function, and cell signaling. In conclusion, the differentially expressed proteins will provide valuable information to understand the pathophysiologic mechanism of acute pancreatitis and may be useful for prognostic indices of acute pancreatitis.