Acute pancreatitis results in induction of heat shock proteins 70 and 27 and heat shock factor-1

Heat shock proteins (HSPs) 70 and 27 are stress-responsive proteins that ar e important for cell survival after injury; the expression of these HSPs is regulated primarily by the transcription factor heat shock factor-1 (HSF-1 ). The purpose of this study was to determine the effect of acute pancreati tis on pancreatic HSPs (70, 27, 60, and 90) expression and to assess potent ial mechanisms for HSP induction using a murine model of cerulein-induced p ancreatitis. We found an increase of both HSP70 and HSP27 levels with expre ssion noted throughout the pancreas after induction of pancreatitis. HSP60 and HSP90 levels were constitutively expressed in the pancreas and did not significantly change with acute pancreatitis. HSF-1 DNA binding activity in creased in accordance with increased HSP expression. We conclude that acute pancreatitis results in a marked increase in the expression of HSP70 and H SP27. Furthermore, the induction of HSP70 and HSP27 expression was associat ed with a concomitant increase in HSF-1 binding activity. The increased exp ression of both HSP70 and HSP27 noted with pancreatic inflammation may conf er a protective effect for the remaining acini after acute pancreatitis.