Heat shock proteins (HSPs) are part of the cellular stress response machinery. HSPs are expressed in the pancreas, but their protective potential has not been thoroughly investigated. The aim of this study was to characterize the pancreatic heat shock response both in vitro and in vivo and to study whether this response has protective effects.

For in vitro experiments, rat pancreatic acini were exposed to heat and protein expression was analyzed through 35S-methionine labeling or Western blots. In vivo, cerulein pancreatitis was induced after whole body hyperthermia (42 degrees C).

After thermal stress (42 degrees C), acini increasingly expressed five proteins of 92, 72, 59, 58, and 30 kilodaltons, with HSP. 70 the most strongly induced 72-kilodalton protein. In vivo, increased expression of four isoforms of pancreatic HSP-70 was found. Isoform-specific antibodies identified the inducible and constitutively expressed (HSC-70) isoform of HSP-70. HSP-60 was also weakly induced after hyperthermia. Concomitantly, cerulein-induced pancreatic organ damage was greatly reduced after whole-body hyperthermia. The time course and strength of HSP induction correlated well with the time course and degree of protection against cerulein- induced pancreatitis.

A causal relation between hyperthermia-induced HSP expression and organ protection seems possible. (Gastroenterology 1996 Nov;111(5):1333-42)