Heat shock proteins (HSPs) have indispensable functions in the synthesis, degradation, folding, transport, and translocation of intracellular proteins. HSPs are proteins that help cells to survive stress conditions by repairing damaged proteins.
To investigate the potential effects of HSP preinduction by cold-water (CWI) or hot-water immersion (HWI) on sodium taurocholate (TC)-induced acute pancreatitis in rats.
TC was injected into the common biliopancreatic duct of the animals at the peak level of HSP synthesis, as determined by Western blot analysis. The rats were killed by exsanguination through the abdominal aorta 6 hours after the TC injection. The serum amylase activity, the IL-1, IL-6 and TNF-α levels, the pancreatic weight/body weight ratio, and the pancreatic contents of DNA, protein, amylase, lipase, and trypsinogen were measured, and a biopsy for histology was taken.
HWI significantly elevated HSP72 expression, whereas CWI significantly increased HSP60 expression. It was demonstrated that CWI pretreatment ameliorated the pancreatic edema and the serum amylase level increase, whereas the morphologic damage was more severe in this form of acute pancreatitis. HWI pretreatment did not have any effects on the measured parameters in TC-induced pancreatitis.
The findings suggest a possible role of HSP60, but not HSP72, in the slight protection in the early phase of this necrohemorrhagic pancreatitis model.
First Department of Medicine, *Department of Pathology, †Department of Microbiology, §Biological Isotope Laboratory, ∥ Department of Clinical Chemistry; ‡Hungarian Academy of Sciences, Biological Research Center, Institute of Biochemistry, Szeged, Hungary
Manuscript received November 21, 2000;
revised manuscript accepted March 20, 2001.
Address correspondence and reprint requests to Dr. Zoltán Rakonczay, First Dept. of Medicine, University of Szeged, H-6701 Szeged, P.O. Box: 469, Hungary. E-mail: email@example.com