Caerulein pancreatitis increases mRNA but reduces protein levels of rat pancreatic heat shock proteins

被引:37
作者
Strowski, MZ
Sparmann, G
Weber, H
Fiedler, F
Printz, H
Jonas, L
Goke, B
Wagner, ACC
机构
[1] UNIV MARBURG, DEPT GASTROENTEROL, KLINIKUM LAHNBERGE, D-35033 MARBURG, GERMANY
[2] UNIV ROSTOCK, DEPT PATHOBIOCHEM, D-18055 ROSTOCK, GERMANY
[3] UNIV ROSTOCK, DEPT PATHOL, D-18055 ROSTOCK, GERMANY
[4] UNIV ROSTOCK, DEPT GASTROENTEROL, D-18055 ROSTOCK, GERMANY
[5] UNIV HEIDELBERG, DEPT ANESTHESIOL, KLINIKUM MANNHEIM, D-68163 HEIDELBERG, GERMANY
来源
AMERICAN JOURNAL OF PHYSIOLOGY-GASTROINTESTINAL AND LIVER PHYSIOLOGY | 1997年 / 273卷 / 04期
关键词
HSP70; HSC70; pancreatic stress reaction;
D O I
10.1152/ajpgi.1997.273.4.G937
中图分类号
R57 [消化系及腹部疾病];
学科分类号
摘要
We have recently reported that preconditioning through hyperthermia induces expression of pancreatic heat shock proteins (HSPs) and protects against caerulein pancreatitis. Here, we investigate caerulein-mediated effects on pancreatic HSPs without prior hyperthermia. Caerulein time and dose dependently increased pancreatic mRNA levels of the constitutive isoform of HSP70 (HSC70). However, pancreatic HSC70 protein levels mere decreased, as mere HSP60 protein levels. Also, in contrast to hyperthermia preconditioning, caerulein did not induce measurable levels of mRNA or protein of the inducible isoform of HSP70. Thus the pancreas reacts to different kinds of stress (hyperthermia vs. hyperstimulation) with differential induction of HSP mRNAs. Clearly, hyperthermia leads to induction of HSP protein expression, whereas caerulein treatment does not. Therefore, our current study further supports the idea that hyperthermia-induced protection against caerulein pancreatitis may be mediated through increased protein levels of pancreatic HSPs. It is further tempting to hypothesize that failure to appropriately increase HSP protein levels in response to high doses of caerulein might be a factor in the development of pancreatitis.
引用
收藏
页码:G937 / G945
页数:9
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