AJP - GI Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Gastrointest Liver Physiol 273: G937-G945, 1997;
0193-1857/97 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Strowski, M. Z.
Right arrow Articles by Wagner, A. C. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Strowski, M. Z.
Right arrow Articles by Wagner, A. C. C.
Vol. 273, Issue 4, G937-G945, October 1997

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

M. Z. Strowski1,2, G. Sparmann3, H. Weber4, F. Fiedler2, H. Printz1, L. Jonas5, B. Göke1, and A. C. C. Wagner1

Departments of 4 Pathobiochemistry, 5 Pathology, and 3 Gastroenterology, University of Rostock, D-18055 Rostock; 2 Department of Anesthesiology, Klinikum Mannheim, University of Heidelberg, D-68163 Heidelberg; and 1 Department of Gastroenterology, Philipps University, D-35033 Marburg, Germany

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 were decreased, as were 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.

HSP70; HSC70; pancreatic stress reaction


This article has been cited by other articles:


Home page
 GutHome page
M Tashiro, C Schafer, H Yao, S A Ernst, and J A Williams
Arginine induced acute pancreatitis alters the actin cytoskeleton and increases heat shock protein expression in rat pancreatic acinar cells
Gut, August 1, 2001; 49(2): 241 - 250.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
A. C. C. Wagner, L. Mazzucchelli, M. Miller, A. M. Camoratto, and B. Goke
CEP-1347 inhibits caerulein-induced rat pancreatic JNK activation and ameliorates caerulein pancreatitis
Am J Physiol Gastrointest Liver Physiol, January 1, 2000; 278(1): G165 - G172.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online