Korean J Gastroenterol.  2002 Oct;40(4):263-267.

The Role of Extracellular-signal-regulated Kinase and p38 in Trypsinogen Activation in Cerulein-Stimulated Rat Pancreatic Acini

Affiliations
  • 1Department of Internal Medicine, Seoul National University College of Medicine, Seoul, Korea. yongtkim@plaza.snu.ac.kr
  • 2Department of Liver Research Institute, Seoul National University College of Medicine, Seoul, Korea.

Abstract

BACKGROUND/AIMS: Intra-acinar cell activation of trypsinogen is a critical event in cerulein-induced pancreatitis. However, little is known about the intracellular signal transduction system that is involved in this process. The aim of this study was to elucidate the role of MAPKs (ERK and p38) in the pathogenesis of acute experimental pancreatitis.
METHODS
Pancreatic acinar cells were prepared from male Wistar rats. The acinar cells were pretreated with MEK inhibitor, PD98059, which suppresses ERK activation, or p38 inhibitor, SB203580. Then, the acinar cells were hyper-stimulated with 100 nM concentration of cerulein. The degree of trypsinogen activation was detected by measuring trypsin activity from acinar cell homogenates.
RESULTS
Cerulein stimulated phosphorylation of ERK and trypsinogen activation in the isolated pancreatic acini. However, PD98059 suppressed cerulein-induced ERK-phophorylation. Both PD98059 and SB203580 suppressed cerulein-induced trypsinogen activation in the pancreatic acini.
CONCLUSIONS
These results suggest that trypsinogen activation in cerulein-hyperstimulated acinar cells requires ERK and p38 pathways.

Keyword

Acute pancreatitis; Acinar cell; Trypsinogen; ERK; p38

MeSH Terms

Acinar Cells
Animals
Ceruletide
Humans
Male
Pancreatitis
Phosphorylation
Phosphotransferases*
Rats*
Rats, Wistar
Signal Transduction
Trypsin
Trypsinogen*
Ceruletide
Phosphotransferases
Trypsin
Trypsinogen
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