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Vol. 302, Issue 1, 36-42, July 2002
Division of Gastroenterology, Tohoku University Graduate School of
Medicine, Sendai, Japan
Alcohol is a major cause of both acute and chronic pancreatitis.
Activated pancreatic stellate cells (PSCs) have recently been
implicated in the pathogenesis of pancreatic inflammation and fibrosis.
Herein, we examined the effect of ethanol and acetaldehyde on the
activation of transcription factors and mitogen-activated protein (MAP)
kinases in PSCs. PSCs were isolated from rat pancreas tissue and used
in their culture-activated, myofibroblast-like phenotype. PSCs were
treated with ethanol and acetaldehyde at clinically relevant
concentrations (50 mM and 200 µM, respectively). Ethanol and
acetaldehyde activated activator protein-1 but not nuclear factor-
B.
In addition, they activated three classes of MAP kinases: extracellular
signal-regulated kinase 1/2, c-Jun N-terminal kinase/stress-activated
protein kinase, and p38 MAP kinase. Ethanol- and acetaldehyde-induced
activation of activator protein-1 and MAP kinases was blocked by
the antioxidant N-acetyl-cysteine, suggesting a role of
oxidative stress in the signal transduction. Ethanol and acetaldehyde
induced 
1(I) procollagen gene expression but did not induce
intercellular adhesion molecule-1 and monocyte chemoattractant
protein-1. The acetaldehyde-induced increase of 1(I) procollagen
gene expression was inhibited by the p38 MAP kinase inhibitor
4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)imidazole (SB203580) but not by the MAP kinase inhibitor
2'-amino-3'-methoxyflavone (PD98059). Specific activation of these
signal transduction pathways may play a role in the pathogenesis of
alcohol-induced pancreatic injury.
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