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Am J Physiol Gastrointest Liver Physiol (December 22, 2005). doi:10.1152/ajpgi.00511.2005
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Submitted on October 31, 2005
Accepted on December 18, 2005

Galectin-1 induces chemokine production and proliferation in pancreatic stellate cells

Atsushi Masamune1*, Masahiro Satoh1, Jun Hirabayashi2, Kenichi Kasai3, Kennichi Satoh1, and Tooru Shimosegawa1

1 Division of Gastroenterology, Tohoku University Graduate School of Medicine, Sendai, Miyagi, Japan
2 Glycostructure Analysis Team, Research Center for Gycoscience, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaragi, Japan
3 Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Sagamiko, Kanagawa, Japan

* To whom correspondence should be addressed. E-mail: amasamune{at}int3.med.tohoku.ac.jp.

Galectin-1 is a {beta}-galactoside-binding lectin. Previous studies have shown that galectin-1 was expressed in fibroblasts of chronic pancreatitis and of desmoplastic reaction associated with pancreatic cancer. These fibroblasts are now recognized as activated pancreatic stellate cells (PSCs). We here examined the role of galectin-1 in cell functions of PSCs. PSCs were isolated from rat pancreas tissue and used in their culture-activated phenotype unless otherwise stated. Expression of galectin-1 was assessed by Western blotting, reverse transcription-PCR, and immunofluorescent staining. The effects of recombinant galectin-1 on chemokine production and proliferation were evaluated. Activation of transcription factors was assessed by electrophoretic mobility shift assay. Activation of MAP kinases was examined by Western blotting using anti-phosphospecific antibodies. Galectin-1 was strongly expressed in culture-activated, but not freshly isolated, PSCs. Recombinant galectin-1 increased proliferation and production of monocyte chemoattractant protein-1 and cytokine-induced neutrophil chemoattractant-1. Galectin-1 activated ERK, JNK, activator protein-1, and NF-{kappa}B, but not p38 MAP kinase or Akt. Galectin-1 induced proliferation through ERK, and chemokine production mainly through the activation of NF-{kappa}B, and in part by JNK and ERK pathways. These effects of galectin-1 were abolished in the presence of thiodigalactosie, an inhibitor of {beta}-galactoside binding. In conclusion, our results suggest a role of galectin-1 in chemokine production and proliferation through its {beta}-galactoside binding activity in activated PSCs.




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