This article is part of the supplement: 11th International Symposium on the Cells of the Hepatic Sinusoid and their Relation to Other Cells .

Proceedings

Involvement of Galectin-1 and Galectin-3 in Proliferation and Migration of Rat Hepatic Stellate Cells in Culture

Naoto Maeda¹ , Norifumi Kawada¹ , Shuichi Seki¹ , Kazuo Ikeda² , Hiroaki Okuyama³ , Jun Hirabayashi⁴ , Ken-ichi Kasai⁴ and Katsutoshi Yoshizato⁵

¹  Department of Hepatology, Graduate School of Medicine, Osaka City University, Osaka 545-8585, Japan

²  Department Anatomy, Graduate School of Medicine, Osaka City University, Osaka 545-8585, Japan

³  Department of Gastroenterological Surgery, Graduate School of Medicine, Kyoto University, Kyoto 606-8397, Japan

⁴  Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Kanagawa 199-0195, Japan

⁵  Department of Biological Science, Graduate School of Science, Hiroshima University, Hiroshima 739-8526, Japan

author email corresponding author email

Comparative Hepatology 2004, 3(Suppl 1):S10doi:10.1186/1476-5926-2-S1-S10

Published:	14 January 2004

First paragraph (this article has no abstract)

Hepatic stellate cells (HSC), liver-specific pericytes, play a pivotal role in hepatic fibrogenesis. Galectin forms a group of animal lectins characterized by their specificity for beta-galactosides. At present, more than 10 galectins have been identified in mammals [1]. Galectin-1 forms a homodimer of 14 kDa subunits, and galectin-3 is a monomer having molecular weights of approximately 32 kDa. Galectin-1 and galectin-3 are localized not only in intracellular space such as the cytoplasm or the nucleus but also in extracellular space such as the cell surface or the extracellular matrix. Although the biological functions of galectin-1 and galectin-3 remain speculative in individual cells, tissues, or diseases, there is evidence that they play a role in cellular proliferation, differentiation, adhesion, neoplastic transformation, apoptosis, neoplastic and extracellular matrix interaction [2-4]. These functions are thought to act by cross-linking beta-galactoside containing glycoconjugates, resulting in modulation of cell signaling [5,6]. Here, we detail the expression pattern of galectin-1 and galectin-3 in activated HSC and in fibrotic liver tissues. We further show that both galectins are possible mitogens for HSC activating MAP kinase pathways presumably by cross-linking extracellular beta-galactoside.