FIND ARTICLE

Volume: 
Issue: 
4
Date of issue: 

Galectin-3 is a member of a family of b-galactoside-binding animal lectins and is the only chimera type galectin. Galectin-3 consists of two structural domains: a N-terminal domain that contains a phosphorylation site and a repeated 9 amino acids sequence rich in Pro, Gly, Tyr and Glu; and a C-terminal domain that contains a carbohydrate recognition domain. In human genome galectin-3 is coded by a single gene LGALS3 which is situated on chromosome 14 and composed of six exons and five introns. Galectin-3 is localized in the cytoplasm as well as in the nucleus. Galectin-3 is involved in many biological processes, such as: cell-cell and cell-extracellular matrix adhesion, mRNA splicing, cell growth and differentiation, cell cycle, signaling, apoptosis and angiogenesis. Consequently, galectin-3 is involved in regulation immune reaction, tumor growth and metastasis. Despite of fact that galectin-3 is synthesised by free ribosomes in the cytosol and lacks signal sequence, there are evidence for its extracellular localization. Differential galectin-3 distribution is associated with many functions it performs in the cell.

Author of the article: 

The Editorial Board
Andrzej Łukaszyk - przewodniczący, Zofia Bielańska-Osuchowska, Szczepan Biliński, Mieczysław Chorąży, Aleksander Koj, Włodzimierz Korochoda, Leszek Kuźnicki, Aleksandra Stojałowska, Lech Wojtczak

Editorial address:
Katedra i Zakład Histologii i Embriologii Uniwersytetu Medycznego w Poznaniu, ul. Święcickiego 6, 60-781 Poznań, tel. +48 61 8546453, fax. +48 61 8546440, email: mnowicki@ump.edu.pl

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