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PMID: 14758075 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Role of galectin-8 as a modulator of cell adhesion and cell growth.

Glycoconjugate journal ·Vol. 19 ·No. 7-9 ·2002-00-00 ·Pages 517-26

Zick Y, Eisenstein M, Goren RA, Hadari YR, Levy Y, Ronen D

Abstract

Galectin-8 belongs to the family of tandem-repeat type galectins. It consists as several isoforms, each made of two domains of approximately 140 amino-acids, both having a carbohydrate recognition domain (CRD). These domains are joined by a 'link peptide' of variable length. The human galectin-8 gene covers 33 kbp of genomic DNA. It is localized on chromosome 1 (1q42.11) and contains 11 exons. The gene produces by alternative splicing 14 different transcripts, altogether encoding 6 proteins. Galectin-8, like other galectins, is a secreted protein. Upon secretion galectin-8 acts as a physiological modulator of cell adhesion. When immobilized, it functions as a matrix protein equipotent to fibronectin in promoting cell adhesion by ligation and clustering of a selective subset of cell surface integrin receptors. Complex formation between galectin-8 and integrins involves sugar-protein interactions and triggers integrin-mediated signaling cascades such as Tyr phosphorylation of FAK and paxillin. In contrast, when present in excess as a soluble ligand, galectin-8 (like fibronectin) forms a complex with integrins that negatively regulates cell adhesion. Such a mechanism allows local signals emitted by secreted galectin-8 to specify territories available for cell adhesion and migration. Due to its dual effects on the adhesive properties of cells and its association with fibronectin, galectin-8 might be considered as a novel type of a matricellular protein. Galectin-8 levels of expression positively correlate with certain human neoplasms, prostate cancer being the best example studied thus far. The overexpressed lectin might give these neoplasms some growth and metastasis related advantages due to its ability to modulate cell adhesion and cellular growth. Hence, galectin-8 may modulate cell-matrix interactions and regulate cellular functions in a variety of physiological and pathological conditions.

MeSH Terms
Animals Cell Adhesion Cell Division Galectins/chemistry,genetics,metabolism Humans Integrins/metabolism Neoplasms/metabolism
Chemicals
Galectins Integrins
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Zick Yehiel
Department of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot 76100, Israel. Yehiel.zick@weizmann.ac.il
Eisenstein Miriam
Goren Rinat A
Hadari Yaron R
Levy Yifat
Ronen Denise
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Article Info
Journal
Glycoconjugate journal
Abbr.
Glycoconj J
ISSN
0282-0080
Published
2002-00-00
Pages
517-26
Language
English
Region
United States
NLM ID
8603310
Subset
IM
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