The promigratory activity of the matricellular protein galectin-3 depends on the activation of PI-3 kinase.

The promigratory activity of the matricellular protein galectin-3 depends on the activation of PI-3 kinase.
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DOI:
10.1371/journal.pone.0029313
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发表时间:
2011
期刊:
影响因子:
3.7
通讯作者:
Chammas R
Chammas R
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Melo FH;Butera D;Junqueira Mde S;Hsu DK;da Silva AM;Liu FT;Santos MF;Chammas R

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Expression of galectin-3 is associated with sarcoma progression, invasion and metastasis. Here we determined the role of extracellular galectin-3 on migration of sarcoma cells on laminin-111. Cell lines from methylcholanthrene-induced sarcomas from both wild type and galectin-3−/− mice were established. Despite the presence of similar levels of laminin-binding integrins on the cell surface, galectin-3−/− sarcoma cells were more adherent and less migratory than galectin-3+/+ sarcoma cells on laminin-111. When galectin-3 was transiently expressed in galectin-3−/− sarcoma cells, it inhibited cell adhesion and stimulated the migratory response to laminin in a carbohydrate-dependent manner. Extracellular galectin-3 led to the recruitment of SHP-2 phosphatase to focal adhesion plaques, followed by a decrease in the amount of phosphorylated FAK and phospho-paxillin in the lamellipodia of migrating cells. The promigratory activity of extracellular galectin-3 was inhibitable by wortmannin, implicating the activation of a PI-3 kinase dependent pathway in the galectin-3 triggered disruption of adhesion plaques, leading to sarcoma cell migration on laminin-111.
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