The promigratory activity of the matricellular protein galectin-3 depends on the activation of PI-3 kinase |
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Authors: | Melo Fabiana H M Butera Diego Junqueira Mara de Souza Hsu Daniel K da Silva Ana Maria Moura Liu Fu-Tong Santos Marinilice F Chammas Roger |
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Institution: | Departamento de Radiologia e Oncologia, Faculdade de Medicina da Universidade de S?o Paulo, S?o Paulo, S?o Paulo, Brazil. |
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Abstract: | 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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