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

Fabiana H M Melo, Diego Butera, Mara Souza de Junqueira, Daniel K. Hsu, Ana Maria Moura da Silva, Fu-Tong Liu, Marinilice F. Santos, Roger Chammas

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


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.

Original languageEnglish (US)
Article numbere29313
JournalPLoS One
Issue number12
StatePublished - Dec 28 2011

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)


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