The Promigratory Activity of the Matricellular Protein Galectin-3 Depends on the Activation of PI-3 Kinase
Melo, Fabiana H. M; Butera, Diego; Junqueira, Mara de Souza; Hsu, Daniel K; Silva, Ana Maria Moura da; Liu, Fu Tong; Santos, Marinilice F; Chammas, Roger.
PLos ONE
; 6(12): 1-11, Dec.2011.
Artículo
en Inglés
| SES-SP, SESSP-IBPROD, SES-SP, SESSP-IBACERVO | ID: biblio-1065094
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-32/2 mice were established. Despite the presence of similar levels of laminin-binding integrins on the cell surface, galectin-32/2 sarcoma cells were more adherent and less migratory than galectin-3+/+ sarcomacells on laminin-111. When galectin-3 was transiently expressed in galectin-32/2 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 FAKand phospho-paxillin in the lamellipodia of migrating cells. The promigratory activity of extracellular galectin-3 wasinhibitable 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.
Biblioteca responsable:
BR78.1
Ubicación: BR78.1
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