info:eu-repo/semantics/article
Glycosylation-dependent binding of galectin-8 to activated leukocyte cell adhesion molecule (ALCAM/CD166) promotes its surface segregation on breast cancer cells
Fecha
2016-04-26Registro en:
Fernández, Marisa Mariel; Ferragut, Fátima; Cardenas Delgado, Victor Manuel; Bracalente, María Candelaria; Bravo, Alicia Ines; et al.; Glycosylation-dependent binding of galectin-8 to activated leukocyte cell adhesion molecule (ALCAM/CD166) promotes its surface segregation on breast cancer cells; Elsevier Science; Biochimica et Biophysica Acta- General Subjects; 1860; 10; 26-4-2016; 2255-2268
0304-4165
1878-2434
CONICET Digital
CONICET
Autor
Fernández, Marisa Mariel
Ferragut, Fátima
Cardenas Delgado, Victor Manuel
Bracalente, María Candelaria
Bravo, Alicia Ines
Cagnoni, Alejandro
Nuñez, Myriam Carmen
Morosi, Luciano Gastón
Quintá, Héctor Ramiro
Espelt, Maria Victoria
Troncoso, María Fernanda
Wolfenstein, Carlota Elisa
Mariño, Karina Valeria
Malchiodi, Emilio Luis
Rabinovich, Gabriel Adrián
Elola, Maria Teresa
Resumen
We previously demonstrated that the activated leukocyte cell adhesion molecule (ALCAM/CD166) can interact with galectin-8 (Gal-8) in endothelial cells. ALCAM is a member of the immunoglobulin superfamily that promotes homophilic and heterophilic cell-cell interactions. Gal-8 is a "tandem-repeat"-type galectin, known as a matricellular protein involved in cell adhesion. Here, we analyzed the physical interaction between both molecules in breast cancer cells and the functional relevance of this phenomenon.