Fa. Vandenbrule et al., GALECTIN-1 MODULATES HUMAN-MELANOMA CELL-ADHESION TO LAMININ, Biochemical and biophysical research communications, 209(2), 1995, pp. 760-767
Galectins constitute a gene family of beta-galactoside-specific lectin
s that show high homology in their carbohydrate-binding site. They hav
e been postulated to be involved in many biological events, but their
specific functions are not yet well defined. Galectin-1 is a laminin b
inding protein that recognizes poly N-acetyllactosamine chains on this
major basement membrane glycoprotein. In this study, we analyzed the
possibility that galectin-1 could modulate interactions between human
melanoma cells and laminin. We demonstrated that A375 and A2058 cell l
ines express galectin-1 both intracellularly and on the cell surface.
in an in vitro assay, recombinant galectin-1 increased melanoma cell a
ttachment to laminin in a dose-dependent manner. This effect was aboli
shed by lactose. Anti-galectin-1 inhibited adhesion of melanoma cells
to laminin in a However, neither galectin-1 nor anti-galectin-1 antibo
dy affected melanoma cell spreading on laminin in vitro. These data in
dicate that galectin-1 might participate in melanoma cell adhesion to
laminin and therefore could be a modulator of invasion and metastasis.
(C) 1995 Academic Press, Inc.