N. Lemarer et Rc. Hughes, EFFECTS OF THE CARBOHYDRATE-BINDING PROTEIN GALECTIN-3 ON THE INVASIVENESS OF HUMAN BREAST-CARCINOMA CELLS, Journal of cellular physiology, 168(1), 1996, pp. 51-58
Galectin-3 is a Mr 30,000 protein with carbohydrate-binding specificit
y for type I and II ABH blood group epitopes and polylactosamine glyca
ns expressed on cell surface and extracellular matrix glycoproteins su
ch as laminin. Cell lines propagated from human normal mammary epithel
ia and from benign or infiltrating components of primary breast tumour
s express low levels of galectin-3 in the cytoplasm. However, galectin
-3 when added exogenously in solution or when bound within a three-dim
ensional matrix markedly enhanced the migration of the primary tumour
cell lines through a Matrigel barrier. Galectin-3 expression in the cy
toplasm and intercellularly on surface membranes was greatly increased
in cell lines propagated from malignant ascites and pleural effusions
of late stage breast cancer. These cell lines were non-invasive in th
e Matrigel assay and exogenous galectin-3 had no enhancing effect on i
nvasiveness. These results suggest that galectin-3 could play multiple
roles in cell metastasis at an early invasive stage by acting in a pa
racrine manner to stimulate cell migration through an extracellular ma
trix, and in later stage cancers in synergy with other mediators of ce
ll-cell aggregation. However,endogenous galectin-3 expression in human
breast cancers is not correlated directly with their invasive potenti
al in vitro. (C) 1996 Wiley-Liss, Inc.