Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P17931 (galectin-3)
 2,860 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tumor invasion of host tissues and trophoblastic penetration of the endometrium share common biological features. Both processes involve the invasion of basement membranes, an event that is initiated by adhesion of cancer or trophoblast cells to basement membrane components and particularly to laminin. Adhesion to this latter glycoprotein is mediated through a variety of cell surface receptors. We have previously shown that the 67 kD Laminin Receptor (67LR) and a 31 kD Human Laminin Binding Protein, recently renamed galectin-3, are inversely modulated as the invasive phenotype of cancer cells progresses, with up regulation of the former, and down regulation of the latter, respectively. In this study, we examined the expression of these two proteins in 27 human trophoblastic specimens at different gestational ages using Northern and Western blot techniques. Expression of the 67LR increased from 7 weeks to a maximum at 12 weeks, when invasion is maximal, and then decreased. Expression of galectin-3 was inversely modulated by the gestational age, with a minimum expression at 12 weeks. Our data demonstrate that invasive trophoblast displays the same pattern of laminin binding proteins expression than invasive cancer cells, and further demonstrates that invasion of the extracellular matrix by trophoblast and cancer cells share common molecular mechanisms.
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PMID:Inverse expression of two laminin binding proteins, 67LR and galectin-3, correlates with the invasive phenotype of trophoblastic tissue. 819

Galectin-3 is a laminin binding protein which expression is altered in a variety of human carcinomas including colon, breast and endometrium. In these tumors, we consistently observed a down regulation of galectin-3 expression related to increased aggressiveness. Galectin-3 belongs to a family of galactose-binding lectins and binds laminin through its numerous poly-N-acetyllactosamine chains. To date, the exact role of galectin-3 in the complex interactions between cancer cells and laminin has not been clearly defined. Adhesion of melanoma cells to laminin is a critical event during tumor invasion and metastasis. In this study, we explore the possibility that galectin-3 could modulate attachment of two human melanoma cell lines to laminin. A2058 and A375 melanoma cell expressed galectin-3 on their surface as demonstrated by immunofluorescence, and attached to laminin in an in vitro assay. We demonstrate that neither recombinant galectin-3 nor an affinity purified antigalectin-3 antiserum altered adhesion of A2058 or A375 melanoma cells to laminin. Our data strongly suggest that galectin-3 is not a key element in adhesion of the melanoma cells to laminin. These results are not surprising in light of the observation that galectin-3 expression is down regulated in cancer and that increased adhesion to laminin is a constant feature of invasive cancer cells.
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PMID:Galectin-3, a laminin binding protein, fails to modulate adhesion of human melanoma cells to laminin. 855 98