Galectin-3, a laminin binding protein, fails to modulate adhesion of human melanoma cells to laminin

F. A. Van Den Brule, C. Buicu, M. E. Sobel, Fu-Tong Liu, V. Castronovo

Research output: Contribution to journalArticlepeer-review

34 Scopus citations


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 orA375 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.

Original languageEnglish (US)
Pages (from-to)215-219
Number of pages5
Issue number5
StatePublished - 1995
Externally publishedYes


  • adhesion
  • galectin-3
  • invasion
  • laminin
  • melanoma
  • metastasis

ASJC Scopus subject areas

  • Cancer Research


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