| |
Year:
2000
| Volume: 8
| Issue: 2
| Pages: 39-43
|
| |
Original Article |
| |
200 kDa GLYCOPROTEIN ISOLATED FROM BREAST CANCER TISSUE: A PUTATIVE LIGAND FOR GALECTIN-1
Miroslava JANKOVIC, Snezana GOLUBOVIC |
| |
DOI:
|
| |
Abstract: |
| |
Background: Interactions between lectins, carbohydrate-binding proteins, and glycoconjugates are important for the organisation of the cell and its response to regulatory factors. This study was aimed at isolation and characterization of the ligand for galectin-1, as a part of complex network of mutually interactive proteins expressed in breast cancer tissue.
Materials and Methods: Soluble protein extract of human breast cancer tissue was purified by affinity chromatography on gal-1-Sepharose column. The molecular mass of isolated material was determined by gel filtration and its glycosylation was examined by means of lectin-affinity chromatography and a solid phase binding assay using plant lectins and specific antibodies.
Results: A protein of molecular mass of 200 kDa was isolated from breast cancer tissue on the affinity column with immobilized gal-1. Ricinus communis agglutinin I, wheat germ agglutinin and Datura stramonium agglutinin were found to bind most effectively to purified galectin-1 binding protein. Accordingly, this protein could be characterized as a glycoprotein with the predominance of galactose- and N-acetylglucosamine-containing structures. 200 kDa protein displaying ligand properties, was recognized by monoclonal antibodies specific for MUC1 mucin. This suggested that its oligosaccharide structures may be expressed on MUC1 peptide backbone.
Conclusion: The binding of 200 kDa breast cancer tissue glycoprotein, having mucin-like protein backbone, by gal-1, presupposes their possible interactions in vivo. It focuses the attention to their importance for the regulation of cell activity in health and disease. |
| |
Key words:
Galectin-1;Breast cancer; Binding protein; Affinity chromatography; MUC1 |
| |
Read
full text in PDF [Full
Text] |
|
|