Article: article from journal or magazin.
Role of CD44H carbohydrate structure in neuroblastoma adhesive properties.
Medical and pediatric oncology
Publication types: Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't - Publication Status: ppublish
BACKGROUND: CD44 represents a heterogeneous group of surface glycoproteins involved in cell-cell and cell-matrix interactions. CD44H is the major receptor for hyaluronate, and most if not all CD44H known functions are attributed to its ability to recognize hyaluronate. We have previously demonstrated a lack of CD44 expression in high stages and NMYC-amplified tumors and further have shown that NMYC-amplified cell lines either did not express CD44 at all or expressed a nonfunctional receptor. On the other hand, nonamplified cells constitutively expressed an active receptor, suggesting that absence of CD44-mediated hy aluronate binding could be related to increased malignancy in human neuroblastoma. PROCEDURE: In the present study we have compared the glycosylated structure of CD44 expressed by NMYC amplified vs. nonamplified cell lines in relation to their adhesive properties for hyaluronate. These adhesive properties were measured after modifications of the carbohydrate structure with enzymes and inhibitors of N- or O-linked glycosylation. RESULTS AND CONCLUSIONS: Our results indicate that increased sialylation, defective N-linked glycosylation, and substitution of the CD44 glycoprotein with keratan sulfate glycosaminoglycan might include modifications observed on neuroblastoma cells that could account for the inability of the receptor to bind hyaluronate.
1-Deoxynojirimycin, Acetylgalactosamine, Antigens, CD44, Blotting, Western, Carbohydrate Conformation, Cell Adhesion, Colonic Neoplasms, Gene Amplification, Genes, myc, Glycosylation, Humans, Hyaluronic Acid, Molecular Weight, Neoplasm Proteins, Neuraminidase, Neuroblastoma, Protein Binding, Protein Processing, Post-Translational, Recombinant Fusion Proteins, Transfection, Tunicamycin
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