Background. CD44 represents a heterogeneous group of surface glycoproteins
involved in cell-cell and cell-matrix interactions. CD44H is the major rece
ptor for hyaluronate, and most if not all CD44H known functions are attribu
ted to its ability to recognize hyaluronate. We have previously demonstrate
d a lack of CD44 expression in high stages and NMYC-amplified tumors and fu
rther have shown that NMYC-amplified cell lines either did not express CD44
at all or expressed a nonfunctional receptor. On the other hand, nonamplif
ied cells constitutively expressed an active receptor, suggesting that abse
nce of CD44-mediated hyaluronate binding could be related to increased mali
gnancy in human neuroblastoma. Procedure. In the present study we have comp
ared the glycosylated structure of CD44 expressed by NMYC amplified vs. non
amplified cell lines in relation to their adhesive properties for hyalurona
te. These adhesive properties were measured after modifications of the carb
ohydrate structure with enzymes and inhibitors of N- or O-linked glycosylat
ion. Results and Conclusions. Our results indicate that increased sialylati
on, defective N-linked glycosylation, and substitution of the CD44 glycopro
tein with keratan sulfate glycosaminoglycan might include modifications obs
erved on neuroblastoma cells that could account for the inability of the re
ceptor to bind hyaluronate. Med. Pediatr. Oncol. 36:139-141, 2001. (C) 2001
Wiley-Liss, Inc.