Glycoproteins with O-glycosidically linked carbohydrate chains of complex s
tructures and functions are found in secretions and on the cell surfaces of
cancer cells. The structures of O-glycans are often unusual or abnormal in
cancer, and greatly contribute to the phenotype and biology of cancer cell
s. Some of the mechanisms of changes in O-glycosylation pathways have been
determined in cancer model systems. However, O-glycan biosynthesis is a com
plex process that is still poorly understood. The glycosyltransferases and
sulfotransferases that synthesize O-glycans appear to exist as families of
related enzymes of which individual members are expressed in a tissue- and
growth-specific fashion. Studies of their regulation in cancer may reveal t
he connection between cancerous transformation and glycosylation which may
help to understand and control the abnormal biology of tumor cells. Cancer
diagnosis may be based on the appearance of certain glycosylated epitopes,
and therapeutic avenues have been designed to attack cancer cells via their
glycans. (C) 1999 Elsevier Science B.V. All rights reserved.