GLYCOPROTEIN CHANGES IN TUMORS - A RENAISSANCE IN CLINICAL-APPLICATIONS

1. Oligosaccharides linked to protein (glycoprotein) or lipid (glycoli pid) are the major components at the outer surface of mammalian cells. Studies using antibodies and lectins have shown in the past that the oligosaccharides they recognize exhibit tumour-associated changes, i.e . they are carbohydrate tumour-associated antigens. 2. The oligosaccha rides have been further characterized in recent years by structural an alysis using high-resolution chromatographic techniques, MS and NMR. N MR gives an oligosaccharide fingerprint that is characteristic of mono saccharide type and linkage and which can be correlated with magnetic resonance spectroscopic data on fine-needle tissue aspirates. 3. Also of relevance is the new understanding of the molecular biology of MUC genes, which code for mucin protein backbones, and of the glycosyltran sferase genes, which determine oligosaccharide structure and immunolog ical recognition. 4. For these reasons, we believe that tumour-associa ted oligosaccharide changes should be revisited in the context of what we now know about structure and expression. This review synopsizes th e past data using the detection of carbohydrate tumour-associated anti gens by binding of lectins and antibodies, and puts it into the contex t of NMR fingerprints or signatures.