Structural changes induced in the sugar chains of glycoproteins by malignant transformation of producing cells and their clinical application.

Altered glycosylation is widely observed in glycoproteins produced by tumors. One of the most consistently observed alterations is the increase of larger asparagine-linked sugar chains in the plasma membrane glycoproteins. This phenomenon is brought about by the increase of N-acetylglucosaminyltransferase V, which is responsible for the formation of the GlcNAc beta 1----6Man alpha-1----6 group. The enrichment of the complex-type sugar chains containing the -GlcNAc beta 1----6(-GlcNAc beta 1----2)Man alpha 1----6 group is correlated with tumorigenicity and metastasic potential of tumor cells. Comparative study of the sugar chains of human chorionic gonadotropin isolated from the urine of pregnant women and of patients with trophoblastic diseases including choriocarcinoma revealed that many new oligosaccharides are included in the tumor hCG. The altered glycosylation of hCG is brought about by the ectopic expression of N-acetylglucosaminyltransferase IV. With use of this altered glycosylation, a novel method useful for the diagnosis of choriocarcinoma was established.