SUGAR CHAIN HETEROGENEITY OF HUMAN URINARY CHORIONIC-GONADOTROPIN DETERMINED BY SERIAL LECTIN AFFINITY-CHROMATOGRAPHY - DIFFERENCE BETWEEN BENIGN AND MALIGNANT DISEASE

Human chorionic gonadotropin (hCG) is a glycoprotein of which sugar ch ains are considered to show structural changes with malignancy. To stu dy the sugar chain heterogeneity of urinary hCG in patients with gynec ological disease, we employed serial lectin affinity chromatography (L AC) using concanavalin A (Con A) and phytohemagglutinin-E (PHA-E) whic h can separate N-glycoside-linked sugar chains, and Jacalin lectin whi ch is specific for O-glycoside-linked sugar chains. The proportion of hCG which did not bind to Con A was clearly higher in patients with ce rvical cancer than in healthy pregnant women. The complex-type sugar c hains bearing bisecting (beta 1-4) N-acetylglucosamine which bound to PHA-E increased in the early stage of cervical cancer, and tri- and te tra-antennary complex type sugar chains also increased in the advanced stages. In addition, the Jacalin-bound hCG increased significantly al ong with the stage of the cancer, especially in advanced cervical canc er with distant metastases. Taken together, these results show that al teration in sugar chain structures of hCG reflect the advanced stage o f cervical cancer.