Sugar Chain Heterogeneity of Human Urinary Chorionic Gonadotropin Determined by Serial Lectin Affinity Chromatography: Difference between Benign and Malignant Disease

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Abstract
Human chorionic gonadotropin (hCG) is a glycoprotein of which sugar chains are considered to show structural changes with malignancy. To study the sugar chain heterogeneity of urinary hCG in patients with gynecological disease, we employed serial lectin affinity chromatography (LAC) using con-canavalin A (Con A) and phytohemagglutinin-E (PHA-E) which can separate N-glycoside-linked sugar chains, and Jacal-in lectin which 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 cervical cancer than in healthy pregnant women. The complex-type sugar chains bearing bisecting (β1-4) N-acetylglucosamine which bound to PHA-E increased in the early stage of cervical cancer, and tri- and tetra-antenna-ry complex type sugar chains also increased in the advanced stages. In addition, the Jacalin-bound hCG increased significantly along with the stage of the cancer, especially in advanced cervical cancer with distant metastases. Taken together, these results show that alteration in sugar chain structures of hCG reflect the advanced stage of cervical cancer.

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