Two Soluble Forms of β1,4-Galactosyltransferase Released from Ovarian Cancer Cells and from COS-1 Cells Transfected with its cDNA (<Symposium I>Recent Progresses in Carbohydrate Histochemistry)

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Employing RMG-1 cells derived from human ovarian adenocarcinoma and COS-1 cells transfected with cDNA for β1,4-galactosyltransferase, we first investigated the intracellular localization of this enzyme and secondly assayed separately the two types of souble forms of it (designated as normal GalT and GAT) in their culture supernatants. As results, the binding of anti-β1,4-galactosyltansferase monoclonal antibody was strongly positive at the Golgi area surrounding nuclei and the staining pattern was the same between RMG-1 cells and COS-1 trnasformants. These data demonstrated that the cells were producing β1,4-galactosyltransferase and had the ability to release in into the culture medium. As for the two soluble forms released from the cells, they were simultaneously detected in the culture medium by Western blotting and enzyme immunoassay using monoclonal antibodies, i.e., Mab8628 reactive to both GAT and normal-GalT and Mab8513 specific for GAT, indicating that both were derived from RMG-1 and from the cDNA introduced into COS-1 cells. Since serum-GAT clinically reflects turmor growth more accurately or specifically than normal GalT does, RMG-1 and COS-1 cells having cDNA for β1,4-galactosyltransferase would be promising as sources of these enzymes in order to investigate the differences in the behaviors of normal GalT and GAT associated with ovarian malignant tumors.
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