Differential expression of glycosyltransferases has the potential to generate functionally distinct glycoforms of otherwise identical proteins. We have previously demonstrated the presence of unique oligosaccharides terminating with GalNAc-4-SO on the pituitary glycoproteins lutropin (LH), thyroid stimulating hormone (TSH), and pro-opiomelanocortin (POMC). A glycoprotein hormone:GalNAc-transferase and a GalNAc-4-sulfotransferase are present in the pituitary and can account for the synthesis of these unique oligosaccharides on specific glycoproteins. Both transferases are coordinately expressed in a number of tissues in addition to pituitary, including submaxillary gland, lacrimal gland, and kidney, suggesting that additional glycoproteins bearing oligosaccharides terminating with GalNAc-4-SO are synthesized in these tissues. In this study we show that while the glycoprotein hormone:GalNAc-transferase and the GalNAc-4-sulfotransferase are coordinately expressed in bovine submaxillary gland, the GalNAc-transferase is expressed in the parotid gland in the absence of the GalNAc-4-sulfotransferase. The relative expression of these two transferases in submaxillary and parotid glands correlates with the presence of unique Asn-linked oligosaccharides on carbonic anhydrase VI (CA VI) synthesized in each of these tissues. The majority of Asn-linked oligosaccharides on CA VI synthesized in submaxillary gland terminate with GalNAc-4-SO. In contrast, CA VI which is synthesized in bovine parotid gland bears oligosaccharides which terminate predominantly with 1,4-linked GalNAc which is not sulfated. The presence of different terminal residues on the Asn-linked oligosaccharides of submaxillary and parotid CA VI thus correlates with the complement of transferases in these glands and suggests differing biological roles for submaxillary and parotid CA VI.

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