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2,3Galß-R ß1,4(GalNAc to Gal) N-Acetylgalactosaminyltransferase Involved in the Synthesis of Sda Antigen in Human Large Intestine and Colorectal Carcinomas1
Dipartimento di Patologia Sperimentale, Università di Bologna [N. M., F. D., G. D., F. S-C.], and Istituto di Clinica Chirurgica I, Policlinico S. Orsola [F. M., D. M.], Bologna, Italy
N-Acetylgalactosamine ß1,4-linked to a galactose residue substituted in O-3 with one N-acetylneuraminic acid residue is the immunodominant sugar of the human blood group Sda antigen which is also largely present in the kidney medulla and colon mucosa. A ß1,4-N-acetylgalactosaminyltransferase very similar to that previously described in urine of Sd(a+) individuals (F. Serafini-Cessi, N. Malagolini, and F. Dall'Olio. Arch. Biochem. Biophys., 266: 573582, 1988) has been identified in cells released from human large intestine. The higher values of ß1,4-N-acetylgalactosaminyltransferase activity were detected in proximal and medial segments of the large intestine, suggesting a proximal-distal gradient of the enzyme expression. When the ß1,4-N-acetylgalactosaminyltransferase activity of colorectal carcinoma specimens from 18 patients was compared with that of the normal mucosa surrounding the tumor, a constant and in several cases drastic reduction of the activity was detected in tumor cells. Three human colorectal adenocarcinoma cell lines (Colo-205, SW-48, and SW-948) have been found to lack the ß1,4-N-acetylgalactosaminyltransferase activity. Altogether, these results support the notion that the malignant transformation drastically affects the expression of this glycosyltransferase in large bowel cells.
1 Supported by the Associazione Italiana per la Ricerca sul Cancro and CNR-Progetto Finalizzato Oncologia.
2 To whom requests for reprints should be addressed, at Dipartimento Patologia Sperimentale, Via S. Giacomo 14, 40126 Bologna, Italy.
Received 4/25/89. Revised 7/21/89. Accepted 8/29/89.
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