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J. Biochem, 2003, Vol. 134, No. 5 675-682
© 2003 Japanese Biochemical Society

MOLECULAR BIOLOGY

Molecular Cloning of the Human ß1,4 N-Acetylgalactosaminyltransferase Responsible for the Biosynthesis of the Sda Histo-Blood Group Antigen: The Sequence Predicts a Very Long Cytoplasmic Domain

Libera Lo Presti, Erik Cabuy*, Mariella Chiricolo and Fabio Dall’Olio§

Dipartimento di Patologia Sperimentale, Università di Bologna, Via S. Giacomo 14, 40126, Bologna, Italy

The Sda antigen is a carbohydrate determinant expressed on erythrocytes, the colonic mucosa and other tissues. This epitope, whose structure is Sia{alpha}2,3[GalNAcß1,4]Gal ß1,4GlcNAc, is synthesized by a ß1,4 N-acetylgalactosaminyltransferase (ß4GalNAc-T) that transfers a ß1,4-linked GalNAc to the galactose residue of an {alpha}2,3-sialylated chain. We have cloned from human colon carcinoma Caco2 cells a cDNA whose transfection in COS cells induces a GalNAc-T active on sialylated but not on asialylated fetuin and putatively represents the human Sda ß4GalNAc-T. The cDNA predicts a 566 aa protein showing 66.6% and 39% identity with mouse CT ß4GalNAc-T and human GM2/GD2 synthase, respectively, with a typical type II glycosyltransferase organization, no potential N-glycosylation sites and a 67 aa cytoplasmic tail, which is probably the longest among the glycosyltransferases cloned to date. The gene maps in chromosome 17q23, and is composed of at least 11 exons. Exons 2–11 are homologous to exons 2–11 of the previously cloned CT ß4GalNAc-T from murine cytotoxic T lymphocytes while exons 1 of the two enzymes are totally different. The mRNA is expressed at a high level in differentiated Caco2 cells and in colonic mucosa and at a much lower level in lymphocytes and other colon cancer cell lines.

* Present address: Genetic Cancer Susceptibility Unit, IARC, 150 Cours Albert Thomas, 69372 Lyon cedex 08, France

§ To whom correspondence should be addressed. Fax: +39-05-1209-4746, E-mail: dallolio{at}alma.unibo.it


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