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Molecular cloning, gene organization and expression of the human UDP-GalNAc:Neu5Acalpha2-3Galbeta-R beta1,4-N-acetylgalactosaminyltransferase responsible for the biosynthesis of the blood group Sda/Cad antigen: evidence for an unusual extended cytoplasmic domain

MONTIEL, Maria-Dolores, KRZEWINSKI-RECCHI, Marie-Ange, DELANNOY, Philippe, HARDUIN-LEPERS, Anne·2003·Biochemical Journal
DOI 10.1042/bj20021892
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Abstract

The human Sda antigen is formed through the addition of an N-acetylgalactosamine residue via a β1,4-linkage to a sub-terminal galactose residue substituted with an α2,3-linked sialic acid residue. We have taken advantage of the previously cloned mouse cDNA sequence of the UDP-GalNAc:Neu5Acα2-3Galβ-R β1,4-N-acetylgalactosaminyltransferase (Sda β1,4GalNAc transferase) to screen the human EST and genomic databases and to identify the corresponding human gene. The sequence spans over 35 kb of genomic DNA on chromosome 17 and comprises at least 12 exons. As judged by reverse transcription PCR, the human gene is expressed widely since it is detected in various amounts in almost all cell types studied. Northern blot analysis indicated that five Sda β1,4GalNAc transferase transcripts of 8.8, 6.1, 4.7, 3.8 and 1.65 kb were highly expressed in colon and to a lesser extent in kidney, stomach, ileum and rectum. The complete coding nucleotide sequence was amplified from Caco-2 cells. Interestingly, the alternative use of two first exons, named E1S and E1L, leads to the production of two transcripts. These nucleotide sequences give rise potentially to two proteins of 506 and 566 amino acid residues, identical in their sequence with the exception of their cytoplasmic tail. The short form is highly similar (74% identity) to the mouse enzyme whereas the long form shows an unusual long cytoplasmic tail of 66 amino acid residues that is as yet not described for any other mammalian glycosyltransferase. Upon transient transfection in Cos-7 cells of the common catalytic domain, a soluble form of the protein was obtained, which catalysed the transfer of GalNAc residues to α2,3-sialylated acceptor substrates, to form the GalNAcβ1-4[Neu5Acα2-3]Galβ1-R trisaccharide common to both Sda and Cad antigens.

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  • Although the human B4GALNT2 gene is functional, its expression levels vary and naturally occurring mutations have been identified that correlate with the Sd(a-) phenotype.

    “Although the human B4GALNT2 gene is functional22, its expression levels vary and naturally occurring mutations have been identified that correlate with the Sd(a-) phenotype23.”

    From Design and testing of a humanized porcine donor for xenotransplantation (2023) · cites this paper as [22]

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Authors
MONTIEL, M.-D., KRZEWINSKI-RECCHI, M.-A., DELANNOY, P., & HARDUIN-LEPERS, A.
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
2003-07-15
Volume
373
Issue
2
Pages
369-379
ISSN
  • 0264-6021
  • 1470-8728
DOI
10.1042/bj20021892
Cited by
75
References
0
Language
en

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