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JHC exPRESS: First Published October 14, 2008. doi:10.1369/jhc.2008.952283
Journal of Histochemistry and Cytochemistry
Copyright © 2008 Gomes et al.

A more recent version of this article appeared on January 1, 2009.
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Expression of UDP-N-acetyl-D-galactosamine: Polypeptide N-acetylgalactosaminyltransferase-6 in Gastric Mucosa, Intestinal Metaplasia, and Gastric Carcinoma

Joana Gomes 1, Nuno T. Marcos 1, Nora Berois 1, Eduardo Osinaga 1, Ana Magalhães 1, João Pinto-de-Sousa 1, Raquel Almeida 1, Fátima Gärtner 1 and Celso A. Reis 1*

1 Institute of Molecular Pathology and Immunology of the University of Porto – IPATIMUP (JG,NTM,AM,RA,FG,CAR), Medical Faculty of the University of Porto (JPS,RA,CAR), and Institute of Biomedical Sciences of Abel Salazar - ICBAS (FG), University of Porto, Porto, Portugal, and Departamento de Inmunobiología, Facultad de Medicina, Universidad de la República and Institut Pasteur Montevideo, Montevideo, Uruguay (NB,EO)

* To whom correspondence should be addressed. E-mail: celso.reis{at}ipatimup.pt.

Submitted on July 18, 2008
Accepted on 23 September 2008


  Abstract
Aberrant mucin O-glycosylation is often observed in cancer and is characterized by the expression of immature simple mucin-type carbohydrate antigens. UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-6 (ppGalNAc-T6) is one of the enzymes responsible for the initial step in O-glycosylation. This study evaluated the expression of ppGalNAc-T6 in human gastric mucosa, intestinal metaplasia and gastric carcinomas. Our results showed that ppGalNAc-T6 is expressed in normal gastric mucosa and in intestinal metaplasia. A heterogeneous expression and staining pattern for this enzyme was observed in gastric carcinomas. ppGalNAc-T6 was expressed in 79% of the cases and its expression level was associated with the presence of venous invasion. Our results provide evidence that ppGalNAc-T6 is an immunohistochemical marker associated with venous invasion in gastric carcinoma, and may contribute to the understanding of the molecular mechanisms that underlie aberrant glycosylation in gastric carcinogenesis and in gastric carcinoma.

Key Words: mucin O-glycosylation, ppGalNAc-T6, gastric mucosa, intestinal metaplasia, gastric carcinoma


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