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Originally published as JHC exPRESS on October 31, 2005.
doi:10.1369/jhc.5A6783.2005
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Journal of Histochemistry and Cytochemistry
Volume 54 (3): 317-328, 2006
Copyright ©The Histochemical Society, Inc.

UDP-N-Acetyl-D-Galactosamine: Polypeptide N-Acetylgalactosaminyltransferase-6 as a New Immunohistochemical Breast Cancer Marker

Nora Berois, Daniel Mazal, Luis Ubillos, Felipe Trajtenberg, André Nicolas, Xavier Sastre-Garau, Henri Magdelenat and Eduardo Osinaga

Departamento de Bioquímica, Laboratorio de Oncología Básica, Facultad de Medicina, Universidad de la República, Montevideo, Uruguay (NB,DM,LU,FT,EO), and Département de Biologie des Tumeurs, Institut Curie, Paris, France (AN,XS-G,HM)

Correspondence to: Eduardo Osinaga, MD, PhD, Depto. de Bioquímica, Facultad de Medicina, Av. Gral. Flores 2125, Montevideo CP 11800, Uruguay. E-mail: eosinaga{at}fmed.edu.uy

Mucin O-glycosylation is characterized in cancer by aberrant expression of immature carbohydrate structures (Tn, T, and sialyl-Tn antigens). The UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferases (ppGalNAc-T) family enzymes regulate the initial steps of mucin O-glycosylation and could be responsible for the altered glycosylation observed in cancer. Considering that we recently found the ppGalNAc-T6 mRNA expressed in breast carcinomas, we produced a highly specific monoclonal antibody (MAb T6.3) to assess the expression profile of ppGalNAc-T6 protein product in breast tissues. The expression of ppGalNAc-T6 by breast carcinoma cells was confirmed on MCF-7 and T47D cell lines. In formalin-fixed tissues, ppGalNAc-T6 expression was observed in 60/74 (81%) breast cancers, 21/23 (91.3%) adjacent ductal carcinoma in situ (DCIS), 4/20 benign breast lesions (2/2 sclerosing adenosis and 2/13 fibroadenoma), and in 0/5 normal breast samples. We observed a statistically significant association of ppGalNAc-T6 expression with T1 tumor stage. This fact, as well as the observation that ppGalNAc-T6 was strongly expressed in sclerosing adenosis and in most DCIS, suggests that ppGalNAc-T6 expression could be an early event during human breast carcinogenesis. Considering that an abnormal O-glycosylation greatly contributes to the phenotype and biology of breast cancer cells, ppGalNAc-T6 expression could provide new insights about breast cancer glycobiology. (J Histochem Cytochem 54:317–328, 2006)

Key Words: breast cancer • immunohistochemistry • O-glycosylation • UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferases • ppGalNAc-T6


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