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UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-6 as a new immunohistochemical breast cancer marker.

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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

The calcitonin receptor on T 47D breast cancer cells. Evidence for glycosylation.

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The glycosyl nature of the receptor for the peptide hormone calcitonin has been investigated in a human breast cancer cell line, T 47D. Studies have been carried out to assess the ability of various lectins and of the antibiotic tunicamycin to inhibit specific binding of calcitonin to the cells, to

Immunolocalisation of members of the polypeptide N-acetylgalactosaminyl transferase (ppGalNAc-T) family is consistent with biologically relevant altered cell surface glycosylation in breast cancer.

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An extensive family of UDP-N-alpha-d-galactosamine: polypeptide N-acetylgalactosaminyltransferases (polypeptide N-acetylgalactosaminyltransferases, ppGalNAc-T's) catalyse the attachment of the first N-acetylgalactosamine (GalNAc) monosaccharide to the polypeptide at the initiation of O-linked

A transfected sialyltransferase that is elevated in breast cancer and localizes to the medial/trans-Golgi apparatus inhibits the development of core-2-based O-glycans.

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The alpha2,3 sialyltransferase, alpha2,3 SAT (O), catalyzes the transfer of sialic acid to Galbeta1,3 N-acetyl-D-galactosamine (GalNAc) (core-1) in mucin type O-glycosylation, and thus terminates chain extension. A Core-2 branch can also be formed from core-1 by the core-2 beta1,6

Structural basis for the regulation of UDP-N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyl transferase-3 gene expression in adenocarcinoma cells.

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The UDP-N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyl transferase-3 (Gal NAc-T3) gene, a member of the Gal NAc transferase gene family, is expressed in a tissue-specific manner. To elucidate the function of this gene, we have focused on the molecular mechanism underlying

GALNT6 Promotes Tumorigenicity and Metastasis of Breast Cancer Cell via β-catenin/MUC1-C Signaling Pathway.

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Polypeptide N-acetylgalactosaminyl transferase-6 (GALNT6), a member of the N-acetyl-D-galactosamine transferase family, was shown to be over-expression in mammary cancer and could be used as a biomarker. However, its roles and underlying mechanisms in the pathogenesis of breast cancer are still

N-Acetylgalactosaminyltransferase-14 as a potential biomarker for breast cancer by immunohistochemistry.

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BACKGROUND The post-translational modification of proteins, including glycosylation, differs between normal and tumor cells. The UDP-N-acetyl-D-galactosamine polypeptide N-acetylgalactosaminyltransferases (GalNAc-Tases) family of enzymes regulates the initial steps of mucin O-glycosylation and is

Prognostic utility of glycosyltransferase expression in breast cancer.

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BACKGROUND The post-translational modification of proteins, including glycosylation, is known to differ between normal and tumour cells. In this study, the expression profile of two glycosyltranferases, UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-6 (ppGalNAc-T6) and

p300/CBP-associated factor (P/CAF) interacts with nuclear respiratory factor-1 to regulate the UDP-N-acetyl-alpha-d-galactosamine: polypeptide N-acetylgalactosaminyltransferase-3 gene.

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We demonstrated recently that expression of the UDP- N -acetyl-alpha-D-galactosamine: polypeptide N -acetylgalactosaminyltrans-ferase-3 (GalNAc-T3) gene is restricted to epithelial glands [Nomoto, Izumi, Ise, Kato, Takano, Nagatani, Shibao, Ohta, Imamura, Kuwano, Matsuo, Yamada, Itoh and Kohno

O-linked mucin-type glycosylation in breast cancer.

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Changes in mucin-type O-linked glycosylation are seen in over 90% of breast cancers where increased sialylation is often observed and a change from branched glycans to linear glycans is often seen. There are many mechanisms involved including increased/altered expression of glycosyltransferases and

Histochemical tumor markers for evaluation of hormone dependence in breast cancer.

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Lectin from the peanut (peanut agglutinin = PNA) possesses a high affinity for D-galactosyl-(1-3)-N-acetyl-D-galactosamine, used for histochemical investigations on formalin-fixed tissue sections of normal mammary gland as well as of benign and malignant breast diseases. Thereby, a lectin-binding

The significance of lectin receptors for the evaluation of hormone dependence in breast cancer.

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Benign and malignant breast diseases were histochemically investigated with regard to their secretory function. Thereby, the labelled lectin from peanut (peanut agglutinin = PNA) which possesses a high affinity for D-galactosyl-(1-3)-N-acetyl-D-galactosamine, showed a binding pattern partly

Endogenous lectins with specificity to beta-galactosides and alpha- or beta-N-acetyl-galactosaminides in human breast cancer. Their glycohistochemical detection in tissue sections by synthetically different types of neoglycoproteins, their quantitation on cultured cells by neoglycoenzymes and their usefulness as targets in lectin-mediated phototherapy in vitro.

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Endogenous lectins may augment the panel of tumor markers. Specific protein-carbohydrate interactions especially involve carbohydrate moieties that are located at sequence termini, e.g. D-galactose and N-acetyl-D-galactosamine. Respective endogenous lectins can be detected by suitably constructed

Tn epitope (N-acetyl-D-galactosamine alpha-O-serine/threonine) density in primary breast carcinoma: a functional predictor of aggressiveness.

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This interpretive review attempts to dovetail advanced work by different groups of investigators on blood group and carcinoma (CA) glycoconjugates that have terminal, immunoreactive Tn epitopes (GalNAc alpha-O-Ser/Thr), and on the interaction of those structures with complementary antibodies and

Camptosemin, a tetrameric lectin of Camptosema ellipticum: structural and functional analysis.

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Lectins have been classified into a structurally diverse group of proteins that bind carbohydrates and glycoconjugates with high specificity. They are extremely useful molecules in the characterization of saccharides, as drug delivery mediators, and even as cellular surface makers. In this study, we

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