Relevant bibliographies by topics / GalNAc-T6

Academic literature on the topic 'GalNAc-T6'

Author: Grafiati
Published: 11 March 2023

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Journal articles on the topic "GalNAc-T6"

1

Ubillos, Luis, Mariela Rondan, Edgardo Berriel, Daniel Mazal, Enrique Barrios, Nora Berois, and Eduardo Osinaga. "Immunihistochemical detection of galNAc-T6 to predict survival in patients with colon cancer." Journal of Clinical Oncology 31, no. 15_suppl (May 20, 2013): e14682-e14682. http://dx.doi.org/10.1200/jco.2013.31.15_suppl.e14682.

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e14682 Background: Alterations in the O-glycosylation is one of the most common changes during colon carcinogenesis, which leads to the expression of short O-glycan antigens (Tn, sialyl-Tn, Tk, and core 6). These structures are associated with malignant behavior being actively investigated as targets for immunotherapy. The enzymes of GalNAc-T family regulate the initial step in mucins O-glycosylation and could be responsible for the altered glycosylation observed in cancer. The aim of this work was to evaluate the expression of GalNAc-T6 in colon cancer, and to determine its role as prognostic marker. Methods: We evaluated GalNAc-T6 expression in colon cell lines by immunocytochemistry, and in colon cancer tissue samples by immunohistochemistry using the monoclonal antibody T6.3 developed by us (Berois et al. J Histochem Cytochem. 2006). We analyzed 103 colon cancer samples and 10 normal colon tissues. Results: We found that GalNAc-T6 (usually expressed in normal placenta, trachea, pancreas and brain) is detected in colon cancer cell lines. GalNAc-T6 was also detected by immunohistochemistry in 50.5% of samples with cancer and no expression was found in normal colon tissue. The staining pattern was predominantly cytoplasmic. Multivariate analysis showed that GalNAc-T6 expression is an independent prognostic marker predicting improved survival in patients with positive tumors (p 0.014). Conclusions: GalNAc-T6 could be a new independent prognostic marker to predict better outcome in colon cancer patients.
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2

Sheta, Razan, Magdalena Bachvarova, Elizabeth Macdonald, Stephane Gobeil, Barbara Vanderhyden, and Dimcho Bachvarov. "The polypeptide GALNT6 Displays Redundant Functions upon Suppression of its Closest Homolog GALNT3 in Mediating Aberrant O-Glycosylation, Associated with Ovarian Cancer Progression." International Journal of Molecular Sciences 20, no. 9 (May 8, 2019): 2264. http://dx.doi.org/10.3390/ijms20092264.

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Epithelial ovarian cancer (EOC) represents the most lethal gynecologic malignancy; a better understanding of the molecular mechanisms associated with EOC etiology could substantially improve EOC management. Aberrant O-glycosylation in cancer is attributed to alteration of N-acetylgalactosaminyltransferases (GalNAc-Ts). Reports suggest a genetic and functional redundancy between GalNAc-Ts, and our previous data are indicative of an induction of GALNT6 expression upon GALNT3 suppression in EOC cells. We performed single GALNT3 and double GALNT3/T6 suppression in EOC cells, using a combination of the CRISPR-Cas9 system and shRNA-mediated gene silencing. The effect of single GALNT3 and double GALNT3/T6 inhibition was monitored both in vitro (on EOC cells roliferation, migration, and invasion) and in vivo (on tumor formation and survival of experimental animals). We confirmed that GALNT3 gene ablation leads to strong and rather compensatory GALNT6 upregulation in EOC cells. Moreover, double GALNT3/T6 suppression was significantly associated with stronger inhibitory effects on EOC cell proliferation, migration, and invasion, and accordingly displayed a significant increase in animal survival rates compared with GALNT3-ablated and control (Ctrl) EOC cells. Our data suggest a possible functional redundancy of GalNAc-Ts (GALNT3 and T6) in EOC, with the perspective of using both these enzymes as novel EOC biomarkers and/or therapeutic targets.
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Marcos, Nuno T., Andrea Cruz, Filipe Silva, Raquel Almeida, Leonor David, Ulla Mandel, Henrik Clausen, Silvia von Mensdorff-Pouilly, and Celso A. Reis. "Polypeptide GalNAc-transferases, ST6GalNAc-transferase I, and ST3Gal-transferase I Expression in Gastric Carcinoma Cell Lines." Journal of Histochemistry & Cytochemistry 51, no. 6 (June 2003): 761–71. http://dx.doi.org/10.1177/002215540305100607.

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Mucin O-glycosylation in cancer is characterized by aberrant expression of immature carbohydrate structures leading to exposure of simple mucin-type carbohydrate antigens and peptide epitopes. Glycosyltransferases controlling the initial steps of mucin O-glycosylation are responsible for the altered glycosylation observed in cancer. We studied the expression in gastric cell lines of six UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-T1, T2, T3, T4, T6, T11) that catalyze the initial key step in the regulation of mucin O-glycosylation, the transfer of GalNAc from UDP-GalNAc to serine and threonine residues. We also studied the expression of ST6GalNAc-I, the enzyme responsible for the synthesis of Sialyl-Tn antigen (NeuAcα2,6GalNAc) and the ST3Gal-I, the enzyme responsible for the synthesis of Sialyl-T antigen (NeuAcα2,3Galβ1,3GalNAc). This study was done using specific monoclonal antibodies, enzymatic assays, and RT-PCR. Our results showed that GalNAc-T1, -T2, and -T3 have an ubiquitous expression in all gastric cell lines, whereas GalNAc-T4, -T6, and -T11 show a restricted expression pattern. The immunoreactivity with MAb VU-2-G7 suggests that, apart from GalNAc-T4, another GalNAc transferase is involved in the glycosylation of the Thr in the PDTR region of the MUC1 tandem repeat. The expression of ST3Gal-I correlates with the expression of the Sialyl-T antigen in gastric cell lines and in the control cell lines studied. The expression of ST6GalNAc-I is low in gastric cell lines, in accordance with the low/absent expression of the Sialyl-Tn antigen.
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Akasaka-Manya, Keiko, Masaki Kawamura, Hiroki Tsumoto, Yuko Saito, Yuriko Tachida, Shinobu Kitazume, Hiroyuki Hatsuta, et al. "Excess APPO-glycosylation by GalNAc-T6 decreases Aβ production." Journal of Biochemistry 161, no. 1 (October 19, 2016): 99–111. http://dx.doi.org/10.1093/jb/mvw056.

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5

Daniel, Earnest James Paul, Matilde las Rivas, Erandi Lira-Navarrete, Ana García-García, Ramon Hurtado-Guerrero, Henrik Clausen, and Thomas A. Gerken. "Ser and Thr acceptor preferences of the GalNAc-Ts vary among isoenzymes to modulate mucin-type O-glycosylation." Glycobiology 30, no. 11 (April 18, 2020): 910–22. http://dx.doi.org/10.1093/glycob/cwaa036.

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Abstract A family of polypeptide GalNAc-transferases (GalNAc-Ts) initiates mucin-type O-glycosylation, transferring GalNAc onto hydroxyl groups of Ser and Thr residues of target substrates. The 20 GalNAc-T isoenzymes in humans are classified into nine subfamilies according to sequence similarity. GalNAc-Ts select their sites of glycosylation based on weak and overlapping peptide sequence motifs, as well prior substrate O-GalNAc glycosylation at sites both remote (long-range) and neighboring (short-range) the acceptor. Together, these preferences vary among GalNAc-Ts imparting each isoenzyme with its own unique specificity. Studies on the first identified GalNAc-Ts showed Thr acceptors were preferred over Ser acceptors; however studies comparing Thr vs. Ser glycosylation across the GalNAc-T family are lacking. Using a series of identical random peptide substrates, with single Thr or Ser acceptor sites, we determined the rate differences (Thr/Ser rate ratio) between Thr and Ser substrate glycosylation for 12 isoenzymes (representing 7 GalNAc-T subfamilies). These Thr/Ser rate ratios varied across subfamilies, ranging from ~2 to ~18 (for GalNAc-T4/GalNAc-T12 and GalNAc-T3/GalNAc-T6, respectively), while nearly identical Thr/Ser rate ratios were observed for isoenzymes within subfamilies. Furthermore, the Thr/Ser rate ratios did not appreciably vary over a series of fixed sequence substrates of different relative activities, suggesting the ratio is a constant for each isoenzyme against single acceptor substrates. Finally, based on GalNAc-T structures, the different Thr/Ser rate ratios likely reflect differences in the strengths of the Thr acceptor methyl group binding to the active site pocket. With this work, another activity that further differentiates substrate specificity among the GalNAc-Ts has been identified.
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6

Lavrsen, Kirstine, Sally Dabelsteen, Sergey Y. Vakhrushev, Asha M. R. Levann, Amalie Dahl Haue, August Dylander, Ulla Mandel, et al. "De novoexpression of human polypeptideN-acetylgalactosaminyltransferase 6 (GalNAc-T6) in colon adenocarcinoma inhibits the differentiation of colonic epithelium." Journal of Biological Chemistry 293, no. 4 (November 29, 2017): 1298–314. http://dx.doi.org/10.1074/jbc.m117.812826.

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7

Banford, Samantha, and David Timson. "UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase- 6 (pp-GalNAc-T6): Role in Cancer and Prospects as a Drug Target." Current Cancer Drug Targets 17, no. 1 (December 2, 2016): 53–61. http://dx.doi.org/10.2174/1568009616666160922102641.

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8

Bennett, Eric Paul, Helle Hassan, Ulla Mandel, Michael A. Hollingsworth, Naoaki Akisawa, Yoshito Ikematsu, Gerard Merkx, Ad Geurts van Kessel, Sigvard Olofsson, and Henrik Clausen. "Cloning and Characterization of a Close Homologue of Human UDP-N-acetyl-α-d-galactosamine:PolypeptideN-Acetylgalactosaminyltransferase-T3, Designated GalNAc-T6." Journal of Biological Chemistry 274, no. 36 (September 3, 1999): 25362–70. http://dx.doi.org/10.1074/jbc.274.36.25362.

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9

Park, JH, and Y. Nakamura. "GALNT6 (UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 6 (GalNAc-T6))." Atlas of Genetics and Cytogenetics in Oncology and Haematology, no. 2 (January 2014). http://dx.doi.org/10.4267/2042/53080.

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10

Ubillos, Luis, Edgardo Berriel, Daniel Mazal, Sabina Victoria, Enrique Barrios, Eduardo Osinaga, and Nora Berois. "Polypeptide‑GalNAc‑T6 expression predicts better overall survival in patients with colon cancer." Oncology Letters, May 10, 2018. http://dx.doi.org/10.3892/ol.2018.8686.

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