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The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation

Mucin-type O-glycosylation is initiated by the UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. Their activity results in the GalNAc α1-O-Thr/Ser structure, termed the Tn antigen, which is further decorated with additional sugars. In neoplastic cells, the Tn ant...

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Autores principales: Herbomel, Gaetan G., Rojas, Raul E., Tran, Duy T., Ajinkya, Monica, Beck, Lauren, Tabak, Lawrence A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5515409/
https://www.ncbi.nlm.nih.gov/pubmed/28719662
http://dx.doi.org/10.1371/journal.pone.0179241
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author Herbomel, Gaetan G.
Rojas, Raul E.
Tran, Duy T.
Ajinkya, Monica
Beck, Lauren
Tabak, Lawrence A.
author_facet Herbomel, Gaetan G.
Rojas, Raul E.
Tran, Duy T.
Ajinkya, Monica
Beck, Lauren
Tabak, Lawrence A.
author_sort Herbomel, Gaetan G.
collection PubMed
description Mucin-type O-glycosylation is initiated by the UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. Their activity results in the GalNAc α1-O-Thr/Ser structure, termed the Tn antigen, which is further decorated with additional sugars. In neoplastic cells, the Tn antigen is often overexpressed. Because O-glycosylation is controlled by the activity of GalNAc-Ts, their regulation is of great interest. Previous reports suggest that growth factors, EGF or PDGF, induce Golgi complex-to-endoplasmic reticulum (ER) relocation of both GalNAc-Ts and Tn antigen in HeLa cells, offering a mechanism for Tn antigen overexpression termed “GALA”. However, we were unable to reproduce these findings. Upon treatment of HeLa cells with either EGF or PDGF we observed no change in the co-localization of endogenous GalNAc-T1, GalNAc-T2 or Tn antigen with the Golgi complex marker TGN46. There was also no enhancement of localization with the ER marker calnexin. We conclude that growth factors do not cause redistribution of GalNAc-Ts from the Golgi complex to the ER in HeLa cells.
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spelling pubmed-55154092017-08-07 The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation Herbomel, Gaetan G. Rojas, Raul E. Tran, Duy T. Ajinkya, Monica Beck, Lauren Tabak, Lawrence A. PLoS One Research Article Mucin-type O-glycosylation is initiated by the UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. Their activity results in the GalNAc α1-O-Thr/Ser structure, termed the Tn antigen, which is further decorated with additional sugars. In neoplastic cells, the Tn antigen is often overexpressed. Because O-glycosylation is controlled by the activity of GalNAc-Ts, their regulation is of great interest. Previous reports suggest that growth factors, EGF or PDGF, induce Golgi complex-to-endoplasmic reticulum (ER) relocation of both GalNAc-Ts and Tn antigen in HeLa cells, offering a mechanism for Tn antigen overexpression termed “GALA”. However, we were unable to reproduce these findings. Upon treatment of HeLa cells with either EGF or PDGF we observed no change in the co-localization of endogenous GalNAc-T1, GalNAc-T2 or Tn antigen with the Golgi complex marker TGN46. There was also no enhancement of localization with the ER marker calnexin. We conclude that growth factors do not cause redistribution of GalNAc-Ts from the Golgi complex to the ER in HeLa cells. Public Library of Science 2017-07-18 /pmc/articles/PMC5515409/ /pubmed/28719662 http://dx.doi.org/10.1371/journal.pone.0179241 Text en https://creativecommons.org/publicdomain/zero/1.0/ This is an open access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 (https://creativecommons.org/publicdomain/zero/1.0/) public domain dedication.
spellingShingle Research Article
Herbomel, Gaetan G.
Rojas, Raul E.
Tran, Duy T.
Ajinkya, Monica
Beck, Lauren
Tabak, Lawrence A.
The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation
title The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation
title_full The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation
title_fullStr The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation
title_full_unstemmed The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation
title_short The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation
title_sort galnac-t activation pathway (gala) is not a general mechanism for regulating mucin-type o-glycosylation
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5515409/
https://www.ncbi.nlm.nih.gov/pubmed/28719662
http://dx.doi.org/10.1371/journal.pone.0179241
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