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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
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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. |
format | Online Article Text |
id | pubmed-5515409 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
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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