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N-acetylgalactosaminyltransferases in cancer

Aberrant mucin-type O-glycosylation by glycosyltransferases is a well-described hallmark of many cancers and is also associated with additional non-cancerous developmental and metabolic disorders. The current review focuses on N-acetylgalactosaminyltransferase genes (GALNTs) and proteins (GalNAcTs)...

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Autores principales: Hussain, Muhammad Ramzan Manwar, Hoessli, Daniel C., Fang, Min
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Impact Journals LLC 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5288242/
https://www.ncbi.nlm.nih.gov/pubmed/27322213
http://dx.doi.org/10.18632/oncotarget.10042
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author Hussain, Muhammad Ramzan Manwar
Hoessli, Daniel C.
Fang, Min
author_facet Hussain, Muhammad Ramzan Manwar
Hoessli, Daniel C.
Fang, Min
author_sort Hussain, Muhammad Ramzan Manwar
collection PubMed
description Aberrant mucin-type O-glycosylation by glycosyltransferases is a well-described hallmark of many cancers and is also associated with additional non-cancerous developmental and metabolic disorders. The current review focuses on N-acetylgalactosaminyltransferase genes (GALNTs) and proteins (GalNAcTs) to illustrate their importance in cancer biology. Aberrant O-glycosylation by GalNAcTs activates a wide range of proteins that carry out interactions of sessile and motile cells affecting organogenesis, responses to agonists and stimulating hyperproliferation and metastatisation of neoplastic cells. As genome-wide analyses have provided abundant clues regarding under- or over-expressed genes that characterize different types of cancers, GALNTs and their transferase products have attracted attention by being unexpected actors in neoplastic contexts. We intend to review the current knowledge on GALNTs and their encoded transferases in cancer and suggest what could be the significance of such information in cancer pathogenesis and management.
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spelling pubmed-52882422017-02-07 N-acetylgalactosaminyltransferases in cancer Hussain, Muhammad Ramzan Manwar Hoessli, Daniel C. Fang, Min Oncotarget Review Aberrant mucin-type O-glycosylation by glycosyltransferases is a well-described hallmark of many cancers and is also associated with additional non-cancerous developmental and metabolic disorders. The current review focuses on N-acetylgalactosaminyltransferase genes (GALNTs) and proteins (GalNAcTs) to illustrate their importance in cancer biology. Aberrant O-glycosylation by GalNAcTs activates a wide range of proteins that carry out interactions of sessile and motile cells affecting organogenesis, responses to agonists and stimulating hyperproliferation and metastatisation of neoplastic cells. As genome-wide analyses have provided abundant clues regarding under- or over-expressed genes that characterize different types of cancers, GALNTs and their transferase products have attracted attention by being unexpected actors in neoplastic contexts. We intend to review the current knowledge on GALNTs and their encoded transferases in cancer and suggest what could be the significance of such information in cancer pathogenesis and management. Impact Journals LLC 2016-06-14 /pmc/articles/PMC5288242/ /pubmed/27322213 http://dx.doi.org/10.18632/oncotarget.10042 Text en Copyright: © 2016 Hussain et al. http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Review
Hussain, Muhammad Ramzan Manwar
Hoessli, Daniel C.
Fang, Min
N-acetylgalactosaminyltransferases in cancer
title N-acetylgalactosaminyltransferases in cancer
title_full N-acetylgalactosaminyltransferases in cancer
title_fullStr N-acetylgalactosaminyltransferases in cancer
title_full_unstemmed N-acetylgalactosaminyltransferases in cancer
title_short N-acetylgalactosaminyltransferases in cancer
title_sort n-acetylgalactosaminyltransferases in cancer
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5288242/
https://www.ncbi.nlm.nih.gov/pubmed/27322213
http://dx.doi.org/10.18632/oncotarget.10042
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