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Core-Fucosylated Tetra-Antennary N-Glycan Containing A Single N-Acetyllactosamine Branch Is Associated with Poor Survival Outcome in Breast Cancer

(1) Glycoproteins account for ~80% of proteins located at the cell surface and in the extracellular matrix. A growing body of evidence indicates that α-L-fucose protein modifications contribute to breast cancer progression and metastatic disease. (2) Using a combination of techniques, including matr...

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Autores principales: Herrera, Harmin, Dilday, Tinslee, Uber, Allison, Scott, Danielle, Zambrano, Joelle N., Wang, Mengjun, Angel, Peggi M., Mehta, Anand S., Drake, Richard R., Hill, Elizabeth G., Yeh, Elizabeth S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6566954/
https://www.ncbi.nlm.nih.gov/pubmed/31126011
http://dx.doi.org/10.3390/ijms20102528
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author Herrera, Harmin
Dilday, Tinslee
Uber, Allison
Scott, Danielle
Zambrano, Joelle N.
Wang, Mengjun
Angel, Peggi M.
Mehta, Anand S.
Drake, Richard R.
Hill, Elizabeth G.
Yeh, Elizabeth S.
author_facet Herrera, Harmin
Dilday, Tinslee
Uber, Allison
Scott, Danielle
Zambrano, Joelle N.
Wang, Mengjun
Angel, Peggi M.
Mehta, Anand S.
Drake, Richard R.
Hill, Elizabeth G.
Yeh, Elizabeth S.
author_sort Herrera, Harmin
collection PubMed
description (1) Glycoproteins account for ~80% of proteins located at the cell surface and in the extracellular matrix. A growing body of evidence indicates that α-L-fucose protein modifications contribute to breast cancer progression and metastatic disease. (2) Using a combination of techniques, including matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI-IMS) based in cell and on tissue imaging and glycan sequencing using exoglycosidase analysis coupled to hydrophilic interaction ultra-high performance liquid chromatography (HILIC UPLC), we establish that a core-fucosylated tetra-antennary glycan containing a single N-acetyllactosamine (F(6)A4G4Lac1) is associated with poor clinical outcomes in breast cancer, including lymph node metastasis, recurrent disease, and reduced survival. (3) This study is the first to identify a single N-glycan, F(6)A4G4Lac1, as having a correlation with poor clinical outcomes in breast cancer.
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spelling pubmed-65669542019-06-17 Core-Fucosylated Tetra-Antennary N-Glycan Containing A Single N-Acetyllactosamine Branch Is Associated with Poor Survival Outcome in Breast Cancer Herrera, Harmin Dilday, Tinslee Uber, Allison Scott, Danielle Zambrano, Joelle N. Wang, Mengjun Angel, Peggi M. Mehta, Anand S. Drake, Richard R. Hill, Elizabeth G. Yeh, Elizabeth S. Int J Mol Sci Article (1) Glycoproteins account for ~80% of proteins located at the cell surface and in the extracellular matrix. A growing body of evidence indicates that α-L-fucose protein modifications contribute to breast cancer progression and metastatic disease. (2) Using a combination of techniques, including matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI-IMS) based in cell and on tissue imaging and glycan sequencing using exoglycosidase analysis coupled to hydrophilic interaction ultra-high performance liquid chromatography (HILIC UPLC), we establish that a core-fucosylated tetra-antennary glycan containing a single N-acetyllactosamine (F(6)A4G4Lac1) is associated with poor clinical outcomes in breast cancer, including lymph node metastasis, recurrent disease, and reduced survival. (3) This study is the first to identify a single N-glycan, F(6)A4G4Lac1, as having a correlation with poor clinical outcomes in breast cancer. MDPI 2019-05-23 /pmc/articles/PMC6566954/ /pubmed/31126011 http://dx.doi.org/10.3390/ijms20102528 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Herrera, Harmin
Dilday, Tinslee
Uber, Allison
Scott, Danielle
Zambrano, Joelle N.
Wang, Mengjun
Angel, Peggi M.
Mehta, Anand S.
Drake, Richard R.
Hill, Elizabeth G.
Yeh, Elizabeth S.
Core-Fucosylated Tetra-Antennary N-Glycan Containing A Single N-Acetyllactosamine Branch Is Associated with Poor Survival Outcome in Breast Cancer
title Core-Fucosylated Tetra-Antennary N-Glycan Containing A Single N-Acetyllactosamine Branch Is Associated with Poor Survival Outcome in Breast Cancer
title_full Core-Fucosylated Tetra-Antennary N-Glycan Containing A Single N-Acetyllactosamine Branch Is Associated with Poor Survival Outcome in Breast Cancer
title_fullStr Core-Fucosylated Tetra-Antennary N-Glycan Containing A Single N-Acetyllactosamine Branch Is Associated with Poor Survival Outcome in Breast Cancer
title_full_unstemmed Core-Fucosylated Tetra-Antennary N-Glycan Containing A Single N-Acetyllactosamine Branch Is Associated with Poor Survival Outcome in Breast Cancer
title_short Core-Fucosylated Tetra-Antennary N-Glycan Containing A Single N-Acetyllactosamine Branch Is Associated with Poor Survival Outcome in Breast Cancer
title_sort core-fucosylated tetra-antennary n-glycan containing a single n-acetyllactosamine branch is associated with poor survival outcome in breast cancer
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6566954/
https://www.ncbi.nlm.nih.gov/pubmed/31126011
http://dx.doi.org/10.3390/ijms20102528
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