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GalNAc glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane

Over-expression of N-acetylgalactosamine glycoproteins as detected by binding of the lectin from Helix pomatia (HPA), is associated with metastatic competence and poor patient prognosis in a range of human adenocarcinomas. These glycoproteins remain poorly characterised, and their functional role ha...

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Detalles Bibliográficos
Autores principales: Brooks, S A, Hall, D M S, Buley, I
Formato: Texto
Lenguaje:English
Publicado: Nature Publishing Group 2001
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2375105/
https://www.ncbi.nlm.nih.gov/pubmed/11592774
http://dx.doi.org/10.1054/bjoc.2001.2028
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author Brooks, S A
Hall, D M S
Buley, I
author_facet Brooks, S A
Hall, D M S
Buley, I
author_sort Brooks, S A
collection PubMed
description Over-expression of N-acetylgalactosamine glycoproteins as detected by binding of the lectin from Helix pomatia (HPA), is associated with metastatic competence and poor patient prognosis in a range of human adenocarcinomas. These glycoproteins remain poorly characterised, and their functional role has yet to be elucidated. This study describes characterisation of a range of human breast/breast cancer cell lines for the expression of the N-acetylgalactosaminylated glycoproteins of interest, and their comparison with normal breast epithelium and a range of clinical breast carcinoma samples. Confocal and light microscopy studies revealed cytochemical HPA-binding patterns consistent with a fundamental disruption in normal glycobiosynthetic pathways attending increasing metastatic potential. We report the most complete comparative analysis of HPA-binding ligands from cultured breast cells, clinical breast carcinoma samples and normal breast epithelium to date. Lectin blotting identified 11 major HPA-binding glycoprotein bands common to both clinical tumour samples and breast cell lines and 6 of these bands were also expressed by samples of normal breast epithelium, albeit at much lower levels. Moreover, very marked quantitative but not qualitative differences in levels of expression consistent with metastatic capability were noted. © 2001 Cancer Research Campaignhttp://www.bjcancer.com
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spelling pubmed-23751052009-09-10 GalNAc glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane Brooks, S A Hall, D M S Buley, I Br J Cancer Regular Article Over-expression of N-acetylgalactosamine glycoproteins as detected by binding of the lectin from Helix pomatia (HPA), is associated with metastatic competence and poor patient prognosis in a range of human adenocarcinomas. These glycoproteins remain poorly characterised, and their functional role has yet to be elucidated. This study describes characterisation of a range of human breast/breast cancer cell lines for the expression of the N-acetylgalactosaminylated glycoproteins of interest, and their comparison with normal breast epithelium and a range of clinical breast carcinoma samples. Confocal and light microscopy studies revealed cytochemical HPA-binding patterns consistent with a fundamental disruption in normal glycobiosynthetic pathways attending increasing metastatic potential. We report the most complete comparative analysis of HPA-binding ligands from cultured breast cells, clinical breast carcinoma samples and normal breast epithelium to date. Lectin blotting identified 11 major HPA-binding glycoprotein bands common to both clinical tumour samples and breast cell lines and 6 of these bands were also expressed by samples of normal breast epithelium, albeit at much lower levels. Moreover, very marked quantitative but not qualitative differences in levels of expression consistent with metastatic capability were noted. © 2001 Cancer Research Campaignhttp://www.bjcancer.com Nature Publishing Group 2001-09 /pmc/articles/PMC2375105/ /pubmed/11592774 http://dx.doi.org/10.1054/bjoc.2001.2028 Text en Copyright © 2001 Cancer Research Campaign https://creativecommons.org/licenses/by/4.0/This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material.If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit https://creativecommons.org/licenses/by/4.0/.
spellingShingle Regular Article
Brooks, S A
Hall, D M S
Buley, I
GalNAc glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane
title GalNAc glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane
title_full GalNAc glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane
title_fullStr GalNAc glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane
title_full_unstemmed GalNAc glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane
title_short GalNAc glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane
title_sort galnac glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane
topic Regular Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2375105/
https://www.ncbi.nlm.nih.gov/pubmed/11592774
http://dx.doi.org/10.1054/bjoc.2001.2028
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AT buleyi galnacglycoproteinexpressionbybreastcelllinesprimarybreastcancerandnormalbreastepithelialmembrane