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Proteolysis in human breast and colorectal cancer
Proteolysis occurs when proteinase activity exceeds inhibitor activity. Proteolysis is normally tightly regulated and is involved in cancer invasion and metastasis. The aim of this study was to compare proteolysis in breast and colorectal cancer. Proteinase and inhibitor expression were analysed in...
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Formato: | Texto |
Lenguaje: | English |
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Nature Publishing Group
1999
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2362855/ https://www.ncbi.nlm.nih.gov/pubmed/10496354 http://dx.doi.org/10.1038/sj.bjc.6690689 |
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author | Garbett, E A Reed, M W R Brown, N J |
author_facet | Garbett, E A Reed, M W R Brown, N J |
author_sort | Garbett, E A |
collection | PubMed |
description | Proteolysis occurs when proteinase activity exceeds inhibitor activity. Proteolysis is normally tightly regulated and is involved in cancer invasion and metastasis. The aim of this study was to compare proteolysis in breast and colorectal cancer. Proteinase and inhibitor expression were analysed in paired tumour and normal tissue samples from 43 breast and 24 colorectal cancer patients using substrate zymography, Western blotting and quenched fluorescence substrate hydrolysis. The expression of the latent forms of matrix metalloproteinase-2 (MMP-2), MMP-3 and MMP-9, urokinase plasminogen activator (uPA), tissue inhibitor of metalloproteinase-1 (TIMP-1) and TIMP-2 expression were observed in both tumour and normal tissue samples from breast and colorectal tissue; however, expression was greater in the tumour tissue. Expression of active MMP-2 and MMP-9 and the total MMP activity were greater in tumour compared to normal samples in both tissues (P< 0.05). The expression of all proteinases and total MMP activity was greater in colorectal tissue than breast tissue samples. Breast and colorectal cancer demonstrated different proteinase profiles, however proteolysis in both tissues was greater in tumour tissue than normal tissue. © 1999 Cancer Research Campaign |
format | Text |
id | pubmed-2362855 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1999 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-23628552009-09-10 Proteolysis in human breast and colorectal cancer Garbett, E A Reed, M W R Brown, N J Br J Cancer Regular Article Proteolysis occurs when proteinase activity exceeds inhibitor activity. Proteolysis is normally tightly regulated and is involved in cancer invasion and metastasis. The aim of this study was to compare proteolysis in breast and colorectal cancer. Proteinase and inhibitor expression were analysed in paired tumour and normal tissue samples from 43 breast and 24 colorectal cancer patients using substrate zymography, Western blotting and quenched fluorescence substrate hydrolysis. The expression of the latent forms of matrix metalloproteinase-2 (MMP-2), MMP-3 and MMP-9, urokinase plasminogen activator (uPA), tissue inhibitor of metalloproteinase-1 (TIMP-1) and TIMP-2 expression were observed in both tumour and normal tissue samples from breast and colorectal tissue; however, expression was greater in the tumour tissue. Expression of active MMP-2 and MMP-9 and the total MMP activity were greater in tumour compared to normal samples in both tissues (P< 0.05). The expression of all proteinases and total MMP activity was greater in colorectal tissue than breast tissue samples. Breast and colorectal cancer demonstrated different proteinase profiles, however proteolysis in both tissues was greater in tumour tissue than normal tissue. © 1999 Cancer Research Campaign Nature Publishing Group 1999-09 /pmc/articles/PMC2362855/ /pubmed/10496354 http://dx.doi.org/10.1038/sj.bjc.6690689 Text en Copyright © 1999 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 Garbett, E A Reed, M W R Brown, N J Proteolysis in human breast and colorectal cancer |
title | Proteolysis in human breast and colorectal cancer |
title_full | Proteolysis in human breast and colorectal cancer |
title_fullStr | Proteolysis in human breast and colorectal cancer |
title_full_unstemmed | Proteolysis in human breast and colorectal cancer |
title_short | Proteolysis in human breast and colorectal cancer |
title_sort | proteolysis in human breast and colorectal cancer |
topic | Regular Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2362855/ https://www.ncbi.nlm.nih.gov/pubmed/10496354 http://dx.doi.org/10.1038/sj.bjc.6690689 |
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