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Angiotensin-converting enzyme and enkephalinase in human breast cyst fluid.
Palpable breast cysts with an apocrine epithelial lining (type 1) are reported to be associated with a higher risk of developing breast cancer. The composition of breast cyst fluid (BCF) might include those factors involved in this increased risk. In this study peptidase activities that were active...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Nature Publishing Group
1996
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2074695/ https://www.ncbi.nlm.nih.gov/pubmed/8795586 |
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author | Frame, K. L. Patton, K. Reed, M. J. Ghilchik, M. W. Parish, D. C. |
author_facet | Frame, K. L. Patton, K. Reed, M. J. Ghilchik, M. W. Parish, D. C. |
author_sort | Frame, K. L. |
collection | PubMed |
description | Palpable breast cysts with an apocrine epithelial lining (type 1) are reported to be associated with a higher risk of developing breast cancer. The composition of breast cyst fluid (BCF) might include those factors involved in this increased risk. In this study peptidase activities that were active against the substrate [125I]metenkephalin-Arg-Phe were detected in BCF. The products were identified by reversed phase high-performance liquid chromatography (HPLC) as [125I]Tyr-Gly-Gly and [125I]Met-enkephalin. This proteolysis was not inhibited by PCMB, pepstatin A, leupeptin or aprotinin but was by EDTA, showing that the activity was due to metalloproteases. The production of [125I]Try-Gly-Gly was inhibited by phosphoramidon and thiorphan, whereas that of [125I]met-enkephalin was inhibited by captopril and Bothrops jararaca peptide, indicating that these activities are enkephalinase and angiotensin-converting enzyme (ACE) respectively. A fluorometric assay for ACE demonstrated that ACE levels are significantly higher in type 2 BCF than in type 1 BCF (30.8 vs 6.1 nmol hr-1 10 microliters-1, P < 0.001). As the increased risk of cancer is linked to type 1 cysts it is possible that higher levels of peptidase in type 2 BCF reflect a protective environment in the breast in which mitogenic peptide growth factors are neutralised by proteolysis. |
format | Text |
id | pubmed-2074695 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1996 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-20746952009-09-10 Angiotensin-converting enzyme and enkephalinase in human breast cyst fluid. Frame, K. L. Patton, K. Reed, M. J. Ghilchik, M. W. Parish, D. C. Br J Cancer Research Article Palpable breast cysts with an apocrine epithelial lining (type 1) are reported to be associated with a higher risk of developing breast cancer. The composition of breast cyst fluid (BCF) might include those factors involved in this increased risk. In this study peptidase activities that were active against the substrate [125I]metenkephalin-Arg-Phe were detected in BCF. The products were identified by reversed phase high-performance liquid chromatography (HPLC) as [125I]Tyr-Gly-Gly and [125I]Met-enkephalin. This proteolysis was not inhibited by PCMB, pepstatin A, leupeptin or aprotinin but was by EDTA, showing that the activity was due to metalloproteases. The production of [125I]Try-Gly-Gly was inhibited by phosphoramidon and thiorphan, whereas that of [125I]met-enkephalin was inhibited by captopril and Bothrops jararaca peptide, indicating that these activities are enkephalinase and angiotensin-converting enzyme (ACE) respectively. A fluorometric assay for ACE demonstrated that ACE levels are significantly higher in type 2 BCF than in type 1 BCF (30.8 vs 6.1 nmol hr-1 10 microliters-1, P < 0.001). As the increased risk of cancer is linked to type 1 cysts it is possible that higher levels of peptidase in type 2 BCF reflect a protective environment in the breast in which mitogenic peptide growth factors are neutralised by proteolysis. Nature Publishing Group 1996-09 /pmc/articles/PMC2074695/ /pubmed/8795586 Text en 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 | Research Article Frame, K. L. Patton, K. Reed, M. J. Ghilchik, M. W. Parish, D. C. Angiotensin-converting enzyme and enkephalinase in human breast cyst fluid. |
title | Angiotensin-converting enzyme and enkephalinase in human breast cyst fluid. |
title_full | Angiotensin-converting enzyme and enkephalinase in human breast cyst fluid. |
title_fullStr | Angiotensin-converting enzyme and enkephalinase in human breast cyst fluid. |
title_full_unstemmed | Angiotensin-converting enzyme and enkephalinase in human breast cyst fluid. |
title_short | Angiotensin-converting enzyme and enkephalinase in human breast cyst fluid. |
title_sort | angiotensin-converting enzyme and enkephalinase in human breast cyst fluid. |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2074695/ https://www.ncbi.nlm.nih.gov/pubmed/8795586 |
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