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Imminent Angiotensin-converting Enzyme Inhibitor from Microbial Source for Cancer Therapy
BACKGROUND: Drugs targeting Angiotensin I-converting enzyme (ACE) have been used broadly in cancer chemotherapy. The recent past coupled with our results demonstrates the effective use of ACE inhibitors (ACEi) as anticancer agents, and they are potentially relevant in deriving new inhibitors. METHOD...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Medknow Publications & Media Pvt Ltd
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5651670/ https://www.ncbi.nlm.nih.gov/pubmed/29114378 http://dx.doi.org/10.4103/ijpvm.IJPVM_324_16 |
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author | Ebrahimi, Lida Ai, Jafar Alizadeh, Aliakbar Shariaty, Mehrdad |
author_facet | Ebrahimi, Lida Ai, Jafar Alizadeh, Aliakbar Shariaty, Mehrdad |
author_sort | Ebrahimi, Lida |
collection | PubMed |
description | BACKGROUND: Drugs targeting Angiotensin I-converting enzyme (ACE) have been used broadly in cancer chemotherapy. The recent past coupled with our results demonstrates the effective use of ACE inhibitors (ACEi) as anticancer agents, and they are potentially relevant in deriving new inhibitors. METHODS: Bacterial strains were isolated from cow milk collected in Coimbatore, Tamil Nadu, India and plated on nutrient agar medium. The identity of the strain was ascertained by 16s rRNA gene sequencing method and was submitted to the NCBI GenBank nucleotide database. Various substrates were screened for ACEi production by the fermentation with the isolated strain. ACEi was purified by sequential steps of ethanol precipitation, ion exchange column chromatography and gel filtration column chromatography. The apparent molecular mass was determined by SDS-PAGE. The anticancer property was analyzed by studying the cytotoxicity effects of ACEi using Breast cancer MCF-7 cell lines RESULTS: The isolate coded as BUCTL09 was selected and identified as Micrococcus luteus. Among the seven substrates, only beef extract fermented broth showed an inhibition of 79% and was reported as the best substrate. The peptide was purified and molecular mass was determined. The IC50 value of peptide was found to be 59.5 μg/ml. The purified peptide has demonstrated to induce apoptosis of cancer cell. CONCLUSIONS: The results of this study revealed that Peptide has been determined as an active compound that inhibited the activity of ACE. These properties indicate the possibilities of the use of purified protein as a potent anticancer agent. |
format | Online Article Text |
id | pubmed-5651670 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Medknow Publications & Media Pvt Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-56516702017-11-07 Imminent Angiotensin-converting Enzyme Inhibitor from Microbial Source for Cancer Therapy Ebrahimi, Lida Ai, Jafar Alizadeh, Aliakbar Shariaty, Mehrdad Int J Prev Med Original Article BACKGROUND: Drugs targeting Angiotensin I-converting enzyme (ACE) have been used broadly in cancer chemotherapy. The recent past coupled with our results demonstrates the effective use of ACE inhibitors (ACEi) as anticancer agents, and they are potentially relevant in deriving new inhibitors. METHODS: Bacterial strains were isolated from cow milk collected in Coimbatore, Tamil Nadu, India and plated on nutrient agar medium. The identity of the strain was ascertained by 16s rRNA gene sequencing method and was submitted to the NCBI GenBank nucleotide database. Various substrates were screened for ACEi production by the fermentation with the isolated strain. ACEi was purified by sequential steps of ethanol precipitation, ion exchange column chromatography and gel filtration column chromatography. The apparent molecular mass was determined by SDS-PAGE. The anticancer property was analyzed by studying the cytotoxicity effects of ACEi using Breast cancer MCF-7 cell lines RESULTS: The isolate coded as BUCTL09 was selected and identified as Micrococcus luteus. Among the seven substrates, only beef extract fermented broth showed an inhibition of 79% and was reported as the best substrate. The peptide was purified and molecular mass was determined. The IC50 value of peptide was found to be 59.5 μg/ml. The purified peptide has demonstrated to induce apoptosis of cancer cell. CONCLUSIONS: The results of this study revealed that Peptide has been determined as an active compound that inhibited the activity of ACE. These properties indicate the possibilities of the use of purified protein as a potent anticancer agent. Medknow Publications & Media Pvt Ltd 2017-10-05 /pmc/articles/PMC5651670/ /pubmed/29114378 http://dx.doi.org/10.4103/ijpvm.IJPVM_324_16 Text en Copyright: © 2017 International Journal of Preventive Medicine http://creativecommons.org/licenses/by-nc-sa/3.0 This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 License, which allows others to remix, tweak, and build upon the work non-commercially, as long as the author is credited and the new creations are licensed under the identical terms. |
spellingShingle | Original Article Ebrahimi, Lida Ai, Jafar Alizadeh, Aliakbar Shariaty, Mehrdad Imminent Angiotensin-converting Enzyme Inhibitor from Microbial Source for Cancer Therapy |
title | Imminent Angiotensin-converting Enzyme Inhibitor from Microbial Source for Cancer Therapy |
title_full | Imminent Angiotensin-converting Enzyme Inhibitor from Microbial Source for Cancer Therapy |
title_fullStr | Imminent Angiotensin-converting Enzyme Inhibitor from Microbial Source for Cancer Therapy |
title_full_unstemmed | Imminent Angiotensin-converting Enzyme Inhibitor from Microbial Source for Cancer Therapy |
title_short | Imminent Angiotensin-converting Enzyme Inhibitor from Microbial Source for Cancer Therapy |
title_sort | imminent angiotensin-converting enzyme inhibitor from microbial source for cancer therapy |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5651670/ https://www.ncbi.nlm.nih.gov/pubmed/29114378 http://dx.doi.org/10.4103/ijpvm.IJPVM_324_16 |
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