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Proteomic analysis of human spermatozoa proteins with oxidative stress
BACKGROUND: Oxidative stress plays a key role in the etiology of male infertility. Significant alterations in the sperm proteome are associated with poor semen quality. The aim of the present study was to examine if elevated levels of reactive oxygen species cause an alteration in the proteomic prof...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3716960/ https://www.ncbi.nlm.nih.gov/pubmed/23688036 http://dx.doi.org/10.1186/1477-7827-11-48 |
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author | Sharma, Rakesh Agarwal, Ashok Mohanty, Gayatri Hamada, Alaa J Gopalan, Banu Willard, Belinda Yadav, Satya du Plessis, Stefan |
author_facet | Sharma, Rakesh Agarwal, Ashok Mohanty, Gayatri Hamada, Alaa J Gopalan, Banu Willard, Belinda Yadav, Satya du Plessis, Stefan |
author_sort | Sharma, Rakesh |
collection | PubMed |
description | BACKGROUND: Oxidative stress plays a key role in the etiology of male infertility. Significant alterations in the sperm proteome are associated with poor semen quality. The aim of the present study was to examine if elevated levels of reactive oxygen species cause an alteration in the proteomic profile of spermatozoa. METHODS: This prospective study consisted of 52 subjects: 32 infertile men and 20 normal donors. Seminal ejaculates were classified as ROS+ or ROS- and evaluated for their proteomic profile. Samples were pooled and subjected to LC-MS/MS analysis through in-solution digestion of proteins for peptide characterization. The expression profile of proteins present in human spermatozoa was examined using proteomic and bioinformatic analysis to elucidate the regulatory pathways of oxidative stress. RESULTS: Of the 74 proteins identified, 10 proteins with a 2-fold difference were overexpressed and 5 were underexpressed in the ROS+ group; energy metabolism and regulation, carbohydrate metabolic processes such as gluconeogenesis and glycolysis, protein modifications and oxidative stress regulation were some of the metabolic processes affected in ROS+ group. CONCLUSIONS: We have identified proteins involved in a variety of functions associated with response and management of oxidative stress. In the present study we focused on proteins that showed a high degree of differential expression and thus, have a greater impact on the fertilizing potential of the spermatozoa. While proteomic analyses identified the potential biomarkers, further studies through Western Blot are necessary to validate the biomarker status of the proteins in pathological conditions. |
format | Online Article Text |
id | pubmed-3716960 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-37169602013-07-21 Proteomic analysis of human spermatozoa proteins with oxidative stress Sharma, Rakesh Agarwal, Ashok Mohanty, Gayatri Hamada, Alaa J Gopalan, Banu Willard, Belinda Yadav, Satya du Plessis, Stefan Reprod Biol Endocrinol Research BACKGROUND: Oxidative stress plays a key role in the etiology of male infertility. Significant alterations in the sperm proteome are associated with poor semen quality. The aim of the present study was to examine if elevated levels of reactive oxygen species cause an alteration in the proteomic profile of spermatozoa. METHODS: This prospective study consisted of 52 subjects: 32 infertile men and 20 normal donors. Seminal ejaculates were classified as ROS+ or ROS- and evaluated for their proteomic profile. Samples were pooled and subjected to LC-MS/MS analysis through in-solution digestion of proteins for peptide characterization. The expression profile of proteins present in human spermatozoa was examined using proteomic and bioinformatic analysis to elucidate the regulatory pathways of oxidative stress. RESULTS: Of the 74 proteins identified, 10 proteins with a 2-fold difference were overexpressed and 5 were underexpressed in the ROS+ group; energy metabolism and regulation, carbohydrate metabolic processes such as gluconeogenesis and glycolysis, protein modifications and oxidative stress regulation were some of the metabolic processes affected in ROS+ group. CONCLUSIONS: We have identified proteins involved in a variety of functions associated with response and management of oxidative stress. In the present study we focused on proteins that showed a high degree of differential expression and thus, have a greater impact on the fertilizing potential of the spermatozoa. While proteomic analyses identified the potential biomarkers, further studies through Western Blot are necessary to validate the biomarker status of the proteins in pathological conditions. BioMed Central 2013-05-20 /pmc/articles/PMC3716960/ /pubmed/23688036 http://dx.doi.org/10.1186/1477-7827-11-48 Text en Copyright © 2013 Sharma et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Sharma, Rakesh Agarwal, Ashok Mohanty, Gayatri Hamada, Alaa J Gopalan, Banu Willard, Belinda Yadav, Satya du Plessis, Stefan Proteomic analysis of human spermatozoa proteins with oxidative stress |
title | Proteomic analysis of human spermatozoa proteins with oxidative stress |
title_full | Proteomic analysis of human spermatozoa proteins with oxidative stress |
title_fullStr | Proteomic analysis of human spermatozoa proteins with oxidative stress |
title_full_unstemmed | Proteomic analysis of human spermatozoa proteins with oxidative stress |
title_short | Proteomic analysis of human spermatozoa proteins with oxidative stress |
title_sort | proteomic analysis of human spermatozoa proteins with oxidative stress |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3716960/ https://www.ncbi.nlm.nih.gov/pubmed/23688036 http://dx.doi.org/10.1186/1477-7827-11-48 |
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