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A Draft Map of the Human Ovarian Proteome for Tissue Engineering and Clinical Applications

Fertility preservation research in women today is increasingly taking advantage of bioengineering techniques to develop new biomimetic materials and solutions to safeguard ovarian cell function and microenvironment in vitro, and in vivo,. However, available data on the human ovary are limited and fu...

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Autores principales: Ouni, Emna, Vertommen, Didier, Chiti, Maria Costanza, Dolmans, Marie-Madeleine, Amorim, Christiani A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Biochemistry and Molecular Biology 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6427241/
https://www.ncbi.nlm.nih.gov/pubmed/29475978
http://dx.doi.org/10.1074/mcp.RA117.000469
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author Ouni, Emna
Vertommen, Didier
Chiti, Maria Costanza
Dolmans, Marie-Madeleine
Amorim, Christiani A.
author_facet Ouni, Emna
Vertommen, Didier
Chiti, Maria Costanza
Dolmans, Marie-Madeleine
Amorim, Christiani A.
author_sort Ouni, Emna
collection PubMed
description Fertility preservation research in women today is increasingly taking advantage of bioengineering techniques to develop new biomimetic materials and solutions to safeguard ovarian cell function and microenvironment in vitro, and in vivo,. However, available data on the human ovary are limited and fundamental differences between animal models and humans are hampering researchers in their quest for more extensive knowledge of human ovarian physiology and key reproductive proteins that need to be preserved. We therefore turned to multi-dimensional label-free mass spectrometry to analyze human ovarian cortex, as it is a high-throughput and conclusive technique providing information on the proteomic composition of complex tissues like the ovary. In-depth proteomic profiling through two-dimensional liquid chromatography-mass spectrometry, Western blotting, histological and immunohistochemical analyses, and data mining helped us to confidently identify 1508 proteins. Moreover, our method allowed us to chart the most complete representation so far of the ovarian matrisome, defined as the ensemble of extracellular matrix proteins and associated factors, including more than 80 proteins. In conclusion, this study will provide a better understanding of ovarian proteomics, with a detailed characterization of the ovarian follicle microenvironment, in order to enable bioengineers to create biomimetic scaffolds for transplantation and three-dimensional in vitro, culture. By publishing our proteomic data, we also hope to contribute to accelerating biomedical research into ovarian health and disease in general.
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spelling pubmed-64272412019-03-22 A Draft Map of the Human Ovarian Proteome for Tissue Engineering and Clinical Applications Ouni, Emna Vertommen, Didier Chiti, Maria Costanza Dolmans, Marie-Madeleine Amorim, Christiani A. Mol Cell Proteomics Research Fertility preservation research in women today is increasingly taking advantage of bioengineering techniques to develop new biomimetic materials and solutions to safeguard ovarian cell function and microenvironment in vitro, and in vivo,. However, available data on the human ovary are limited and fundamental differences between animal models and humans are hampering researchers in their quest for more extensive knowledge of human ovarian physiology and key reproductive proteins that need to be preserved. We therefore turned to multi-dimensional label-free mass spectrometry to analyze human ovarian cortex, as it is a high-throughput and conclusive technique providing information on the proteomic composition of complex tissues like the ovary. In-depth proteomic profiling through two-dimensional liquid chromatography-mass spectrometry, Western blotting, histological and immunohistochemical analyses, and data mining helped us to confidently identify 1508 proteins. Moreover, our method allowed us to chart the most complete representation so far of the ovarian matrisome, defined as the ensemble of extracellular matrix proteins and associated factors, including more than 80 proteins. In conclusion, this study will provide a better understanding of ovarian proteomics, with a detailed characterization of the ovarian follicle microenvironment, in order to enable bioengineers to create biomimetic scaffolds for transplantation and three-dimensional in vitro, culture. By publishing our proteomic data, we also hope to contribute to accelerating biomedical research into ovarian health and disease in general. The American Society for Biochemistry and Molecular Biology 2019-03-15 2018-02-23 /pmc/articles/PMC6427241/ /pubmed/29475978 http://dx.doi.org/10.1074/mcp.RA117.000469 Text en © 2019 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice,—Final version open access under the terms of the Creative Commons CC-BY license (http://creativecommons.org/licenses/by/4.0) .
spellingShingle Research
Ouni, Emna
Vertommen, Didier
Chiti, Maria Costanza
Dolmans, Marie-Madeleine
Amorim, Christiani A.
A Draft Map of the Human Ovarian Proteome for Tissue Engineering and Clinical Applications
title A Draft Map of the Human Ovarian Proteome for Tissue Engineering and Clinical Applications
title_full A Draft Map of the Human Ovarian Proteome for Tissue Engineering and Clinical Applications
title_fullStr A Draft Map of the Human Ovarian Proteome for Tissue Engineering and Clinical Applications
title_full_unstemmed A Draft Map of the Human Ovarian Proteome for Tissue Engineering and Clinical Applications
title_short A Draft Map of the Human Ovarian Proteome for Tissue Engineering and Clinical Applications
title_sort draft map of the human ovarian proteome for tissue engineering and clinical applications
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6427241/
https://www.ncbi.nlm.nih.gov/pubmed/29475978
http://dx.doi.org/10.1074/mcp.RA117.000469
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