Cargando…
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...
Autores principales: | , , , , |
---|---|
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 |
_version_ | 1783405164165595136 |
---|---|
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. |
format | Online Article Text |
id | pubmed-6427241 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | The American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT ouniemna adraftmapofthehumanovarianproteomefortissueengineeringandclinicalapplications AT vertommendidier adraftmapofthehumanovarianproteomefortissueengineeringandclinicalapplications AT chitimariacostanza adraftmapofthehumanovarianproteomefortissueengineeringandclinicalapplications AT dolmansmariemadeleine adraftmapofthehumanovarianproteomefortissueengineeringandclinicalapplications AT amorimchristiania adraftmapofthehumanovarianproteomefortissueengineeringandclinicalapplications AT ouniemna draftmapofthehumanovarianproteomefortissueengineeringandclinicalapplications AT vertommendidier draftmapofthehumanovarianproteomefortissueengineeringandclinicalapplications AT chitimariacostanza draftmapofthehumanovarianproteomefortissueengineeringandclinicalapplications AT dolmansmariemadeleine draftmapofthehumanovarianproteomefortissueengineeringandclinicalapplications AT amorimchristiania draftmapofthehumanovarianproteomefortissueengineeringandclinicalapplications |