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Altered proteomics profile in the amnion of patients with oligohydramnios

In pregnancy, idiopathic oligohydramnios is an obstetrical complication that compromises maternal health with poor perinatal outcome. Effective therapeutic treatment of this condition has been hampered by the unknown etiology and lack of understanding of cellular and molecular mechanisms that underl...

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Autores principales: Cheung, Cecilia Y., Brace, Robert A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7048322/
https://www.ncbi.nlm.nih.gov/pubmed/32109340
http://dx.doi.org/10.14814/phy2.14381
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author Cheung, Cecilia Y.
Brace, Robert A.
author_facet Cheung, Cecilia Y.
Brace, Robert A.
author_sort Cheung, Cecilia Y.
collection PubMed
description In pregnancy, idiopathic oligohydramnios is an obstetrical complication that compromises maternal health with poor perinatal outcome. Effective therapeutic treatment of this condition has been hampered by the unknown etiology and lack of understanding of cellular and molecular mechanisms that underlie idiopathic oligohydramnios. Amniotic fluid volume (AFV) is determined by intramembranous (IM) transport of amniotic fluid across the amnion and this pathway is regulated to maintain AFV within the normal range. To gain understanding of the causes of idiopathic oligohydramnios, we performed proteomics analysis of the human amnion to investigate the changes in protein expression profiles of cellular transport pathways and regulators in patients with oligohydramnios. Placental amnions from five patients with normal pregnancies and five patients with oligohydramnios were subjected to proteomics experiments followed by bioinformatics analysis. Using Ingenuity Pathway Analysis (IPA) software, five categories of biological functions and multiple canonical pathways within each category were revealed. The top differentially expressed proteins that participate in mediating these pathways were identified. The functional pathways activated include: (a) cellular assembly and organization, (b) cell signaling and energy metabolism, and (c) immunological, infectious, and inflammatory functions. Furthermore, the analysis identified the category of pathways that facilitate molecular endocytosis and vesicular uptake. Under oligohydramniotic conditions, the mediators of clathrin vesicle‐mediated uptake and transport as well as intracellular trafficking mediators were up‐regulated. These findings suggest that idiopathic oligohydramnios may be associated with alternations in cellular organization and immunological functions as well as increases in activity of vesicular transport pathways across the amnion.
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spelling pubmed-70483222020-03-05 Altered proteomics profile in the amnion of patients with oligohydramnios Cheung, Cecilia Y. Brace, Robert A. Physiol Rep Original Research In pregnancy, idiopathic oligohydramnios is an obstetrical complication that compromises maternal health with poor perinatal outcome. Effective therapeutic treatment of this condition has been hampered by the unknown etiology and lack of understanding of cellular and molecular mechanisms that underlie idiopathic oligohydramnios. Amniotic fluid volume (AFV) is determined by intramembranous (IM) transport of amniotic fluid across the amnion and this pathway is regulated to maintain AFV within the normal range. To gain understanding of the causes of idiopathic oligohydramnios, we performed proteomics analysis of the human amnion to investigate the changes in protein expression profiles of cellular transport pathways and regulators in patients with oligohydramnios. Placental amnions from five patients with normal pregnancies and five patients with oligohydramnios were subjected to proteomics experiments followed by bioinformatics analysis. Using Ingenuity Pathway Analysis (IPA) software, five categories of biological functions and multiple canonical pathways within each category were revealed. The top differentially expressed proteins that participate in mediating these pathways were identified. The functional pathways activated include: (a) cellular assembly and organization, (b) cell signaling and energy metabolism, and (c) immunological, infectious, and inflammatory functions. Furthermore, the analysis identified the category of pathways that facilitate molecular endocytosis and vesicular uptake. Under oligohydramniotic conditions, the mediators of clathrin vesicle‐mediated uptake and transport as well as intracellular trafficking mediators were up‐regulated. These findings suggest that idiopathic oligohydramnios may be associated with alternations in cellular organization and immunological functions as well as increases in activity of vesicular transport pathways across the amnion. John Wiley and Sons Inc. 2020-02-28 /pmc/articles/PMC7048322/ /pubmed/32109340 http://dx.doi.org/10.14814/phy2.14381 Text en © 2020 The Authors. Physiological Reports published by Wiley Periodicals, Inc. on behalf of The Physiological Society and the American Physiological Society. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Research
Cheung, Cecilia Y.
Brace, Robert A.
Altered proteomics profile in the amnion of patients with oligohydramnios
title Altered proteomics profile in the amnion of patients with oligohydramnios
title_full Altered proteomics profile in the amnion of patients with oligohydramnios
title_fullStr Altered proteomics profile in the amnion of patients with oligohydramnios
title_full_unstemmed Altered proteomics profile in the amnion of patients with oligohydramnios
title_short Altered proteomics profile in the amnion of patients with oligohydramnios
title_sort altered proteomics profile in the amnion of patients with oligohydramnios
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7048322/
https://www.ncbi.nlm.nih.gov/pubmed/32109340
http://dx.doi.org/10.14814/phy2.14381
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