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A proteomic profile of the healthy human placenta

BACKGROUND: The placenta remains one of the least studied organs within the human body. Yet, placental dysfunction has been associated with various pregnancy complications leading to both maternal and fetal death and long-term health consequences. The aim of this study was to characterise the protei...

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Autores principales: Manna, Samprikta, Scheel, Julia, Noone, Aisling, McElwain, Colm J., Scaife, Caitriona, Gupta, Shailendra, English, Jane, McCarthy, Cathal, McCarthy, Fergus P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9808999/
https://www.ncbi.nlm.nih.gov/pubmed/36593452
http://dx.doi.org/10.1186/s12014-022-09388-4
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author Manna, Samprikta
Scheel, Julia
Noone, Aisling
McElwain, Colm J.
Scaife, Caitriona
Gupta, Shailendra
English, Jane
McCarthy, Cathal
McCarthy, Fergus P.
author_facet Manna, Samprikta
Scheel, Julia
Noone, Aisling
McElwain, Colm J.
Scaife, Caitriona
Gupta, Shailendra
English, Jane
McCarthy, Cathal
McCarthy, Fergus P.
author_sort Manna, Samprikta
collection PubMed
description BACKGROUND: The placenta remains one of the least studied organs within the human body. Yet, placental dysfunction has been associated with various pregnancy complications leading to both maternal and fetal death and long-term health consequences. The aim of this study was to characterise the protein networks of healthy term placental sub-anatomical regions using label free quantification mass spectrometry. METHODS: Three healthy placentae were sampled at five sample sites and each biopsy was dissected into maternal-, middle-, and fetal- sub-anatomical regions. Quadrupole-orbitrap mass spectrometer was used in data dependant analysis mode to identify 1859 unique proteins before detailed differential expression between regions. RESULTS: Protein profiling identified 1081, 1086, and 1101 proteins in maternal, middle, and fetal sub-anatomical regions respectively. Differentially expressed proteins were identified considering the effect between sample site location and sub-anatomical region on protein expression. Of these, 374 differentially expressed proteins (Two-way ANOVA adjusted p-value < 0.05, HSD Tukey adjusted p-value 0.05) were identified between sample site locations and sub-anatomical regions. The placenta specific disease map NaviCenta (https://www.sbi.uni-rostock.de/minerva/index.xhtml?id=NaviCenta) was used to focus functional analysis results to the placenta specific context. Subsequently, functional analysis with a focus on senescence, and mitochondrial function were performed. Significant differences were observed between sub-anatomical regions in protein intensity and composition. A decrease in anti-senescent proteins within the maternal sub-anatomical region, and an increase in proteins associated with a switch from ATP to fatty acid consumption as a source of energy between middle and fetal sub-anatomical regions were observed. CONCLUSION: These results suggest that normal proteomic variations exist within the anatomical structure of the placenta, thus recommending serial sectioning methodology for consistent placental research. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12014-022-09388-4.
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spelling pubmed-98089992023-01-04 A proteomic profile of the healthy human placenta Manna, Samprikta Scheel, Julia Noone, Aisling McElwain, Colm J. Scaife, Caitriona Gupta, Shailendra English, Jane McCarthy, Cathal McCarthy, Fergus P. Clin Proteomics Review BACKGROUND: The placenta remains one of the least studied organs within the human body. Yet, placental dysfunction has been associated with various pregnancy complications leading to both maternal and fetal death and long-term health consequences. The aim of this study was to characterise the protein networks of healthy term placental sub-anatomical regions using label free quantification mass spectrometry. METHODS: Three healthy placentae were sampled at five sample sites and each biopsy was dissected into maternal-, middle-, and fetal- sub-anatomical regions. Quadrupole-orbitrap mass spectrometer was used in data dependant analysis mode to identify 1859 unique proteins before detailed differential expression between regions. RESULTS: Protein profiling identified 1081, 1086, and 1101 proteins in maternal, middle, and fetal sub-anatomical regions respectively. Differentially expressed proteins were identified considering the effect between sample site location and sub-anatomical region on protein expression. Of these, 374 differentially expressed proteins (Two-way ANOVA adjusted p-value < 0.05, HSD Tukey adjusted p-value 0.05) were identified between sample site locations and sub-anatomical regions. The placenta specific disease map NaviCenta (https://www.sbi.uni-rostock.de/minerva/index.xhtml?id=NaviCenta) was used to focus functional analysis results to the placenta specific context. Subsequently, functional analysis with a focus on senescence, and mitochondrial function were performed. Significant differences were observed between sub-anatomical regions in protein intensity and composition. A decrease in anti-senescent proteins within the maternal sub-anatomical region, and an increase in proteins associated with a switch from ATP to fatty acid consumption as a source of energy between middle and fetal sub-anatomical regions were observed. CONCLUSION: These results suggest that normal proteomic variations exist within the anatomical structure of the placenta, thus recommending serial sectioning methodology for consistent placental research. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12014-022-09388-4. BioMed Central 2023-01-02 /pmc/articles/PMC9808999/ /pubmed/36593452 http://dx.doi.org/10.1186/s12014-022-09388-4 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Review
Manna, Samprikta
Scheel, Julia
Noone, Aisling
McElwain, Colm J.
Scaife, Caitriona
Gupta, Shailendra
English, Jane
McCarthy, Cathal
McCarthy, Fergus P.
A proteomic profile of the healthy human placenta
title A proteomic profile of the healthy human placenta
title_full A proteomic profile of the healthy human placenta
title_fullStr A proteomic profile of the healthy human placenta
title_full_unstemmed A proteomic profile of the healthy human placenta
title_short A proteomic profile of the healthy human placenta
title_sort proteomic profile of the healthy human placenta
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9808999/
https://www.ncbi.nlm.nih.gov/pubmed/36593452
http://dx.doi.org/10.1186/s12014-022-09388-4
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