Cargando…

Proteomic Analysis of Chicken Skeletal Muscle during Embryonic Development

Embryonic growth and development of skeletal muscle is a major determinant of muscle mass, and has a significant effect on meat production in chicken. To assess the protein expression profiles during embryonic skeletal muscle development, we performed a proteomics analysis using isobaric tags for re...

Descripción completa

Detalles Bibliográficos
Autores principales: Ouyang, Hongjia, Wang, Zhijun, Chen, Xiaolan, Yu, Jiao, Li, Zhenhui, Nie, Qinghua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5420592/
https://www.ncbi.nlm.nih.gov/pubmed/28533755
http://dx.doi.org/10.3389/fphys.2017.00281
_version_ 1783234419342966784
author Ouyang, Hongjia
Wang, Zhijun
Chen, Xiaolan
Yu, Jiao
Li, Zhenhui
Nie, Qinghua
author_facet Ouyang, Hongjia
Wang, Zhijun
Chen, Xiaolan
Yu, Jiao
Li, Zhenhui
Nie, Qinghua
author_sort Ouyang, Hongjia
collection PubMed
description Embryonic growth and development of skeletal muscle is a major determinant of muscle mass, and has a significant effect on meat production in chicken. To assess the protein expression profiles during embryonic skeletal muscle development, we performed a proteomics analysis using isobaric tags for relative and absolute quantification (iTRAQ) in leg muscle tissues of female Xinghua chicken at embryonic age (E) 11, E16, and 1-day post hatch (D1). We identified 3,240 proteins in chicken embryonic muscle and 491 of them were differentially expressed (fold change ≥ 1.5 or ≤ 0.666 and p < 0.05). There were 19 up- and 32 down-regulated proteins in E11 vs. E16 group, 238 up- and 227 down-regulated proteins in E11 vs. D1 group, and 13 up- and 5 down-regulated proteins in E16 vs. D1 group. Protein interaction network analyses indicated that these differentially expressed proteins were mainly involved in the pathway of protein synthesis, muscle contraction, and oxidative phosphorylation. Integrative analysis of proteome and our previous transcriptome data found 189 differentially expressed proteins that correlated with their mRNA level. The interactions between these proteins were also involved in muscle contraction and oxidative phosphorylation pathways. The lncRNA-protein interaction network found four proteins DMD, MYL3, TNNI2, and TNNT3 that are all involved in muscle contraction and may be lncRNA regulated. These results provide several candidate genes for further investigation into the molecular mechanisms of chicken embryonic muscle development, and enable us to better understanding their regulation networks and biochemical pathways.
format Online
Article
Text
id pubmed-5420592
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher Frontiers Media S.A.
record_format MEDLINE/PubMed
spelling pubmed-54205922017-05-22 Proteomic Analysis of Chicken Skeletal Muscle during Embryonic Development Ouyang, Hongjia Wang, Zhijun Chen, Xiaolan Yu, Jiao Li, Zhenhui Nie, Qinghua Front Physiol Physiology Embryonic growth and development of skeletal muscle is a major determinant of muscle mass, and has a significant effect on meat production in chicken. To assess the protein expression profiles during embryonic skeletal muscle development, we performed a proteomics analysis using isobaric tags for relative and absolute quantification (iTRAQ) in leg muscle tissues of female Xinghua chicken at embryonic age (E) 11, E16, and 1-day post hatch (D1). We identified 3,240 proteins in chicken embryonic muscle and 491 of them were differentially expressed (fold change ≥ 1.5 or ≤ 0.666 and p < 0.05). There were 19 up- and 32 down-regulated proteins in E11 vs. E16 group, 238 up- and 227 down-regulated proteins in E11 vs. D1 group, and 13 up- and 5 down-regulated proteins in E16 vs. D1 group. Protein interaction network analyses indicated that these differentially expressed proteins were mainly involved in the pathway of protein synthesis, muscle contraction, and oxidative phosphorylation. Integrative analysis of proteome and our previous transcriptome data found 189 differentially expressed proteins that correlated with their mRNA level. The interactions between these proteins were also involved in muscle contraction and oxidative phosphorylation pathways. The lncRNA-protein interaction network found four proteins DMD, MYL3, TNNI2, and TNNT3 that are all involved in muscle contraction and may be lncRNA regulated. These results provide several candidate genes for further investigation into the molecular mechanisms of chicken embryonic muscle development, and enable us to better understanding their regulation networks and biochemical pathways. Frontiers Media S.A. 2017-05-08 /pmc/articles/PMC5420592/ /pubmed/28533755 http://dx.doi.org/10.3389/fphys.2017.00281 Text en Copyright © 2017 Ouyang, Wang, Chen, Yu, Li and Nie. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Physiology
Ouyang, Hongjia
Wang, Zhijun
Chen, Xiaolan
Yu, Jiao
Li, Zhenhui
Nie, Qinghua
Proteomic Analysis of Chicken Skeletal Muscle during Embryonic Development
title Proteomic Analysis of Chicken Skeletal Muscle during Embryonic Development
title_full Proteomic Analysis of Chicken Skeletal Muscle during Embryonic Development
title_fullStr Proteomic Analysis of Chicken Skeletal Muscle during Embryonic Development
title_full_unstemmed Proteomic Analysis of Chicken Skeletal Muscle during Embryonic Development
title_short Proteomic Analysis of Chicken Skeletal Muscle during Embryonic Development
title_sort proteomic analysis of chicken skeletal muscle during embryonic development
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5420592/
https://www.ncbi.nlm.nih.gov/pubmed/28533755
http://dx.doi.org/10.3389/fphys.2017.00281
work_keys_str_mv AT ouyanghongjia proteomicanalysisofchickenskeletalmuscleduringembryonicdevelopment
AT wangzhijun proteomicanalysisofchickenskeletalmuscleduringembryonicdevelopment
AT chenxiaolan proteomicanalysisofchickenskeletalmuscleduringembryonicdevelopment
AT yujiao proteomicanalysisofchickenskeletalmuscleduringembryonicdevelopment
AT lizhenhui proteomicanalysisofchickenskeletalmuscleduringembryonicdevelopment
AT nieqinghua proteomicanalysisofchickenskeletalmuscleduringembryonicdevelopment