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iTRAQ-based proteomic analysis reveals key proteins affecting muscle growth and lipid deposition in pigs

Growth rate and meat quality, two economically important traits in pigs, are controlled by multiple genes and biological pathways. In the present study, we performed a proteomic analysis of longissimus dorsi muscle from six-month-old pigs from two Chinese native mini-type breeds (TP and DSP) and two...

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Autores principales: Wang, Zhixiu, Shang, Peng, Li, Qinggang, Wang, Liyuan, Chamba, Yangzom, Zhang, Bo, Zhang, Hao, Wu, Changxin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5402282/
https://www.ncbi.nlm.nih.gov/pubmed/28436483
http://dx.doi.org/10.1038/srep46717
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author Wang, Zhixiu
Shang, Peng
Li, Qinggang
Wang, Liyuan
Chamba, Yangzom
Zhang, Bo
Zhang, Hao
Wu, Changxin
author_facet Wang, Zhixiu
Shang, Peng
Li, Qinggang
Wang, Liyuan
Chamba, Yangzom
Zhang, Bo
Zhang, Hao
Wu, Changxin
author_sort Wang, Zhixiu
collection PubMed
description Growth rate and meat quality, two economically important traits in pigs, are controlled by multiple genes and biological pathways. In the present study, we performed a proteomic analysis of longissimus dorsi muscle from six-month-old pigs from two Chinese native mini-type breeds (TP and DSP) and two introduced western breeds (YY and LL) using isobaric tag for relative and absolute quantification (iTRAQ). In total, 4,815 peptides corresponding to 969 proteins were detected. Comparison of expression patterns between TP-DSP and YY-LL revealed 288 differentially expressed proteins (DEPs), of which 169 were up-regulated and 119 were down-regulated. Functional annotation suggested that 28 DEPs were related to muscle growth and 15 to lipid deposition. Protein interaction network predictions indicated that differences in muscle growth and muscle fibre between TP-DSP and YY-LL groups were regulated by ALDOC, ENO3, PGK1, PGK2, TNNT1, TNNT3, TPM1, TPM2, TPM3, MYL3, MYH4, and TNNC2, whereas differences in lipid deposition ability were regulated by LPL, APOA1, APOC3, ACADM, FABP3, ACADVL, ACAA2, ACAT1, HADH, and PECI. Twelve DEPs were analysed using parallel reaction monitoring to confirm the reliability of the iTRAQ analysis. Our findings provide new insights into key proteins involved in muscle growth and lipid deposition in the pig.
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spelling pubmed-54022822017-04-26 iTRAQ-based proteomic analysis reveals key proteins affecting muscle growth and lipid deposition in pigs Wang, Zhixiu Shang, Peng Li, Qinggang Wang, Liyuan Chamba, Yangzom Zhang, Bo Zhang, Hao Wu, Changxin Sci Rep Article Growth rate and meat quality, two economically important traits in pigs, are controlled by multiple genes and biological pathways. In the present study, we performed a proteomic analysis of longissimus dorsi muscle from six-month-old pigs from two Chinese native mini-type breeds (TP and DSP) and two introduced western breeds (YY and LL) using isobaric tag for relative and absolute quantification (iTRAQ). In total, 4,815 peptides corresponding to 969 proteins were detected. Comparison of expression patterns between TP-DSP and YY-LL revealed 288 differentially expressed proteins (DEPs), of which 169 were up-regulated and 119 were down-regulated. Functional annotation suggested that 28 DEPs were related to muscle growth and 15 to lipid deposition. Protein interaction network predictions indicated that differences in muscle growth and muscle fibre between TP-DSP and YY-LL groups were regulated by ALDOC, ENO3, PGK1, PGK2, TNNT1, TNNT3, TPM1, TPM2, TPM3, MYL3, MYH4, and TNNC2, whereas differences in lipid deposition ability were regulated by LPL, APOA1, APOC3, ACADM, FABP3, ACADVL, ACAA2, ACAT1, HADH, and PECI. Twelve DEPs were analysed using parallel reaction monitoring to confirm the reliability of the iTRAQ analysis. Our findings provide new insights into key proteins involved in muscle growth and lipid deposition in the pig. Nature Publishing Group 2017-04-24 /pmc/articles/PMC5402282/ /pubmed/28436483 http://dx.doi.org/10.1038/srep46717 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Wang, Zhixiu
Shang, Peng
Li, Qinggang
Wang, Liyuan
Chamba, Yangzom
Zhang, Bo
Zhang, Hao
Wu, Changxin
iTRAQ-based proteomic analysis reveals key proteins affecting muscle growth and lipid deposition in pigs
title iTRAQ-based proteomic analysis reveals key proteins affecting muscle growth and lipid deposition in pigs
title_full iTRAQ-based proteomic analysis reveals key proteins affecting muscle growth and lipid deposition in pigs
title_fullStr iTRAQ-based proteomic analysis reveals key proteins affecting muscle growth and lipid deposition in pigs
title_full_unstemmed iTRAQ-based proteomic analysis reveals key proteins affecting muscle growth and lipid deposition in pigs
title_short iTRAQ-based proteomic analysis reveals key proteins affecting muscle growth and lipid deposition in pigs
title_sort itraq-based proteomic analysis reveals key proteins affecting muscle growth and lipid deposition in pigs
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5402282/
https://www.ncbi.nlm.nih.gov/pubmed/28436483
http://dx.doi.org/10.1038/srep46717
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