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iTRAQ-based proteomic analysis reveals key proteins affecting cardiac function in broilers that died of sudden death syndrome

Sudden death syndrome (SDS), which is a cardiac-related condition commonly observed in chickens selected for rapid growth, causes significant economic losses to the global poultry industry. Its pathogenesis in broilers is poorly understood, and little is known about the proteome of the heart tissue...

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Autores principales: Ning, Hongmei, Cui, Yunli, Song, Xiaochao, Chen, Lingli, Yin, Zhihong, Hua, Liushuai, Ren, Fei, Suo, Yu, Wang, Xinrui, Zhang, Hongli, Hu, Dongfang, Ge, Yaming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8913949/
https://www.ncbi.nlm.nih.gov/pubmed/31509194
http://dx.doi.org/10.3382/ps/pez532
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author Ning, Hongmei
Cui, Yunli
Song, Xiaochao
Chen, Lingli
Yin, Zhihong
Hua, Liushuai
Ren, Fei
Suo, Yu
Wang, Xinrui
Zhang, Hongli
Hu, Dongfang
Ge, Yaming
author_facet Ning, Hongmei
Cui, Yunli
Song, Xiaochao
Chen, Lingli
Yin, Zhihong
Hua, Liushuai
Ren, Fei
Suo, Yu
Wang, Xinrui
Zhang, Hongli
Hu, Dongfang
Ge, Yaming
author_sort Ning, Hongmei
collection PubMed
description Sudden death syndrome (SDS), which is a cardiac-related condition commonly observed in chickens selected for rapid growth, causes significant economic losses to the global poultry industry. Its pathogenesis in broilers is poorly understood, and little is known about the proteome of the heart tissue of SDS broilers. A quantitative proteomic approach using isobaric tags for relative and absolute quantification labeling of peptides was used to characterize the protein expression profiles in the left ventricle of SDS broilers. These proteins were further analyzed by bioinformatics, and two proteins were validated by western blot analysis. We identified 186 differentially expressed proteins (DEPs), of which 72 were upregulated, and 114 were downregulated in the SDS group. Functional annotation suggested that 7 DEPs were related to cardiac muscle contraction, and another 7 DEPs were related to cardiac energy metabolism. Protein interaction network predictions indicated that differences in cardiac muscle contraction between SDS and healthy groups were regulated by troponin T, tropomyosin alpha-1 chain, fast myosin heavy chain HCIII, myosin-1B, coronin, and myoglobin, whereas differences in cardiac energy metabolism and biosynthesis of amino acids were regulated by gamma-enolase, phosphoglycerate mutase, NADH-ubiquinone oxidoreductase chain 2, serine/threonine-protein kinase, myoglobin, and alpha-amylase. Our expression profiles provide useful information and new insights into key proteins to elucidate SDS for further studies.
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spelling pubmed-89139492022-03-12 iTRAQ-based proteomic analysis reveals key proteins affecting cardiac function in broilers that died of sudden death syndrome Ning, Hongmei Cui, Yunli Song, Xiaochao Chen, Lingli Yin, Zhihong Hua, Liushuai Ren, Fei Suo, Yu Wang, Xinrui Zhang, Hongli Hu, Dongfang Ge, Yaming Poult Sci Immunology, Health and Disease Sudden death syndrome (SDS), which is a cardiac-related condition commonly observed in chickens selected for rapid growth, causes significant economic losses to the global poultry industry. Its pathogenesis in broilers is poorly understood, and little is known about the proteome of the heart tissue of SDS broilers. A quantitative proteomic approach using isobaric tags for relative and absolute quantification labeling of peptides was used to characterize the protein expression profiles in the left ventricle of SDS broilers. These proteins were further analyzed by bioinformatics, and two proteins were validated by western blot analysis. We identified 186 differentially expressed proteins (DEPs), of which 72 were upregulated, and 114 were downregulated in the SDS group. Functional annotation suggested that 7 DEPs were related to cardiac muscle contraction, and another 7 DEPs were related to cardiac energy metabolism. Protein interaction network predictions indicated that differences in cardiac muscle contraction between SDS and healthy groups were regulated by troponin T, tropomyosin alpha-1 chain, fast myosin heavy chain HCIII, myosin-1B, coronin, and myoglobin, whereas differences in cardiac energy metabolism and biosynthesis of amino acids were regulated by gamma-enolase, phosphoglycerate mutase, NADH-ubiquinone oxidoreductase chain 2, serine/threonine-protein kinase, myoglobin, and alpha-amylase. Our expression profiles provide useful information and new insights into key proteins to elucidate SDS for further studies. Elsevier 2019-12-17 /pmc/articles/PMC8913949/ /pubmed/31509194 http://dx.doi.org/10.3382/ps/pez532 Text en © 2019 Poultry Science Association Inc. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Immunology, Health and Disease
Ning, Hongmei
Cui, Yunli
Song, Xiaochao
Chen, Lingli
Yin, Zhihong
Hua, Liushuai
Ren, Fei
Suo, Yu
Wang, Xinrui
Zhang, Hongli
Hu, Dongfang
Ge, Yaming
iTRAQ-based proteomic analysis reveals key proteins affecting cardiac function in broilers that died of sudden death syndrome
title iTRAQ-based proteomic analysis reveals key proteins affecting cardiac function in broilers that died of sudden death syndrome
title_full iTRAQ-based proteomic analysis reveals key proteins affecting cardiac function in broilers that died of sudden death syndrome
title_fullStr iTRAQ-based proteomic analysis reveals key proteins affecting cardiac function in broilers that died of sudden death syndrome
title_full_unstemmed iTRAQ-based proteomic analysis reveals key proteins affecting cardiac function in broilers that died of sudden death syndrome
title_short iTRAQ-based proteomic analysis reveals key proteins affecting cardiac function in broilers that died of sudden death syndrome
title_sort itraq-based proteomic analysis reveals key proteins affecting cardiac function in broilers that died of sudden death syndrome
topic Immunology, Health and Disease
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8913949/
https://www.ncbi.nlm.nih.gov/pubmed/31509194
http://dx.doi.org/10.3382/ps/pez532
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