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Phosphorylated proteomics analysis of human coronary artery endothelial cells stimulated by Kawasaki disease patients serum

BACKGROUND: Kawasaki disease (KD) is an acute febrile childhood systemic vasculitis that disturbs coronary arteries. The pathogenesis remains unknown. The study of phosphorylated proteins helps to elucidate the relevant pathophysiological mechanisms of cardiovascular disease. However, few researches...

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Autores principales: Li, Shui-Ming, Liu, Wan-Ting, Yang, Fang, Yi, Qi-Jian, Zhang, Shuai, Jia, Hong-Ling
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6337789/
https://www.ncbi.nlm.nih.gov/pubmed/30654760
http://dx.doi.org/10.1186/s12872-018-0982-2
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author Li, Shui-Ming
Liu, Wan-Ting
Yang, Fang
Yi, Qi-Jian
Zhang, Shuai
Jia, Hong-Ling
author_facet Li, Shui-Ming
Liu, Wan-Ting
Yang, Fang
Yi, Qi-Jian
Zhang, Shuai
Jia, Hong-Ling
author_sort Li, Shui-Ming
collection PubMed
description BACKGROUND: Kawasaki disease (KD) is an acute febrile childhood systemic vasculitis that disturbs coronary arteries. The pathogenesis remains unknown. The study of phosphorylated proteins helps to elucidate the relevant pathophysiological mechanisms of cardiovascular disease. However, few researches explored phosphorylated proteins in KD patients. METHODS: We compared phosphoprotein profiles of HCAECs stimulated by the serum of KD patients and normal children using iTRAQ technology, TiO(2) enrichment phosphorylated peptide and MS analysis. Then we conducted the functional analysis by ClueGO and the biological interaction networking analysis by ReactomeFIViz. Western blotting was performed to identify the hub proteins. RESULTS: Our results revealed that phosphorylation of 148 proteins showed different intensities between the two HCAECs groups, which are enriched in MAPK, VEGFR, EGFR, Angiopoietin receptor, mTOR, FAK signaling pathway and so on. Through the Network Analyzer analysis, the hub proteins are CDKN1A, MAPK1 and POLR2A, which were experimentally validated. CONCLUSION: In summary, we provided evidence addressing the valuable phosphorylation signaling that could be useful resource to understand the molecular mechanism and the potential targets for novel therapy of KD. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12872-018-0982-2) contains supplementary material, which is available to authorized users.
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spelling pubmed-63377892019-01-23 Phosphorylated proteomics analysis of human coronary artery endothelial cells stimulated by Kawasaki disease patients serum Li, Shui-Ming Liu, Wan-Ting Yang, Fang Yi, Qi-Jian Zhang, Shuai Jia, Hong-Ling BMC Cardiovasc Disord Research Article BACKGROUND: Kawasaki disease (KD) is an acute febrile childhood systemic vasculitis that disturbs coronary arteries. The pathogenesis remains unknown. The study of phosphorylated proteins helps to elucidate the relevant pathophysiological mechanisms of cardiovascular disease. However, few researches explored phosphorylated proteins in KD patients. METHODS: We compared phosphoprotein profiles of HCAECs stimulated by the serum of KD patients and normal children using iTRAQ technology, TiO(2) enrichment phosphorylated peptide and MS analysis. Then we conducted the functional analysis by ClueGO and the biological interaction networking analysis by ReactomeFIViz. Western blotting was performed to identify the hub proteins. RESULTS: Our results revealed that phosphorylation of 148 proteins showed different intensities between the two HCAECs groups, which are enriched in MAPK, VEGFR, EGFR, Angiopoietin receptor, mTOR, FAK signaling pathway and so on. Through the Network Analyzer analysis, the hub proteins are CDKN1A, MAPK1 and POLR2A, which were experimentally validated. CONCLUSION: In summary, we provided evidence addressing the valuable phosphorylation signaling that could be useful resource to understand the molecular mechanism and the potential targets for novel therapy of KD. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12872-018-0982-2) contains supplementary material, which is available to authorized users. BioMed Central 2019-01-17 /pmc/articles/PMC6337789/ /pubmed/30654760 http://dx.doi.org/10.1186/s12872-018-0982-2 Text en © The Author(s). 2019 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Li, Shui-Ming
Liu, Wan-Ting
Yang, Fang
Yi, Qi-Jian
Zhang, Shuai
Jia, Hong-Ling
Phosphorylated proteomics analysis of human coronary artery endothelial cells stimulated by Kawasaki disease patients serum
title Phosphorylated proteomics analysis of human coronary artery endothelial cells stimulated by Kawasaki disease patients serum
title_full Phosphorylated proteomics analysis of human coronary artery endothelial cells stimulated by Kawasaki disease patients serum
title_fullStr Phosphorylated proteomics analysis of human coronary artery endothelial cells stimulated by Kawasaki disease patients serum
title_full_unstemmed Phosphorylated proteomics analysis of human coronary artery endothelial cells stimulated by Kawasaki disease patients serum
title_short Phosphorylated proteomics analysis of human coronary artery endothelial cells stimulated by Kawasaki disease patients serum
title_sort phosphorylated proteomics analysis of human coronary artery endothelial cells stimulated by kawasaki disease patients serum
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6337789/
https://www.ncbi.nlm.nih.gov/pubmed/30654760
http://dx.doi.org/10.1186/s12872-018-0982-2
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