Succinylation profiles of brain injury after intracerebral hemorrhage

Protein posttranslational modifications (PTMs) regulate the biological processes of human diseases by genetic code expansion and cellular pathophysiology regulation; however, system-wide changes in PTM levels in the intracerebral hemorrhage (ICH) brain remain poorly understood. Succinylation refers...

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Autores principales:	Yuan-Hong Deng, Xin-Xiao Zhang, Chuan-Yuan Tao, Yan-Jing Liang, Jing Yuan, Su-Hao Yang, Yuan-Rui Yang, Xiao-Yi Xiong
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ed86a7f43d7c43b48d0586cbb5aab16c
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spelling	oai:doaj.org-article:ed86a7f43d7c43b48d0586cbb5aab16c2021-11-25T06:10:56ZSuccinylation profiles of brain injury after intracerebral hemorrhage1932-6203https://doaj.org/article/ed86a7f43d7c43b48d0586cbb5aab16c2021-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8592435/?tool=EBIhttps://doaj.org/toc/1932-6203Protein posttranslational modifications (PTMs) regulate the biological processes of human diseases by genetic code expansion and cellular pathophysiology regulation; however, system-wide changes in PTM levels in the intracerebral hemorrhage (ICH) brain remain poorly understood. Succinylation refers to a major PTM during the regulation of multiple biological processes. In this study, according to the methods of quantitative succinyllysine proteomics based on high-resolution mass spectrometry, we investigated ICH-associated brain protein succinyllysine modifications and obtained 3,680 succinylated sites and quantified around 3,530 sites. Among them, 25 succinyllysine sites on 23 proteins were upregulated (hypersuccinylated), whereas 13 succinyllysine sites on 12 proteins were downregulated (hyposuccinylated) following ICH. The cell component enrichment analysis of these succinylproteins with significant changes showed that 58.3% of the hyposuccinylated proteins were observed in the mitochondria, while the hyper-succinylproteins located in mitochondria decreased in the percentage to about 35% in ICH brains with a concomitant increase in the percentage of cytoplasm to 30.4%. Further bioinformatic analysis showed that the succinylproteins were mostly mitochondria and synapse-related subcellular located and involved in many pathophysiological processes, like metabolism, synapse working, and ferroptosis. Moreover, the integrative analysis of our succinylproteomics data and previously published transcriptome data showed that the mRNAs matched by most differentially succinylated proteins were especially highly expressed in neurons, endothelial cells, and astrocytes. Our study uncovers some succinylation-affected processes and pathways in response to ICH brains and gives us novel insights into understanding pathophysiological processes of brain injury caused by ICH.Yuan-Hong DengXin-Xiao ZhangChuan-Yuan TaoYan-Jing LiangJing YuanSu-Hao YangYuan-Rui YangXiao-Yi XiongPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yuan-Hong Deng Xin-Xiao Zhang Chuan-Yuan Tao Yan-Jing Liang Jing Yuan Su-Hao Yang Yuan-Rui Yang Xiao-Yi Xiong Succinylation profiles of brain injury after intracerebral hemorrhage
description	Protein posttranslational modifications (PTMs) regulate the biological processes of human diseases by genetic code expansion and cellular pathophysiology regulation; however, system-wide changes in PTM levels in the intracerebral hemorrhage (ICH) brain remain poorly understood. Succinylation refers to a major PTM during the regulation of multiple biological processes. In this study, according to the methods of quantitative succinyllysine proteomics based on high-resolution mass spectrometry, we investigated ICH-associated brain protein succinyllysine modifications and obtained 3,680 succinylated sites and quantified around 3,530 sites. Among them, 25 succinyllysine sites on 23 proteins were upregulated (hypersuccinylated), whereas 13 succinyllysine sites on 12 proteins were downregulated (hyposuccinylated) following ICH. The cell component enrichment analysis of these succinylproteins with significant changes showed that 58.3% of the hyposuccinylated proteins were observed in the mitochondria, while the hyper-succinylproteins located in mitochondria decreased in the percentage to about 35% in ICH brains with a concomitant increase in the percentage of cytoplasm to 30.4%. Further bioinformatic analysis showed that the succinylproteins were mostly mitochondria and synapse-related subcellular located and involved in many pathophysiological processes, like metabolism, synapse working, and ferroptosis. Moreover, the integrative analysis of our succinylproteomics data and previously published transcriptome data showed that the mRNAs matched by most differentially succinylated proteins were especially highly expressed in neurons, endothelial cells, and astrocytes. Our study uncovers some succinylation-affected processes and pathways in response to ICH brains and gives us novel insights into understanding pathophysiological processes of brain injury caused by ICH.
format	article
author	Yuan-Hong Deng Xin-Xiao Zhang Chuan-Yuan Tao Yan-Jing Liang Jing Yuan Su-Hao Yang Yuan-Rui Yang Xiao-Yi Xiong
author_facet	Yuan-Hong Deng Xin-Xiao Zhang Chuan-Yuan Tao Yan-Jing Liang Jing Yuan Su-Hao Yang Yuan-Rui Yang Xiao-Yi Xiong
author_sort	Yuan-Hong Deng
title	Succinylation profiles of brain injury after intracerebral hemorrhage
title_short	Succinylation profiles of brain injury after intracerebral hemorrhage
title_full	Succinylation profiles of brain injury after intracerebral hemorrhage
title_fullStr	Succinylation profiles of brain injury after intracerebral hemorrhage
title_full_unstemmed	Succinylation profiles of brain injury after intracerebral hemorrhage
title_sort	succinylation profiles of brain injury after intracerebral hemorrhage
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/ed86a7f43d7c43b48d0586cbb5aab16c
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_version_	1718414136203804672

Succinylation profiles of brain injury after intracerebral hemorrhage

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