Characterization of the Phosphoproteome in SLE Patients.

Protein phosphorylation is a complex regulatory event that is involved in the signaling networks that affect virtually every cellular process. The protein phosphorylation may be a novel source for discovering biomarkers and drug targets. However, a systematic analysis of the phosphoproteome in patie...

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Autores principales:	Xinzhou Zhang, Hualin Ma, Jianrong Huang, Yong Dai
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/1a2ebaca1aef49219815ee563e1548d7
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spelling	oai:doaj.org-article:1a2ebaca1aef49219815ee563e1548d72021-11-18T08:03:14ZCharacterization of the Phosphoproteome in SLE Patients.1932-620310.1371/journal.pone.0053129https://doaj.org/article/1a2ebaca1aef49219815ee563e1548d72012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23285258/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Protein phosphorylation is a complex regulatory event that is involved in the signaling networks that affect virtually every cellular process. The protein phosphorylation may be a novel source for discovering biomarkers and drug targets. However, a systematic analysis of the phosphoproteome in patients with SLE has not been performed. To clarify the pathogenesis of systemic lupus erythematosus (SLE), we compared phosphoprotein expression in PBMCs from SLE patients and normal subjects using proteomics analyses. Phosphopeptides were enriched using TiO₂ from PBMCs isolated from 15 SLE patients and 15 healthy subjects and then analyzed by automated LC-MS/MS analysis. Phosphorylation sites were identified and quantitated by MASCOT and MaxQuant. A total of 1035 phosphorylation sites corresponding to 618 NCBI-annotated genes were identified in SLE patients compared with normal subjects. Differentially expressed proteins, peptides and phosphorylation sites were then subjected to bioinformatics analyses. Gene ontology(GO) and pathway analyses showed that nucleic acid metabolism, cellular component organization, transport and multicellular organismal development pathways made up the largest proportions of the differentially expressed genes. Pathway analyses showed that the mitogen-activated protein kinase (MAPK) signaling pathway and actin cytoskeleton regulators made up the largest proportions of the metabolic pathways. Network analysis showed that rous sarcoma oncogene (SRC), v-rel reticuloendotheliosis viral oncogene homolog A (RELA), histone deacetylase (HDA1C) and protein kinase C, delta (PRKCD) play important roles in the stability of the network. These data suggest that aberrant protein phosphorylation may contribute to SLE pathogenesis.Xinzhou ZhangHualin MaJianrong HuangYong DaiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 12, p e53129 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Xinzhou Zhang Hualin Ma Jianrong Huang Yong Dai Characterization of the Phosphoproteome in SLE Patients.
description	Protein phosphorylation is a complex regulatory event that is involved in the signaling networks that affect virtually every cellular process. The protein phosphorylation may be a novel source for discovering biomarkers and drug targets. However, a systematic analysis of the phosphoproteome in patients with SLE has not been performed. To clarify the pathogenesis of systemic lupus erythematosus (SLE), we compared phosphoprotein expression in PBMCs from SLE patients and normal subjects using proteomics analyses. Phosphopeptides were enriched using TiO₂ from PBMCs isolated from 15 SLE patients and 15 healthy subjects and then analyzed by automated LC-MS/MS analysis. Phosphorylation sites were identified and quantitated by MASCOT and MaxQuant. A total of 1035 phosphorylation sites corresponding to 618 NCBI-annotated genes were identified in SLE patients compared with normal subjects. Differentially expressed proteins, peptides and phosphorylation sites were then subjected to bioinformatics analyses. Gene ontology(GO) and pathway analyses showed that nucleic acid metabolism, cellular component organization, transport and multicellular organismal development pathways made up the largest proportions of the differentially expressed genes. Pathway analyses showed that the mitogen-activated protein kinase (MAPK) signaling pathway and actin cytoskeleton regulators made up the largest proportions of the metabolic pathways. Network analysis showed that rous sarcoma oncogene (SRC), v-rel reticuloendotheliosis viral oncogene homolog A (RELA), histone deacetylase (HDA1C) and protein kinase C, delta (PRKCD) play important roles in the stability of the network. These data suggest that aberrant protein phosphorylation may contribute to SLE pathogenesis.
format	article
author	Xinzhou Zhang Hualin Ma Jianrong Huang Yong Dai
author_facet	Xinzhou Zhang Hualin Ma Jianrong Huang Yong Dai
author_sort	Xinzhou Zhang
title	Characterization of the Phosphoproteome in SLE Patients.
title_short	Characterization of the Phosphoproteome in SLE Patients.
title_full	Characterization of the Phosphoproteome in SLE Patients.
title_fullStr	Characterization of the Phosphoproteome in SLE Patients.
title_full_unstemmed	Characterization of the Phosphoproteome in SLE Patients.
title_sort	characterization of the phosphoproteome in sle patients.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/1a2ebaca1aef49219815ee563e1548d7
work_keys_str_mv	AT xinzhouzhang characterizationofthephosphoproteomeinslepatients AT hualinma characterizationofthephosphoproteomeinslepatients AT jianronghuang characterizationofthephosphoproteomeinslepatients AT yongdai characterizationofthephosphoproteomeinslepatients
_version_	1718422591058739200

Characterization of the Phosphoproteome in SLE Patients.

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