4.7 Article

Identification of proteins associated with development of psoriatic arthritis in peripheral blood mononuclear cells: a quantitative iTRAQ-based proteomics study

Journal

JOURNAL OF TRANSLATIONAL MEDICINE
Volume 19, Issue 1, Pages -

Publisher

BMC
DOI: 10.1186/s12967-021-03006-x

Keywords

Psoriatic arthritis; Proteomics; iTRAQ; Peripheral blood; Biomarkers

Funding

  1. National Natural Science Foundation of China [81773322, 81673054]
  2. KeyProject in Basic Research Advocated by Shanghai Science and Technology Commission [13JC1402300]
  3. Clinical Research Plan of SHDC [SHDC2020CR6022, SHDC2020CR1014B]

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By analyzing the proteome profile of PBMCs from patients with PsA, PsO, and healthy controls, this study identified 14 potential biomarkers for PsA diagnosis. Additionally, the expression of SIRT2 was significantly higher in PsA patients compared to PsO and healthy controls, and was negatively correlated with the phosphorylation of p38MAPK.
BackgroundBiomarkers for distinguishing psoriatic arthritis (PsA) from psoriasis without arthritis (PsO) are still lacking.MethodsWe applied isobaric tags for relative and absolute quantification (iTRAQ) and LC-MS/MS to analyze the proteome profile of peripheral blood mononuclear cells (PBMCs) collected from patients with PsO, patients with PsA, and healthy controls. Bioinformatics analysis and western blotting were performed to identify and validate differentially expressed proteins.ResultsWe identified 389, 199, 291, and 60 significantly differentially expressed proteins (adj.p<0.05) in the comparison of all psoriatic patients versus healthy controls, PsO group versus healthy controls, PsA group versus healthy controls, and PsA group versus PsO group, respectively. Among these proteins, 14 proteins may represent promising biomarkers for PsA: SIRT2, NAA50, ARF6, ADPRHL2, SF3B6, SH3KBP1, UBA3, SCP2, RPS5, NUDT5, NCBP1, SYNE1, NDUFB7, HTATSF1. Furthermore, western blotting confirmed that SIRT2 expression was significantly higher in PBMCs from PsA patients than PsO and healthy controls, and was negatively correlated with the phosphorylation of p38 mitogen-activated protein kinase (p-p38MAPK; p=0.006, r=- 0.582).ConclusionsThis pilot study provided a broad characterization of the proteome of PBMCs in PsA as compared to PsO and healthy controls, which may help to provide prospective strategies for PsA diagnosis.

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