PRM-based quantitative proteomics analysis of altered HSP abundance in villi and decidua of patients with early missed abortion.

IF 2.1 3区生物学 Q3 BIOCHEMICAL RESEARCH METHODS Proteome Science Pub Date : 2023-08-16 DOI:10.1186/s12953-023-00213-w

Xiao-Fang Chen, Xiao-Qing Chen, Hai-Lian Luo, Li-Na Xia, Shu-Hui Huang, Qi Chen

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Abstract

Objective: In this study, we aimed to identify differentially expressed heat shock protein (HSP) profiles in the villi and decidua from patients with early missed abortion (EMA).

Methods: By using high-throughput and high-precision parallel reaction monitoring (PRM)-based targeted proteomics techniques, this study examined the abundance of HSPs in the villi and decidua of 10 patients with EMA and 10 controls. Moreover, the abundance of 3 HSPs in the villi of another 22 patients with EMA and 22 controls was verified with Western blotting and immunohistochemistry (IHC).

Results: There were potential differences in the abundance of 16 HSPs and 42 polypeptides in human villi and decidua compared with those of the control group. Among them, HSP90AB1, HSPD1 and HSPA13 were downregulated in abundance in villi of patients with EMA, with a statistically significant difference, which was consistent with the verification results of Western blots and IHC.

Conclusion: Using a PRM-based targeted proteomics technique, this study is the first to screen and quantitatively analyze the expression profile of HSPs in the villi and decidua of patients with EMA. The significant downregulation of HSP90AB1, HSPD1 and HSPA13 was found to have a potentially intimate association with the occurrence of EMA. The findings in our study may provide novel potential research targets related to HSPs for the pathogenesis, prevention and treatment of EMA.

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基于prm的早期漏产患者绒毛和蜕膜HSP丰度变化定量蛋白质组学分析。

目的:在本研究中，我们旨在鉴定早期漏产(EMA)患者绒毛和蜕膜中差异表达的热休克蛋白(HSP)谱。方法:采用基于高通量、高精度平行反应监测(PRM)的靶向蛋白质组学技术，检测了10例EMA患者和10例对照组的绒毛和蜕膜中热休克蛋白的丰度。此外，用Western blotting和免疫组化(IHC)验证了另外22例EMA患者和22例对照者绒毛中3种HSPs的丰度。结果:人绒毛和蜕膜中16种热休克蛋白和42种多肽的丰度与对照组相比存在潜在差异。其中，HSP90AB1、HSPD1、HSPA13在EMA患者绒毛中大量下调，差异有统计学意义，与Western blots和免疫组化验证结果一致。结论:利用基于prm的靶向蛋白质组学技术，本研究首次筛选并定量分析了EMA患者绒毛和蜕膜中热休克蛋白的表达谱。发现HSP90AB1、HSPD1和HSPA13的显著下调与EMA的发生有潜在的密切关系。本研究结果可能为EMA的发病机制、预防和治疗提供与热休克蛋白相关的新的潜在研究靶点。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Proteome Science 生物-生化研究方法

CiteScore

2.90

自引率

0.00%

发文量

审稿时长

4.5 months

期刊介绍： Proteome Science is an open access journal publishing research in the area of systems studies. Proteome Science considers manuscripts based on all aspects of functional and structural proteomics, genomics, metabolomics, systems analysis and metabiome analysis. It encourages the submissions of studies that use large-scale or systems analysis of biomolecules in a cellular, organismal and/or environmental context. Studies that describe novel biological or clinical insights as well as methods-focused studies that describe novel methods for the large-scale study of any and all biomolecules in cells and tissues, such as mass spectrometry, protein and nucleic acid microarrays, genomics, next-generation sequencing and computational algorithms and methods are all within the scope of Proteome Science, as are electron topography, structural methods, proteogenomics, chemical proteomics, stem cell proteomics, organelle proteomics, plant and microbial proteomics. In spite of its name, Proteome Science considers all aspects of large-scale and systems studies because ultimately any mechanism that results in genomic and metabolomic changes will affect or be affected by the proteome. To reflect this intrinsic relationship of biological systems, Proteome Science will consider all such articles.