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Detergent-Insoluble Proteome Analysis Revealed Aberrantly Aggregated Proteins in Human Preeclampsia Placentas
Wanling Zhang1, Xing Chen1, Ziqi Yan1
1Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University , 601 Huangpu Avenue West, Guangzhou, Guangdong 510632, China.
Insights
Preeclampsia (PE) is linked to abnormal protein aggregates in the placenta. This study identified specific differentially aggregated proteins in PE placentas, offering new insights into the disease mechanisms.
Area of Science:
- Proteomics
- Biochemistry
- Pathology
Background:
- Preeclampsia (PE) is a placenta-associated disease with unknown causes.
- PE placentas exhibit endoplasmic reticulum (ER) stress and unfolded protein response (UPR).
- Detergent-insoluble proteins (DIPs) represent protein aggregates, potentially reflecting cellular stress.
Purpose of the Study:
- To characterize placenta UPR in PE by analyzing DIPs.
- To identify and quantify differentially aggregated proteins in PE placentas using mass spectrometry.
Main Methods:
- Isolation of detergent-insoluble proteins (DIPs) from normal and PE human placenta tissues.
- Data-independent acquisition (DIA) mass spectrometry for proteomic analysis.
- Immunoblotting to validate protein quantitation (endoglin, vimentin).
Main Results:
- Identified 2066 DIPs; 110 were significantly upregulated and 108 downregulated in PE placentas.
- Differential DIPs could distinguish PE from normal placentas.
- Upregulated DIPs in PE were associated with lipid metabolism and cellular processes; increased cytoplasmic endoglin observed.
Conclusions:
- PE placentas contain disease-relevant differential DIPs, indicating aberrant protein aggregation.
- These findings provide insights into the molecular mechanisms of PE.
- Proteomics data are publicly available for further research.
Abstract:
Preeclampsia (PE) is a placenta disease, featured by hypertension, proteinuria, and other multiorgan dysfunctions, and its etiology is unclear. We and others have shown that intensive endoplasmic reticulum (ER) stress and unfolded protein response (UPR) occur in the PE placenta. In this study, we isolated detergent-insoluble proteins (DIPs) from human placenta tissues, which were enriched with protein aggregates, to characterize the placenta UPR in PE. With data-independent acquisition (DIA) mass spectrometry, we identified 2066 DIPs across all normal (n = 10) and PE (n = 10) placenta samples, among which 110 and 108 DIPs were significantly up- and down-regulated in PE, respectively. Per clustering analysis, differential DIPs could generally distinguish PE from normal placentas. We verified the MS quantitation of endoglin and vimentin by immunoblotting. In addition, we observed that PE placenta tissues have remarkably more endoglin in the cytoplasm. Furthermore, we found that DIPs were evenly distributed across different chromosomes and could be enriched in diversified gene ontology terms, while differential DIPs avoided to distribute on X-chromosome. Significantly up-regulated DIPs in PE were focused on the top functions of lipid metabolism, while 23 of these DIPs could form the top network regulating cellular movement, development, growth, and proliferation. Our results implicate that human PE placentas have disease-relevant differential DIPs, which reflect aberrantly aggregated proteins of placental tissues. The mass spectrometry proteomics data have been deposited to ProteomeXchange consortium with the data set identifier PXD006654, and iProX database (accession number: IPX0000948000).
