iProXProteomicsYang ChenHomo Sapienshttp://www.iprox.org/page/project.html?id=IPX0007191000chenyang1816185048@bjmu.edu.cnPeking University Health Science Center, Peking UniversityiProXObstetric antiphospholipid syndrome (OAPS) is a multisystem disorder characterized by thrombosis or recurrent fetal loss. In this study, we aim to explore the pathological mechanism of OAPS. Herein, we carried out data-independent acquisition (DIA) mass spectrometry quantitative proteomic analysis of serum samples from OAPS patients and healthy controls. A set of 93 differentially expressed proteins was identified, including 75 upregulated and 18 downregulated proteins compared with the levels in controls. Those proteins are enriched in KEGG pathways related to autoimmune diseases, allergic diseases, and pathogen infection. Interestingly, metabolic pathways such as fatty acid degradation and type I diabetes were enriched, indicating that OAPS is metabolic disease related. The significantly increased triglyceride also supported this idea. The differentially expressed proteins insulin-like growth factor-binding protein-1 (IGFBP-1), C-reactive protein (CRP), and ferritin light chain (FTL) were validated by ELISA. Our study presented a deep serum proteomics of OAPS and advanced our understanding of OAPS pathogenesis.Proteomics of Serum Samples for the Exploration of the Pathological Mechanism of Obstetric Antiphospholipid Syndrome.Zhang Yinmei Y, Jin Shangjia S, Tian Wenmin W, Shi Dongxue D, Chen Yang Y, Cui Liyan L, Zheng Jiajia JfalseDIA proteomic of serum samples for the exploration of the pathological mechanism of Obstetric Antiphospholipid syndormeObstetric Antiphospholipid syndrome (OAPS) is a multisystem disorder characterized by thrombosis and/or recurrent fetal loss. In this study, we aim to further explore the pathological mechanism of OAPS. Herein, we carried out quantitative proteomic analysis of serum samples from OAPS patients and healthy controls to identify differentially expressed proteins between them. A data-independent Acquisition (DIA) mass spectrometry method for unbiased proteome profiling for the high sensitivity detection of clinical microsamples. A set of 93 proteins were differentially identified, including 75 up-regulated and 18 down-regulated proteins compared with the levels in controls. GO enrichment analysis showed that most of the differentially expressed proteins were located in extracellular region part, extracellular region and extracellular space, mainly involved in in biological processes such as response to chemical, response to organic substance and cellular response to chemical stimulus, and the main molecular functions are protein binding, receptor binding and identical protein binding. The most enriched KEGG pathways were autoimmune diseases and allergic diseases pathway, metabolic related pathways, pathogen infection pathways, and lysosome pathways. There were key nodes among the differentially expressed proteins including HLA-DRA,CRP and TNFSF13B. Our study formed a basis to perform new proteomic studies in OAPS to better understand the proteins involved in the pathogenesis of the syndrome and to provides the possibility to explore the pathogenesis of OAPS.Mon Sep 25 00:00:00 BST 2023PXD045626960638048430