Dataset Information

Promotion of Subtotal Uterine Reconstruction by a Tissue-engineered Uterus Biomimeticing Structure and Extracellular Matrix Microenvironment

ABSTRACT: To better characterize the ECM signature of the ECMEC-SIS and ECMSMC-PU/SIS, a 4D label free proteomic analyses was carried out. In total 2761 and 1520 proteins have been identified for the ECMEC-SIS and ECMSMC-PU/SIS, respectively, including 1055 in common . An ECM-specific categorization database, MatrisomeDB 2.0, was employed to analyze the ECM matrisome protein and ECM-associated proteins.In the ECMEC-SIS group, the ECM matisome, matrisome-associated, and other proteins have accounted for 17.87%, 17.00%, and 65.13%, respectively. However, the proportion of ECM proteins, especially glycoproteins and regulators, was greater in ECMSMC-PU/SIS group compared with the ECMEC-SIS group. In the ECMSMC-PU/SIS group, the ECM matisome, matrisome-associated, and other proteins have accounted for 26.39%, 20.85%, and 52.77%, respectively.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture, Uterine Smooth Muscle Cell

DISEASE(S): Disease Free

SUBMITTER: Long-mei Zhao

LAB HEAD: Hui-qi Xie

PROVIDER: PXD041467 | Pride | 2024-01-26

REPOSITORIES: pride

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Promotion of uterine reconstruction by a tissue-engineered uterus with biomimetic structure and extracellular matrix microenvironment.

Zhao Long-Mei LM Da Lin-Cui LC Wang Rui R Wang Long L Jiang Yan-Lin YL Zhang Xiu-Zhen XZ Li Ya-Xing YX Lei Xiong-Xin XX Song Yu-Ting YT Zou Chen-Yu CY Huang Li-Ping LP Zhang Wen-Qian WQ Zhang Qing-Yi QY Li Qian-Jin QJ Nie Rong R Zhang Yi Y Liang Yan Y Li-Ling Jesse J Xie Hui-Qi HQ

Science advances 20231115 46

The recurrence rate for severe intrauterine adhesions is as high as 60%, and there is still lack of effective prevention and treatment. Inspired by the nature of uterus, we have developed a bilayer scaffold (ECM-SPS) with biomimetic heterogeneous features and extracellular matrix (ECM) microenvironment of the uterus. As proved by subtotal uterine reconstruction experiments, the mechanical and antiadhesion properties of the bilayer scaffold could meet the requirement for uterine repair. With the ...[more]

PMID: 37967178

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Project description:The current state of proteomics requires a choice between targeted and discovery methods. The former provides exceptional quantitation and data completeness, but only with few analytes. Discovery proteomics can identify hundreds and thousands of proteins in a sample, but with poor quantitation and data completeness. We have established and optimized a method that combines targeted and data-independent acquisition for absolute quantitation of all plasma proteins in a single sequential window acquisition of all theoretical fragment ions (SWATH) acquisition run using a panel of spike-in standards (SIS). We compared the absolute quantitation (AQ) of SWATH and high-resolution multiple-reaction monitoring (MRM-HR) acquisition methods using the 100 protein PlasmaDive SIS panel spiked into human plasma. SWATH provided equivalent quantitation and differentially abundant protein profiles as MRM-HR. Absolute quantities of the SIS peptides from the SWATH data were used to estimate the absolute quantities (eAQ) for all the proteins in the run. The eAQ values provided similar quantitation and differentially abundant protein profiles as AQ and protein group (PG) values, and the eAQ method was the only scheme where all selected proteins were verified by MRM-HR. We applied the eAQ method to a cohort of 16 non-small cell lung cancer (NSCLC) patients receiving immunotherapeutics and found that fibronectin (FN1) and proteoglycan 4 (PRG4) were useful markers for predicting patients who would stay on these agents for at least 6 months (area under the curve of 0.8438 and 0.6735, respectively). Thirteen additional plasma samples confirmed that FN1 and PRG4 are putative biomarkers (positive predictive value is 100% and 85.7%, respectively) for a prolonged (>6 months) response to immunotherapeutic agents. In conclusion, we describe an optimized method for absolute quantification of all proteins in a SWATH run, and this approach is amenable for the identification of plasma biomarkers.

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