scholarly journals Using one–to–many urine proteome comparisons to provide clues for fever of unknown origin

2021 ◽  
Author(s):  
Chenyang Zhao ◽  
Lilong Wei ◽  
Jing Wei ◽  
Youhe Gao
Keyword(s):  
Acute Phase Response ◽  
Fever Of Unknown Origin ◽  
Unknown Origin ◽  
Biological Pathways ◽  
Combined Method ◽  
Proteomics Analysis ◽  
Urine Proteomics ◽  
Chromatography Tandem Mass Spectrometry ◽  
Differential Proteins ◽  
Liquid Chromatography Tandem Mass

AbstractObjectiveTo provide diagnostic evidence and clues for patients with fever of unknown origin (FUO) through urine proteomics analysis.MethodsUrine samples of FUO were one–to–many analysed by using liquid chromatography tandem mass spectrometry(LC–MS/MS) to identify differential proteins and related biological pathways. One–to–many analysis means a comparative analysis of one sample to many controls.ResultsWe observed biological pathways related to fever, such as LXR/RXR activation, FXR/RXR activation and acute phase response signaling, etc., which indicates that urine can obviously distinguish disease from health status. In addition, we found that the results of each sample were different, which highlight the necessity of one–to–many analysis.ConclusionsThe combined method of urine proteomics and one–to–many analysis can provide clues for FUO, and might also be applied to the exploration of any unknown disease.

scholarly journals Dynamic changes in the urine proteome of tumor-bearing mouse models of B16 melanoma and RM-1 prostate cancer

2020 ◽  
Author(s):  
Lujun Li ◽  
Xuanzhen Pan ◽  
Yongtao Liu ◽  
Ting Wang ◽  
Youhe Gao
Keyword(s):  
Prostate Cancer ◽  
Mouse Models ◽  
Dynamic Changes ◽  
Urine Proteome ◽  
Early Biomarkers ◽  
Tumor Bearing ◽  
Data Independent Acquisition ◽  
Chromatography Tandem Mass Spectrometry ◽  
Differential Proteins ◽  
Liquid Chromatography Tandem Mass

AbstractUrine can accumulate changes and reflect early physiological and pathological changes of various diseases, such as tumors. Therefore, urine is an ideal source for identification of early biomarkers. In this study, melanoma and prostate cancer-bearing mouse models were established by subcutaneous injection of B16 and RM-1 cells, respectively. Urine samples were collected at four time points during tumor growth. Based on data-independent acquisition (DIA) technology, liquid chromatography-tandem mass spectrometry (LC-MS/MS) was used for quantitative analysis. Compared with those before the injection of B16 cells, 38 human homologous differential proteins were identified, and 18 proteins were reported to be related to melanoma. Before the tumor was visible, there were 4 differential proteins, and all were reported to be related to melanoma. Compared with that before the injection of RM-1 cells, a total of 14 human homologous differential proteins were identified, and 9 proteins were reported to be associated with prostate cancer. Before the tumor was palpable, 9 proteins showed significant differences. There were significant differences between the two tumor-bearing models. Through the above experiments and analysis, we found that the urine proteome can reflect the changes in the development and provide early biomarkers of the two tumors and provide clues for the early clinical diagnosis of these diseases.

scholarly journals Neuroanatomical Quantitative Proteomics Reveals Common Pathogenic Biological Routes between Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Dementia (FTD)

2018 ◽  
Vol 20 (1) ◽  
pp. 4 ◽  
Author(s):  
Marina Iridoy ◽  
Irene Zubiri ◽  
María Zelaya ◽  
Leyre Martinez ◽  
Karina Ausín ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Amyotrophic Lateral Sclerosis ◽  
Frontotemporal Dementia ◽  
Quantitative Proteomics ◽  
Binding Protein ◽  
Proteomics Analysis ◽  
Differential Proteins ◽  
Liquid Chromatography Tandem Mass ◽  
Specific Proteins ◽  
Lateral Sclerosis

(1) Background: Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are neurodegenerative disorders with an overlap in clinical presentation and neuropathology. Common and differential mechanisms leading to protein expression changes and neurodegeneration in ALS and FTD were studied trough a deep neuroproteome mapping of the spinal cord. (2) Methods: A liquid chromatography tandem mass spectrometry (LC-MS/MS) analysis of the spinal cord from ALS-TAR DNA-binding protein 43 (TDP-43) subjects, ubiquitin-positive frontotemporal lobar degeneration (FTLD-U) subjects and controls without neurodegenerative disease was performed. (3) Results: 281 differentially expressed proteins were detected among ALS versus controls, while 52 proteins were dysregulated among FTLD-U versus controls. Thirty-three differential proteins were shared between both syndromes. The resulting data was subjected to network-driven proteomics analysis, revealing mitochondrial dysfunction and metabolic impairment, both for ALS and FTLD-U that could be validated through the confirmation of expression levels changes of the Prohibitin (PHB) complex. (4) Conclusions: ALS-TDP-43 and FTLD-U share molecular and functional alterations, although part of the proteostatic impairment is region- and disease-specific. We have confirmed the involvement of specific proteins previously associated with ALS (Galectin 2 (LGALS3), Transthyretin (TTR), Protein S100-A6 (S100A6), and Protein S100-A11 (S100A11)) and have shown the involvement of proteins not previously described in the ALS context (Methanethiol oxidase (SELENBP1), Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN-1), Calcyclin-binding protein (CACYBP) and Rho-associated protein kinase 2 (ROCK2)).

scholarly journals Urine proteome changes in an α-synuclein transgenic mouse model of Parkinson’s disease

2020 ◽  
Author(s):  
Lujun Li ◽  
Xuanzhen Pan ◽  
Ting Wang ◽  
Yuanrui Hua ◽  
Youhe Gao
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Transgenic Mice ◽  
Urine Proteome ◽  
Data Independent Acquisition ◽  
Chromatography Tandem Mass Spectrometry ◽  
Differential Proteins ◽  
Liquid Chromatography Tandem Mass ◽  
Proteome Changes ◽  
Old Mice

AbstractUrine accommodates more changes than other fluids, and it is a good source in the search for early sensitive biomarkers. The present study collected urine samples from 2-, 4-, 6-, 8- and 10-month-old α-synuclein transgenic mice. Based on data-independent acquisition (DIA) technology, liquid chromatography-tandem mass spectrometry (LC-MS/MS) was used for quantitative analysis. Seventeen human homologous differential proteins were screened and compared with those in the urine of 2-month-old mice, and 9 proteins were related to Parkinson’s disease (PD). Formin-2, Splicing factor 3A subunit 1, and Isopentenyl-diphosphate Delta-isomerase 1 changed continuously in months 6, 8 and 10. These experiments and analyses demonstrated that the urine proteome reflected the development of α-synuclein transgenic mice and provided clues for the early clinical diagnosis of PD.

scholarly journals Proteomics Analysis Reveals Diverse Molecular Characteristics between Endocardial and Aortic-Valvular Endothelium

Genes ◽  
2021 ◽  
Vol 12 (7) ◽  
pp. 1005
Author(s):  
A. Aneesh Kumar ◽  
G. S. Ajith Kumar ◽  
Gopika Satheesh ◽  
Arun Surendran ◽  
Mahesh Chandran ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Profile ◽  
Molecular Characteristics ◽  
Cell Surface Markers ◽  
Label Free ◽  
Proteomics Analysis ◽  
Chromatography Tandem Mass Spectrometry ◽  
Liquid Chromatography Tandem Mass ◽  
Related Proteins ◽  
Endocardial Endothelium

The variations in the protein profile of aortic-valvular (AVE) and endocardial endothelial (EE) cells are currently unknown. The current study’s objective is to identify differentially expressed proteins and associated pathways in both the endothelial cells. We used endothelial cells isolated from the porcine (Sus scrofa) aortic valve and endocardium for the profiling of proteins. Label-free proteomics was performed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Our proteomics analysis revealed that 29 proteins were highly expressed, and 25 proteins were less expressed in the valve than the endocardial endothelium. The cell surface markers, such as CD63, ICAM1, PECAM1, PROCR, and TFRC, were highly expressed in EE. In contrast, CD44 was highly expressed in AVE. The pathway analysis showed that metabolic process-related proteins and extracellular matrix-related proteins were enriched in valves. Differential enrichment of signaling pathways was observed in the endocardium. The hemostasis function-related proteins were increased in both endothelial cells. The proteins and pathways enriched in aortic-valvular and endocardial endothelial cells revealed the distinct phenotype of these two closely related cells.

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