scholarly journals Comparison of urine proteome among rat models by intraperitoneal injection with single bacteria and co-injection with two bacteria

PLoS ONE ◽  
2021 ◽  
Vol 16 (12) ◽  
pp. e0261488
Author(s):  
Wenshu Meng ◽  
Chenyang Zhao ◽  
Youhe Gao
Keyword(s):  
Mass Spectrometry ◽  
Intraperitoneal Injection ◽  
Single Injection ◽  
Tandem Mass ◽  
Human Pathogens ◽  
Rat Models ◽  
Urine Proteome ◽  
Differential Proteins ◽  
Proteome Changes ◽  
S Model

Purpose To explore and compare urine proteome changes among rat models by intraperitoneal injection with single bacteria and co-injection with two bacteria. Method Escherichia coli and Staphylococcus aureus are two common human pathogens. Three rat models were established: (i) the intraperitoneal co-injection of E. coli and S. aureus model (ES model), (ii) intraperitoneal injection of E. coli model (E model), and (iii) intraperitoneal injection of S. aureus model (S model). Urinary proteomes on days 0, 1 and 2 of the three models were analyzed by liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS). Results A total of 111, 34 and 94 differential proteins were identified in the ES model, E model and S model, respectively. Among them, some differential proteins were reported to be associated with bacterial infection. Approximately 47% differential proteins in the E model overlapped with ES model, and 37% differential proteins in the S model overlapped with ES model. Compared with the E model and S model, a total of 71 unique differential proteins were identified in the ES model. Conclusion Our results indicated that (1) the urine proteome could distinguish different bacterial intraperitoneal injections models and (2) the effects of co-injection with two bacteria on the urine proteome were not simple superposition of single injection.

scholarly journals Lysophospholipids, Lysophosphatidic Acids and Monoacylglycerols: New Therapeutic Targets in Cardiovascular Diseases?

2021 ◽  
Author(s):  
Thomas Duflot ◽  
Ly Tu ◽  
Matthieu Leuillier ◽  
Hind Messaoudi ◽  
Déborah Groussard ◽  
...  
Keyword(s):  
Heart Failure ◽  
Mass Spectrometry ◽  
Pulmonary Hypertension ◽  
Cardiovascular Diseases ◽  
Multiple Testing ◽  
Premature Death ◽  
The Other ◽  
Tandem Mass ◽  
Rat Models ◽  
Induced Hypertension

Cardiovascular diseases (CVD) are the leading cause of premature death and disability in humans. Increasing data suggest that CVD is closely related to lipid metabolism and signaling. This study aimed to assess whether circulating lysophospholipids (LPL), lysophosphatidic acids (LPA) and monoacylglycerols (MAG) may be considered as biomarkers of CVD. For this objective, the evolution of the plasma levels of 22 compounds (13 LPL, 6 LPA and 3 MAG) was monitored by liquid chromatography coupled with tandem mass spectrometry (HPLC/MS²) in different rat models of CVD, i.e. angiotensin-II-induced hypertension (HTN), ischemic chronic heart failure (CHF) and sugen/hypoxia(SuHx)-induced pulmonary hypertension (PH). On one hand, there was modest changes on the monitored compounds in HTN (LPA 16:0, 18:1 and 20:4), LPC 16:1) and CHF (LPA 16:0, LPC 18:1 and LPE 16:0 and 18:0) models compared to control rats but these changes were no longer significant after correction for multiple testing. On the other hand, PH was associated with important changes in plasma LPA with a significant increase in the 16:0, 18:1, 18:2, 20:4 and 22:6 species. A deleterious impact of LPA was confirmed on isolated human pulmonary smooth muscle cells with an increase in their proliferation. This study demonstrates that circulating LPA species are increased in rats with PH and may contribute to the pathophysiology of this disease. Additional experiments are needed to assess whether the modulation of LPA signaling in PH may be of interest.

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 Synthesis Spectroscopy and Computational Studies of Manganese (II) Complexes Incorporating (N,O)(O,O`) Ligands and Their Biological Activity

2019 ◽  
pp. 1-10
Author(s):  
Rania Ahmad Abokhater ◽  
Salem Eltuhami Ashoor ◽  
Suad A. Gadir
Keyword(s):  
Mass Spectrometry ◽  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Optimization Method ◽  
Computational Studies ◽  
Tandem Mass ◽  
Convergence Criteria ◽  
Human Pathogens ◽  
Klebsiella Spp ◽  
Chloride Hydrate

Manganese (II) complexes were synthesized via the reaction equimolar quantity of Manganese(II) chloride-hydrate (MnCl2.6H2O) with Chiral saccharides such {(OH)5(CH2)(C5H5)O} or {(OH)6(CH2)(C5H5)O} and (C9H7NO) as secondary ligands [Mn(C9H7NO){(OH)5(CH2)(C5H5)O}]Cl2 (C1), [Mn(QH){(OH)6(CH2)(C5H5)O}]Cl2 (C2), respectively where (C9H7NO) is 8-hydroxyquinoline, {(OH)5(CH2)(C5H5)O} Dextrose (Dex), {(OH)6(CH2)(C5H5)O} fructose (fru). Theses complexes were characterized by UV-vis, IR spectroscopy, tandem mass spectrometry and elemental analysis. The complexes have been found to have square planer geometry as the optimization method. The molecular geometries obtained from XRD data. The pre-optimized to standard convergence criteria using the basis Minimize Energy to Minimum. The isolated compounds were screened for its antibacterial activity against six standard human pathogens (Staphylococcus aureus, Streptococcus spp., Escherichia coli, Klebsiella spp., Psuedomones spp. and Protues spp.) and the results were obtained. About 10 to 70% for complex (C1) and about 10 to 60% for complex (C2) of the activity.

scholarly journals Urine proteome changes in a chronic unpredictable mild stress (CUMS) mouse model of major depressive disorder

2020 ◽  
Author(s):  
Yuhang Huan ◽  
Jing Wei ◽  
Tong Su ◽  
Youhe Gao
Keyword(s):  
Major Depressive Disorder ◽  
Mouse Model ◽  
Depressive Disorder ◽  
Mild Stress ◽  
Chronic Unpredictable Mild Stress ◽  
Major Depressive ◽  
Urine Proteome ◽  
Random Combination ◽  
Differential Proteins ◽  
Proteome Changes

AbstractBackgroundMajor depressive disorder (MDD) is a prevalent complex psychiatric disorder with a high prevalence rate. Because MDD is a systemic multifactorial disorder involving complex interactions and disturbances of various molecular pathways, there are no effective biomarkers for clinical diagnosis. Urine is not subjected to homeostatic control, allowing it to reflect the sensitive and comprehensive changes that occur in various diseases. In this study, we examined the urine proteome changes in a CUMS mouse model of MDD.MethodsMale C57BL/6 mice were subjected to chronic unpredictable mild stress for 5 weeks. The tail suspension test (TST) and sucrose consumption test (SCT) were then applied to evaluate depression-like behaviors. The urine proteomes on day 0 and day 36 in the CUMS group were profiled by liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS).ResultsA total of 45 differential proteins were identified, 24 of which have been associated with the pathogenic mechanisms of MDD, while 10 proteins have been previously suggested as MDD biomarkers. There was an average of two differential proteins that were identified through 1048574 random combination statistical analyses, indicating that at least 95% of the differential proteins were reliable and not the result of random combination. The differential proteins were mainly associated with blood coagulation, inflammatory responses and central nervous system development.ConclusionsOur preliminary results indicated that the urine proteome can reflect changes associated with MDD in the CUMS model, which provides potential clues for the diagnosis of clinical MDD patients.

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