scholarly journals Proteomic mapping of atrial and ventricular heart tissue in patients with aortic valve stenosis

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Boris Barbarics ◽  
Katja Eildermann ◽  
Lars Kaderali ◽  
Lukas Cyganek ◽  
Uwe Plessmann ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
High Resolution ◽  
Aortic Valve ◽  
Aortic Valve Stenosis ◽  
High Resolution Mass Spectrometry ◽  
Heart Tissue ◽  
Left Ventricular ◽  
Myocardial Tissue ◽  
High Resolution Mass ◽  
Resolution Mass

AbstractAortic valve stenosis (AVS) is one of the most common valve diseases in the world. However, detailed biological understanding of the myocardial changes in AVS hearts on the proteome level is still lacking. Proteomic studies using high-resolution mass spectrometry of formalin-fixed and paraffin-embedded (FFPE) human myocardial tissue of AVS-patients are very rare due to methodical issues. To overcome these issues this study used high resolution mass spectrometry in combination with a stem cell-derived cardiac specific protein quantification-standard to profile the proteomes of 17 atrial and 29 left ventricular myocardial FFPE human myocardial tissue samples from AVS-patients. In our proteomic analysis we quantified a median of 1980 (range 1495–2281) proteins in every single sample and identified significant upregulation of 239 proteins in atrial and 54 proteins in ventricular myocardium. We compared the proteins with published data. Well studied proteins reflect disease-related changes in AVS, such as cardiac hypertrophy, development of fibrosis, impairment of mitochondria and downregulated blood supply. In summary, we provide both a workflow for quantitative proteomics of human FFPE heart tissue and a comprehensive proteomic resource for AVS induced changes in the human myocardium.

scholarly journals Proteomic Analysis of Cardiac Adaptation to Exercise by High Resolution Mass Spectrometry

2021 ◽  
Vol 8 ◽  
Author(s):  
Afnan Saleh Al-Menhali ◽  
Cali Anderson ◽  
Alexander V. Gourine ◽  
Andrey Y. Abramov ◽  
Alicia D’Souza ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
High Resolution ◽  
Exercise Training ◽  
High Resolution Mass Spectrometry ◽  
High Energy ◽  
Left Ventricular ◽  
Beneficial Effects ◽  
High Resolution Mass ◽  
Ventricular Tissue ◽  
Resolution Mass

Regular exercise has many health benefits, among which is a significant reduction of cardiovascular risk. Although many beneficial effects of exercise are well described, the exact mechanisms by which exercise confers cardiovascular benefits are yet to be fully understood. In the current study, we have used high resolution mass spectrometry to determine the proteomic responses of the heart to exercise training in mice. The impact of exercise-induced oxidative stress on modifications of cardiomyocyte proteins with lipid peroxidation biomarker 4-hydroxynonenal (4-HNE) was examined as well. Fourteen male mice were randomized into the control (sedentary) group and the exercise group that was subjected to a swim exercise training program for 5 days a week for 5 months. Proteins were isolated from the left ventricular tissue, fractionated and digested for shotgun proteomics. Peptides were separated by nanoliquid chromatography and analyzed on an Orbitrap Fusion mass spectrometer using high-energy collision–induced dissociation and electron transfer dissociation fragmentation. We identified distinct ventricular protein signatures established in response to exercise training. Comparative proteomics identified 23 proteins that were upregulated and 37 proteins that were downregulated with exercise, in addition to 65 proteins that were identified only in ventricular tissue samples of exercised mice. Most of the proteins specific to exercised mice are involved in respiratory electron transport and/or implicated in glutathione conjugation. Additionally, 10 proteins were found to be modified with 4-HNE. This study provides new data on the effects of exercise on the cardiac proteome and contributes to our understanding of the molecular mechanisms underlying the beneficial effects of exercise on the heart.

Exploring the Active Compounds of Traditional Mongolian Medicine Agsirga in Intervention of Novel Coronavirus (2019-nCoV) Based on HPLC-Q-Exactive-MS/MS and Molecular Docking Method

2020 ◽  
Author(s):  
Jie Cheng ◽  
Yuchen Tang ◽  
Baoquan Bao ◽  
Ping Zhang
Keyword(s):  
Mass Spectrometry ◽  
Molecular Docking ◽  
High Resolution ◽  
Mass Spectra ◽  
High Resolution Mass Spectrometry ◽  
Structural Formula ◽  
Active Compounds ◽  
High Resolution Mass ◽  
Q Exactive ◽  
Resolution Mass

<p><a></a><a></a><a></a><a><b>Objective</b></a>: To screen all compounds of Agsirga based on the HPLC-Q-Exactive high-resolution mass spectrometry and find potential inhibitors that can respond to 2019-nCoV from active compounds of Agsirga by molecular docking technology.</p> <p><b>Methods</b>: HPLC-Q-Exactive high-resolution mass spectrometry was adopted to identify the complex components of Mongolian medicine Agsirga, and separated by the high-resolution mass spectrometry Q-Exactive detector. Then the Orbitrap detector was used in tandem high-resolution mass spectrometry, and the related molecular and structural formula were found by using the chemsipider database and related literature, combined with precise molecular formulas (errors ≤ 5 × 10<sup>−6</sup>) , retention time, primary mass spectra, and secondary mass spectra information, The fragmentation regularities of mass spectra of these compounds were deduced. Taking ACE2 as the receptor and deduced compounds as the ligand, all of them were pretreated by discover studio, autodock and Chem3D. The molecular docking between the active ingredients and the target protein was studied by using AutoDock molecular docking software. The interaction between ligand and receptor is applied to provide a choice for screening anti-2019-nCoV drugs.</p> <p><b>Result</b>: Based on the fragmentation patterns of the reference compounds and consulting literature, a total of 96 major alkaloids and stilbenes were screened and identified in Agsirga by the HPLC-Q-Exactive-MS/MS method. Combining with molecular docking, a conclusion was got that there are potential active substances in Mongolian medicine Agsirga which can block the binding of ACE2 and 2019-nCoV at the molecular level.</p>

Determination of quaternary ammonium compounds in food products by the method of ultra-performance liquid chromatography/high resolution mass-spectrometry

2020 ◽  
Vol 86 (8) ◽  
pp. 23-31
Author(s):  
V. G. Amelin ◽  
D. S. Bolshakov
Keyword(s):  
Mass Spectrometry ◽  
High Resolution ◽  
Quaternary Ammonium ◽  
High Resolution Mass Spectrometry ◽  
Food Products ◽  
Quaternary Ammonium Compounds ◽  
High Resolution Mass ◽  
Ammonium Compounds ◽  
Resolution Mass

The goal of the study is developing a methodology for determination of the residual amounts of quaternary ammonium compounds (QAC) in food products by UHPLC/high-resolution mass spectrometry after water-acetonitrile extraction of the determined components from the analyzed samples. The identification and determination of QAC was carried out on an «UltiMate 3000» ultra-high-performance liquid chromatograph (Thermo Scientific, USA) equipped with a «maXis 4G» high-resolution quadrupole-time-of-flight mass spectrometric detector and an ion spray «ionBooster» source (Bruker Daltonics, Germany). Samples of milk, cheese (upper cortical layer), dumplings, pork, chicken skin and ground beef were used as working samples. Optimal conditions are specified for chromatographic separation of the mixture of five QAC, two of them being a mixture of homologues with a linear structure (including isomeric forms). The identification of QAC is carried out by the retention time, exact mass of the ions, and coincidence of the mSigma isotopic distribution. The limits for QAC detection are 0.1 – 0.5 ng/ml, the determination limits are 1 ng/ml for aqueous standard solutions. The determinable content of QAC in food products ranges within 1 – 100 ng/g. The results of analysis revealed the residual amount of QAC present in all samples, which confirms data of numerous sources of information about active use of QAC-based disinfectants in the meat and dairy industry. The correctness of the obtained results is verified by introduction of the additives in food products at a level of 10 ng/g for each QAC. The relative standard deviation of the analysis results does not exceed 0.18. The duration of the analysis is 30 – 40 min.

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