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.

Label-free quantitative proteomics analysis reveals distinct molecular characteristics in endocardial endothelium

2018 ◽  
Vol 451 (1-2) ◽  
pp. 1-10 ◽  
Author(s):  
Abdul Jaleel ◽  
A. Aneesh Kumar ◽  
G. S. Ajith Kumar ◽  
Arun Surendran ◽  
Chandrashekaran C. Kartha
Keyword(s):  
Quantitative Proteomics ◽  
Molecular Characteristics ◽  
Label Free ◽  
Proteomics Analysis ◽  
Endocardial Endothelium

scholarly journals A Label-Free LC/MS/MS-Based Enzymatic Activity Assay for the Detection of Genuine Caspase Inhibitors and SAR Development

2013 ◽  
Vol 18 (8) ◽  
pp. 868-878 ◽  
Author(s):  
Michel C. Maillard ◽  
Celia Dominguez ◽  
Mark J. Gemkow ◽  
Florian Krieger ◽  
Hyunsun Park ◽  
...  
Keyword(s):  
Published Data ◽  
Tandem Mass ◽  
Label Free ◽  
Activity Assay ◽  
Fluorogenic Substrates ◽  
Enzymatic Assays ◽  
Chromatography Tandem Mass Spectrometry ◽  
Liquid Chromatography Tandem Mass ◽  
Enzymatic Activity Assay ◽  
Assay Interference

The resurgence of interest in caspases (Csp) as therapeutic targets for the treatment of neurodegenerative diseases prompted us to examine the suitability of published nonpeptidic Csp-3 and Csp-6 inhibitors for our medicinal chemistry programs. To support this effort, fluorescence-based Csp-2, Csp-3, and Csp-6 enzymatic assays were optimized for robustness against apparent enzyme inhibition caused by redox-cycling or aggregating compounds. The data obtained under these improved conditions challenge the validity of previously published data on Csp-3 and Csp-6 inhibitors for all but one series, namely, the isatins. Furthermore, in this series, it was observed that the nature of the rhodamine-labeled substrate, typically used to measure caspase activity, interfered with the pharmacological sensitivity of the Csp-2 assay. As a result, a liquid chromatography/tandem mass spectrometry–based assay that eliminates label-dependent assay interference was developed for Csp-2 and Csp-3. In these label-free assays, the activity values of the Csp-2 and Csp-3 reference inhibitors were in agreement with those obtained with the fluorogenic substrates. However, isatin 10a was 50-fold less potent in the label-free Csp-2 assay compared with the rhodamine-based fluorescence format, thus proving the need for an orthogonal readout to validate inhibitors in this class of targets highly susceptible to artifactual inhibition.

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.

Analysis of the uterine flush fluid proteome of healthy mares and mares with endometritis or fibrotic endometrial degeneration

2020 ◽  
Vol 32 (6) ◽  
pp. 572 ◽  
Author(s):  
Mariana Diel de Amorim ◽  
Firdous A. Khan ◽  
Tracey S. Chenier ◽  
Elizabeth L. Scholtz ◽  
M. Anthony Hayes
Keyword(s):  
Mass Spectrometry ◽  
Liquid Chromatography ◽  
Tandem Mass ◽  
Label Free ◽  
Chromatography Tandem Mass Spectrometry ◽  
Uterine Health ◽  
Liquid Chromatography Tandem Mass ◽  
Specific Proteins ◽  
Health And Disease ◽  
Flush Fluid

The objective of this study was to evaluate the differences in the uterine flush fluid proteome between healthy mares and mares with endometritis or fibrotic endometrial degeneration (FED). Uterine flush fluid samples were collected from healthy mares (n=8; oestrus n=5 and dioestrus n=3) and mares with endometritis (n=23; oestrus n=14 and dioestrus n=9) or FED (n=7; oestrus n=6 and dioestrus n=1). Proteomic analysis was performed using label-free liquid chromatography–tandem mass spectrometry. Of 216 proteins identified during oestrus, 127 were common to all three groups, one protein was exclusively detected in healthy mares, 47 proteins were exclusively detected in mares with endometritis and four proteins were exclusively detected in mares with FED. Of 188 proteins identified during dioestrus, 113 proteins were common between healthy mares and mares with endometritis, eight proteins were exclusively detected in healthy mares and 67 proteins were exclusively detected in mares with endometritis. Quantitative analysis revealed a subset of proteins differing in abundance between the three groups during oestrus and between healthy mares and mares with endometritis during dioestrus. These results provide a springboard for evaluation of specific proteins as biomarkers of uterine health and disease and for investigation of their roles in the establishment and maintenance of pregnancy.

Analysis of the human pituitary proteome by data independent label-free liquid chromatography tandem mass spectrometry

PROTEOMICS ◽  
2011 ◽  
Vol 11 (3) ◽  
pp. 495-500 ◽  
Author(s):  
Divya Krishnamurthy ◽  
Yishai Levin ◽  
Laura W. Harris ◽  
Yagnesh Umrania ◽  
Sabine Bahn ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Liquid Chromatography ◽  
Tandem Mass Spectrometry ◽  
Tandem Mass ◽  
Label Free ◽  
Human Pituitary ◽  
Chromatography Tandem Mass Spectrometry ◽  
Liquid Chromatography Tandem Mass

scholarly journals Hemocyte proteome of the Lake Baikal endemic Eulimnogammarus verrucosus (Crustacea: Amphipoda) sheds light on immune-related proteins

2021 ◽  
Vol 66 (4) ◽  
Author(s):  
Elena Zolotovskaya ◽  
Anna Nazarova ◽  
Alexandra Saranchina ◽  
Andrei Mutin ◽  
Polina Drozdova ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Immune Response ◽  
Pattern Recognition ◽  
Antimicrobial Activity ◽  
Liquid Chromatography ◽  
Lake Baikal ◽  
Tandem Mass ◽  
Chromatography Tandem Mass Spectrometry ◽  
Liquid Chromatography Tandem Mass ◽  
Related Proteins

Hemocytes are cells circulating in the hemolymph and playing an important role in crustacean immunity. These cells not only function as phagocytes but also express immune compounds to the hemolymph. Here we obtained hemocyte proteome of the endemic amphipod (Amphipoda, Crustacea) Eulimnogammarus verrucosus from Lake Baikal, the first hemocyte proteome of an amphipod, using liquid chromatography/tandem mass spectrometry (LC-MS/MS). A total of 1152 unique proteins were discovered with LC-MS/MS. We discovered both proteins directly involved in the immune response, such as pattern recognition proteins (C-type lectins), and compounds with antimicrobial activity (ctenidin and anti-lipopolysaccharide factor/scygonadin). Moreover, hemocyanins which may act as a phenoloxidase and C-type lectins were among the most diverse protein groups in the hemocyte proteome. The obtained data can be useful for further studies of immune components and mechanisms in Baikal amphipods.

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