scholarly journals Proteomic Changes in Chicken Plasma Induced by Salmonella typhimurium Lipopolysaccharides

2016 ◽  
Vol 7 ◽  
pp. PRI.S31609 ◽  
Author(s):  
Balamurugan Packialakshmi ◽  
Rohana Liyanage ◽  
Jackson O. Lay ◽  
Sarbjeet K. Makkar ◽  
Narayan C. Rath
Keyword(s):  
Mass Spectrometry ◽  
Defense Mechanisms ◽  
Gram Negative Bacteria ◽  
Laser Desorption Ionization ◽  
Label Free ◽  
Flight Mass Spectrometry ◽  
Chromatography Tandem Mass Spectrometry ◽  
Liquid Chromatography Tandem Mass ◽  
Infection And Inflammation ◽  
Wall Components

Lipopolysaccharides (LPS) are cell wall components of Gram-negative bacteria that produce inflammation and sickness in higher animals. The objective was to identify plasma proteomic changes in an avian model of inflammation. Chickens were treated with either saline or LPS, and blood was collected at 24 hours postinjection. The pooled plasma samples were depleted of high-abundant proteins and analyzed by matrix-assisted laser desorption ionization (MALDI)-time-of-flight mass spectrometry and liquid chromatography–tandem mass spectrometry (LC–MS/MS). MALDI analyses showed an increase in fibrinogen beta-derived peptide and a decrease in apolipoprotein-AII-derived peptide in LPS samples. Label-free quantitation of LC–MS/MS spectra revealed an increase in the levels of α1-acid glycoprotein, a chemokine CCLI10, and cathelicidin-2, but a decrease in an interferonstimulated gene-12-2 protein in the LPS group. These differentially expressed proteins are associated with immunomodulation, cytokine changes, and defense mechanisms, which may be useful as candidate biomarkers of infection and inflammation.

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
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