Analysis of the Mouse Liver Proteome Using Advanced Mass Spectrometry

2007 ◽  
Vol 6 (8) ◽  
pp. 2963-2972 ◽  
Author(s):  
Rong Shi ◽  
Chanchal Kumar ◽  
Alexandre Zougman ◽  
Yanling Zhang ◽  
Alexandre Podtelejnikov ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Mouse Liver ◽  
Liver Proteome

scholarly journals Histone Adduction with Nicotine: A Bio-Ams Study

Radiocarbon ◽  
1997 ◽  
Vol 39 (3) ◽  
pp. 293-297 ◽  
Author(s):  
X. H. Wu ◽  
H. F. Wang ◽  
Y. F. Liu ◽  
X. Y. Lu ◽  
J. J. Wang ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Accelerator Mass Spectrometry ◽  
Human Exposure ◽  
Mouse Liver ◽  
Dose Range ◽  
The Other ◽  
Histone 3 ◽  
Protein Adduction ◽  
Dna Adduction

Based on the study of DNA adduction with nicotine, we have measured the mouse hepatic histone adduction with 14C-labeled nicotine in vivo by bio-accelerator mass spectrometry (bio-AMS). In the exposure of mice to nicotine, the dose range administered was from 0.2 μg to 6.0 μg kg b.w.-1, which was equivalent to a very low level of human exposure to cigarette smoke. The adducts of either histone 1 (H1) or histone 3 (H3) with nicotine in mouse liver increased markedly with increasing nicotine dose. Our results have demonstrated that in the study of protein adduction with toxic xenobiotics as a biomarker, the AMS method achieves the highest sensitivity, 4.6 × 10-17 mol (46 amol) adducts per mg H1 protein, compared to all the other methods used previously.

scholarly journals Control of protein function through oxidation and reduction of persulfidated states

2020 ◽  
Vol 6 (1) ◽  
pp. eaax8358 ◽  
Author(s):  
É. Dóka ◽  
T. Ida ◽  
M. Dagnell ◽  
Y. Abiko ◽  
N. C. Luong ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Mouse Liver ◽  
Cellular Responses ◽  
Selenium Supplementation ◽  
Related Protein ◽  
Loss Of Function ◽  
Quantitative Mass Spectrometry ◽  
Irreversible Oxidation ◽  
Thioredoxin System

Irreversible oxidation of Cys residues to sulfinic/sulfonic forms typically impairs protein function. We found that persulfidation (CysSSH) protects Cys from irreversible oxidative loss of function by the formation of CysSSO1-3H derivatives that can subsequently be reduced back to native thiols. Reductive reactivation of oxidized persulfides by the thioredoxin system was demonstrated in albumin, Prx2, and PTP1B. In cells, this mechanism protects and regulates key proteins of signaling pathways, including Prx2, PTEN, PTP1B, HSP90, and KEAP1. Using quantitative mass spectrometry, we show that (i) CysSSH and CysSSO3H species are abundant in mouse liver and enzymatically regulated by the glutathione and thioredoxin systems and (ii) deletion of the thioredoxin-related protein TRP14 in mice altered CysSSH levels on a subset of proteins, predicting a role for TRP14 in persulfide signaling. Furthermore, selenium supplementation, polysulfide treatment, or knockdown of TRP14 mediated cellular responses to EGF, suggesting a role for TrxR1/TRP14-regulated oxidative persulfidation in growth factor responsiveness.

Development of an Ion-Pair Reverse-Phase Liquid Chromatographic/Tandem Mass Spectrometry Method for the Determination of an 18-Mer Phosphorothioate Oligonucleotide in Mouse Liver Tissue

2005 ◽  
Vol 11 (2) ◽  
pp. 209-215 ◽  
Author(s):  
Anthony T. Murphy ◽  
Patricia Brown-Augsburger ◽  
Rosie Z. Yu ◽  
Richard S. Geary ◽  
Stefan Thibodeaux ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Liver Tissue ◽  
Mouse Liver ◽  
Ion Pair ◽  
Tandem Mass ◽  
Phosphorothioate Oligonucleotide ◽  
Reverse Phase ◽  
Discovery Research

A quantitative method for the determination of a partially modified, 2′-ribose alkoxy 18-mer phosphorothioate oligonucleotide in liver tissue has been developed. A liquid:liquid extraction, ion-pair reverse phase chromatographic separation and tandem mass spectrometry were used to achieve a quantitation range of 125 to 10,000 ng g−1 mouse liver tissue. A total cycle time of 5 min was obtained while maintaining separation of three potential impurities. Separations were performed using a Discovery RP-Amide C16, 100 × 2 mm column packed with 5 μm particles. The separation was facilitated by the use of triethylamine (TEA) and hexafluoroisopropanol (HFIP) as ion-pair agents. The method has subsequently been used for the determination of other phosphorothioate oligonucleotides in support of discovery research.

Identification of glycerophospholipid fatty acid remodeling by using mass spectrometry imaging in bisphenol S induced mouse liver

2018 ◽  
Vol 29 (8) ◽  
pp. 1281-1283 ◽  
Author(s):  
Chao Zhao ◽  
Peisi Xie ◽  
Ti Yang ◽  
Hailin Wang ◽  
Arthur Chi Kong Chung ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Fatty Acid ◽  
Mouse Liver ◽  
Mass Spectrometry Imaging ◽  
Bisphenol S
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