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Proteomics study of N-acetylcysteine response in H1N1-infected cells by using mass spectrometry

tetano

Editor, Senior Moderator
Rapid Commun Mass Spectrom. 2014 Apr 15;28(7):741-9. doi: 10.1002/rcm.6840.
Proteomics study of N-acetylcysteine response in H1N1-infected cells by using mass spectrometry.
Wu H1, Song W, Gao X, Liu N, Wang P, Chen H, Cai Z.
Author information
Abstract
RATIONALE:

The pathology of A/Puerto Rico/8/1934 (H1N1) infection associated with the interaction of virus and its host cells is not clear. N-Acetylcysteine (NAC) is an antioxidant as well as a premier antitoxin and immune support substance. A high dose of NAC was recently reported for a therapy of H1N1 (2009) influenza pneumonia.
METHODS:

NAC was used as a small-molecule organic probe to investigate the protein expression of human lung carcinoma cell line (A549) infected by influenza virus A/Puerto Rico/8/1934 (H1N1). Differential proteins were identified from MALDI-TOF MS and Q-TOF MS/MS analyses.
RESULTS:

The obtained results showed that NAC kept cells away from apoptosis. Virus-infected cells were arrested in G0/G1 phase. The lowest cell population of G0/G1 phase was detected when the cells were treated by 10 mM NAC for one day. Application of MS-based proteomics allowed the identification of the differential proteins. Software analysis showed that four proteins had close relationship.
CONCLUSIONS:

The results indicated that NAC as a small-molecule probe might effect the protein expression of A549 cells infected by the H1N1 virus. Copyright ? 2014 John Wiley & Sons, Ltd.

Copyright ? 2014 John Wiley & Sons, Ltd.

PMID:
24573805
[PubMed - in process]

http://www.ncbi.nlm.nih.gov/pubmed/24573805
 
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