Proteomics study of N‐acetylcysteine response in H1N1‐infected cells by using mass spectrometry. (13th February 2014)
- Record Type:
- Journal Article
- Title:
- Proteomics study of N‐acetylcysteine response in H1N1‐infected cells by using mass spectrometry. (13th February 2014)
- Main Title:
- Proteomics study of N‐acetylcysteine response in H1N1‐infected cells by using mass spectrometry
- Authors:
- Wu, Hanzhi
Song, Wenjun
Gao, Xiang
Liu, Ning
Wang, Pui
Chen, Honglin
Cai, Zongwei - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="rcm6840-sec-0001" sec-type="section"> <title>RATIONALE</title> <p>The pathology of A/Puerto Rico/8/1934 (H1N1) infection associated with the interaction of virus and its host cells is not clear. <italic>N</italic>‐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.</p> </sec> <sec id="rcm6840-sec-0002" sec-type="section"> <title>METHODS</title> <p>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.</p> </sec> <sec id="rcm6840-sec-0003" sec-type="section"> <title>RESULTS</title> <p>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.</p> </sec> <sec id="rcm6840-sec-0004" sec-type="section"> <title>CONCLUSIONS</title> <p>The results indicated that NAC as a small‐molecule probe might effect the protein<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="rcm6840-sec-0001" sec-type="section"> <title>RATIONALE</title> <p>The pathology of A/Puerto Rico/8/1934 (H1N1) infection associated with the interaction of virus and its host cells is not clear. <italic>N</italic>‐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.</p> </sec> <sec id="rcm6840-sec-0002" sec-type="section"> <title>METHODS</title> <p>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.</p> </sec> <sec id="rcm6840-sec-0003" sec-type="section"> <title>RESULTS</title> <p>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.</p> </sec> <sec id="rcm6840-sec-0004" sec-type="section"> <title>CONCLUSIONS</title> <p>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 &amp; Sons, Ltd.</p> </sec> </abstract> … (more)
- Is Part Of:
- Rapid communications in mass spectrometry. Volume 28:Number 7(2014)
- Journal:
- Rapid communications in mass spectrometry
- Issue:
- Volume 28:Number 7(2014)
- Issue Display:
- Volume 28, Issue 7 (2014)
- Year:
- 2014
- Volume:
- 28
- Issue:
- 7
- Issue Sort Value:
- 2014-0028-0007-0000
- Page Start:
- 741
- Page End:
- 749
- Publication Date:
- 2014-02-13
- Subjects:
- Mass spectrometry -- Periodicals
543.65 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1002/rcm.6840 ↗
- Languages:
- English
- ISSNs:
- 0951-4198
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 7254.440000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3963.xml