Document Detail


Cigarette smoke induces nucleic-acid oxidation in lung fibroblasts.
MedLine Citation:
PMID:  20008282     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Oxidative stress is widely proposed as a pathogenic mechanism for chronic obstructive pulmonary disease (COPD), but the molecular pathway connecting oxidative damage to tissue destruction remains to be fully defined. We suggest that reactive oxygen species (ROS) oxidatively damage nucleic acids, and this effect requires multiple repair mechanisms, particularly base excision pathway components 8-oxoguanine-DNA glycosylase (OGG1), endonuclease III homologue 1 (NTH1), and single-strand-selective monofunctional uracil-DNA glycosylase 1 (SMUG1), as well as the nucleic acid-binding protein, Y-box binding protein 1 (YB1). This study was therefore designed to define the levels of nucleic-acid oxidation and expression of genes involved in the repair of COPD and in corresponding models of this disease. We found significant oxidation of nucleic acids localized to alveolar lung fibroblasts, increased levels of OGG1 mRNA expression, and decreased concentrations of NTH1, SMUG1, and YB1 mRNA in lung samples from subjects with very severe COPD compared with little or no COPD. Mice exposed to cigarette smoke exhibited a time-dependent accumulation of nucleic-acid oxidation in alveolar fibroblasts, which was associated with an increase in OGG1 and YB1 mRNA concentrations. Similarly, human lung fibroblasts exposed to cigarette smoke extract exhibited ROS-dependent nucleic-acid oxidation. The short interfering RNA (siRNA)-dependent knockdown of OGG1 and YB1 expression increased nucleic-acid oxidation at the basal state and after exposure to cigarette smoke. Together, our results demonstrate ROS-dependent, cigarette smoke-induced nucleic-acid oxidation in alveolar fibroblasts, which may play a role in the pathogenesis of emphysema.
Authors:
Gaetan Deslee; Tracy L Adair-Kirk; Tomoko Betsuyaku; Jason C Woods; Carla H Moore; David S Gierada; Susan H Conradi; Jeffrey J Atkinson; Holly M Toennies; John T Battaile; Dale K Kobayashi; G Alexander Patterson; Michael J Holtzman; Richard A Pierce
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2009-12-11
Journal Detail:
Title:  American journal of respiratory cell and molecular biology     Volume:  43     ISSN:  1535-4989     ISO Abbreviation:  Am. J. Respir. Cell Mol. Biol.     Publication Date:  2010 Nov 
Date Detail:
Created Date:  2010-10-25     Completed Date:  2010-11-10     Revised Date:  2011-11-01    
Medline Journal Info:
Nlm Unique ID:  8917225     Medline TA:  Am J Respir Cell Mol Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  576-84     Citation Subset:  IM    
Affiliation:
Division of Pulmonary and Critical Care Medicine, School of Medicine, Washington University, St. Louis, Missouri 63110, USA.
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MeSH Terms
Descriptor/Qualifier:
Adult
Aged
Animals
Apoptosis
DNA Glycosylases / antagonists & inhibitors,  genetics,  metabolism
DNA-Binding Proteins / antagonists & inhibitors,  genetics,  metabolism
Deoxyribonuclease (Pyrimidine Dimer) / metabolism
Down-Regulation
Emphysema / enzymology,  genetics,  pathology
Female
Fibroblasts / enzymology,  metabolism*,  pathology*
Humans
Lung
Male
Mice
Mice, Inbred C57BL
Middle Aged
Nuclear Proteins / antagonists & inhibitors,  genetics,  metabolism
Nucleic Acids / metabolism*
Oxidation-Reduction
Pulmonary Alveoli / enzymology,  pathology
RNA, Messenger / genetics,  metabolism
Reactive Oxygen Species / metabolism
Smoking / adverse effects*
Uracil-DNA Glycosidase / metabolism
Grant Support
ID/Acronym/Agency:
P50HL084922/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/DNA-Binding Proteins; 0/Nuclear Proteins; 0/Nucleic Acids; 0/RNA, Messenger; 0/Reactive Oxygen Species; 0/YBX1 protein, human; EC 3.1.25.1/Deoxyribonuclease (Pyrimidine Dimer); EC 3.1.25.1/NTHL1 protein, human; EC 3.2.2.-/DNA Glycosylases; EC 3.2.2.-/SMUG1 protein, human; EC 3.2.2.-/Uracil-DNA Glycosidase; EC 3.2.2.-/oxoguanine glycosylase 1, human

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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