Journal
OXIDATIVE/NITROSATIVE STRESS AND DISEASE
Volume 1203, Issue -, Pages 23-28Publisher
BLACKWELL PUBLISHING
DOI: 10.1111/j.1749-6632.2010.05553.x
Keywords
S-glutathionylation; glutaredoxin; Fas; apoptosis; fibrosis; lung
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Funding
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL085464, R03HL095404, R01HL060014, R01HL079331] Funding Source: NIH RePORTER
- NHLBI NIH HHS [R01 HL060014-13, R03 HL095404-02, R01 HL079331-07, R01 HL085464, R01 HL060014, R03 HL095404, R01 HL079331, R01 HL085464-04] Funding Source: Medline
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Tissue fibrosis is believed to be a manifestation of dysregulated repair following injury, in association with impaired reepithelialization, and aberrant myofibroblast activation and proliferation. Numerous pathways have been linked to the pathogenesis of fibrotic lung disease, including the death receptor Fas, which contributes to apoptosis of lung epithelial cells. A redox imbalance also has been implicated in disease pathogenesis, although mechanistic details whereby oxidative changes intersect with profibrotic signaling pathways remain elusive. Oxidation of cysteines in proteins, such as S-glutathionylation (PSSG), is known to act as a regulatory event that affects protein function. This manuscript will discuss evidence that S-glutathionylation regulates death receptor induced apoptosis, and the potential implications for cysteine oxidations in the pathogenesis of in fibrotic lung disease.
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