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- Title
Modulation of Nitrosative Stress via Glutathione-Dependent Formaldehyde Dehydrogenase and 5-Nitrosoglutathione Reductase.
- Authors
Chuian-Fu Ken; Chih-Yu Huang; Wen, Lisa; Huang, Jenq-Kuen; Chi-Tsai Lin
- Abstract
Glutathione-dependent formaldehyde dehydrogenase (GFD) from Taiwanofungus camphorata plays important roles in formaldehyde detoxification and antioxidation. The enzyme is bifunctional. In addition to the GFD activity, it also functions as an effective S-nitrosoglutathione reductase (GSNOR) against nitrosative stress. We investigated the modulation of HEK (human embryonic kidney) 293T cells under nitrosative stress by transfecting a codon optimized GFD cDNA from Taiwanofungus camphorata (Tc-GFD-O) to these cells. The parental and transfected HEK 293T cells were then subjected to S-nitrosoglutathione treatment to induce nitrosative stress. The results showed that in Tc-GFD-O-transfected 293T cells, the expression and activity of GFD increased. Additionally, these cells under the nitrosative stress induced by S-nitrosoglutathione showed both higher viability and less apoptosis than the parental 293T cells. This finding suggests that the Tc-GFD-0 in HEK 293T cells may provide a protective function under nitrosative stress.
- Subjects
GLUTATHIONE; FORMALDEHYDE dehydrogenase; GLUTATHIONE reductase; NITRIC-oxide synthases; BASIDIOMYCOTA; PHYSIOLOGICAL stress; FUNGI
- Publication
International Journal of Molecular Sciences, 2014, Vol 15, Issue 8, p14166
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms150814166