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Heme oxygenase‐1 induction by endogenous nitric oxide: influence of intracellular glutathione
Author(s) -
André Muriel,
Felley-Bosco Emanuela
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00576-3
Subject(s) - glutathione , heme oxygenase , buthionine sulfoximine , nitric oxide , nitric oxide synthase , intracellular , chemistry , endogeny , heme , oxidative stress , biochemistry , arginine , enzyme , amino acid , organic chemistry
To investigate the influence of glutathione (GSH) on cellular effects of nitric oxide (NO) formation, human colon adenocarcinoma cells were transfected with a vector allowing controlled expression of inducible nitric oxide synthase (iNOS). Protein levels of oxidative stress‐sensitive heme oxygenase‐1 (HO‐1) were analyzed in the presence or absence of GSH depletion using L ‐buthionine‐[ S , R ]‐sulfoximine and iNOS induction. While no effect was observed in the presence of iNOS activity alone, a synergistic effect on HO‐1 expression was observed in the presence of iNOS expression and GSH depletion. This effect was prevented by addition of N ‐methyl‐ L ‐arginine. Therefore, targeting of endogenous NO may be modulated by intracellular GSH.

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