Reactive oxygen species radiation

Jobling ME Mott JD, Finnegan MT et al. (2006) Isoform-specific activation of latent transforming growth factor beta (LTGF-beta) by reactive oxygen species. Radiat Res 166 ... 

The importance of superoxide-mediated damage to cancer cells was also demonstrated in the experiments with overexpressed mitochondrial MnSOD. Hirose et al. [186] showed that the overexpression of mitochondrial MnSOD enhanced the survival of human melanoma cells exposed to cytokines IL-1 and TNF-a, anticancer antibiotics doxorubicin and mitomycin C, and y-irradiation. Similarly, Motoori et al. [187] found that overexpression of MnSOD reduced the levels of reactive oxygen species in mitochondria, the intracellular production of 4-hydroxy-2-nonenal, and prevented radiation-induced cell death in human hepatocellular... 

Babu, T.S. et al.. Similar stress responses are elicited by copper and ultraviolet radiation in the aquatic plant Lemna gibba implication of reactive oxygen species as common signals, Plant Cell Physiol, 44, 1320, 2003. 

Magda, D. et al. (2001) Redox cycling by motexafin gadolinium enhances cellular response to ionizing radiation by forming reactive oxygen species, Int. J. Radiat. Oncol. Biol. 51, 1025-1036. 

The same amidation reaction was employed by Joshi et al. to covalently functionalize MWNTs with a specific peptide sequence, which specifically binds to the heptameric receptor-binding subunit of anthrax toxin.33 These nanotube-peptide conjugates were found to selectively destroy anthrax toxin with the reactive oxygen species generated by the nanotubes upon near-IR radiation.33... 

Hydroxylation and oxidation by the reactive oxygen species and the ionized radiations. 

The other amino acid residue present in proteins that is susceptible to oxidation is the indole moiety of tryptophan (Fig. 11). The reducing potential of tryptophan is considerably less than that of cysteine and methionine, so oxidation of tryptophanyl residues usually does not occur until all exposed thiol residues are oxidized. Also, the spontaneous oxidation of tryptophanyl residues in proteins is much less probable than that of cysteinyl and methionyl residues. Tryptophan residues are the only chromophoric moieties in proteins which can be photooxi-dized to tryptophanyl radicals by solar UV radiation, even by wavelengths as long as 305 nm (B12). Tryptophanyl residues readily react with all reactive oxygen species, hypochlorite, peroxynitrite, and chloramines. Oxidative modifications of other amino acid residues require use of strong oxidants, which eventually are produced in the cells. Detailed mechanisms of action of these oxidants is described in subsequent sections of this chapter. 

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