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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Glutathione modifies the oxidation products of 2 `-deoxyguanosine by singlet molecular oxygen

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Peres, Patricia S. [1] ; Valerio, Andressa [1] ; Cadena, Silvia M. S. C. [1] ; Winnischofer, Sheila M. B. [1] ; Scalfo, Alexsandra C. [2] ; Di Mascio, Paolo [2] ; Martinez, Glaucia R. [1]
Total Authors: 7
[1] Univ Fed Parana, Setor Ciencias Biol, Dept Bioquim & Biol Mol, Lab Oxidacoes Biol, BR-80060000 Curitiba, PR - Brazil
[2] Univ Sao Paulo, Inst Quim, Dept Bioquim, BR-01498 Sao Paulo, PR - Brazil
Total Affiliations: 2
Document type: Journal article
Source: Archives of Biochemistry and Biophysics; v. 586, p. 33-44, NOV 15 2015.
Web of Science Citations: 4

The oxidation of the free nucleoside 2'-deoxyguanosine (dGuo) by singlet molecular oxygen (O-1(2)) has been studied over the three last decades due to the major role of DNA oxidation products in process such as ageing, mutation and carcinogenesis. In the present work we investigated the dGuo oxidation by O-1(2) in the presence of the important low molecular antioxidant, glutathione, in its reduced (GSH) and oxidized (GSSG) forms. There were applied different conditions of concentration, pH, time of incubation, and the use of a {[}O-18]-labeled thermolabile endoperoxide naphthalene derivative as a source of {[}O-18]labeled O-1(2). Data was obtained through high performance liquid chromatography (HPLC) and HPLC coupled to micrOTOF Q-II analysis of the main oxidation products: the diastereomers of spiroiminodihydantoin-2'-deoxyribonucleosides (dSp) and 8-oxo-7,8-dihydro-2'-deoxyguanosine (8-oxodGuo). An intriguing result was that 8-oxodGuo levels increased by 100 fold when dGuo was oxidized by O-1(2) in the presence of GSH and by 2 fold in the presence of GSSG, while dSp levels dropped to zero for both conditions. All data from dGuo, 8-oxodGuo and dSp quantification together with the analysis of residual GSH/GSSG content in each sample strongly suggest that glutathione modifies the mechanism of dGuo oxidation by O-1(2) by disfavoring the pathway of dSp formation. (C) 2015 Published by Elsevier Inc. (AU)

FAPESP's process: 13/07937-8 - Redoxome - Redox Processes in Biomedicine
Grantee:Ohara Augusto
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 12/12663-1 - Singlet molecular oxygen and peroxides in chemical biology
Grantee:Paolo Di Mascio
Support type: Research Projects - Thematic Grants