Presença e atividade da proteína quiescina sulfidril oxidase em sorofetal e neonatal
AUTOR(ES)
João Vitor Pelizzari
DATA DE PUBLICAÇÃO
2005
RESUMO
Production of reactive oxygen and nitrogen species during embryonic and fetal development has been demonstrated in the last few years. Among these species, superoxide radical anion, hydrogen peroxide and nitric oxide radical, enzymatically produced, have been considered. Their tightly controlled production provides the adequate concentrations necessary for the developmental process. In addition, the antioxidant system consists of reducing biomolecules and enzymes, particularly those belonging to the thioredoxin superfamily, which are essential to the thiol-disulfide equilibrium-dependent redox state. Indeed, knockout of the thioredoxins-1 and -2 genes are lethal for murine embryos. Quiescin sulfhydryl oxidase (QSOX) is a thiol oxidase, whose function has not been established, that catalyzes disulfide bridges and hydrogen peroxide formation. Its expression in some fetal and embryonic tissues has been reported. In this project, we analyzed QSOX presence and activity in bovine fetal and neonatal sera. A high level of QSOX was found in fetal serum, which decreases with age. QSOX identity was unequivocally characterized by Western blotting. Sulfhydryl oxidase activity, determined by hydrogen peroxide production rate, correlated with its expression levels. These data suggest a possible QSOX-dependent redox role in the modulation of developmental programs.
ASSUNTO(S)
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