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Effects of oxidative and nitrosative stress on Tetrahymena pyriformis glyceraldehydes-3-phosphate dehydrogenase

Autor Fourrat, Latifa; Iddar, Abdelghani; Valverde, Federico ; Serrano, Aurelio ; Soukri, Abdelaziz
Palabras clave Central carbon metabolism
oxidative reagents
protein modification
regulatory network
Fecha de publicación 2-jul-2007
ResumenPrevious reports showed that hydrogen peroxide and the NO-generating reagent sodium nitroprusside (SNP)-modulated enzymatic activity of animal glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC These modifications are suggested to have a physiological regulatory role. To gain further insight into this regulatory process the model ciliated protozoan Tetrahymena pyriformis was chosen. Both reagents inhibited growth of T. pyriformis cultures and produced a specific increase of GAPDH protein but only NO seemed to reduce GAPDH activity in cell-free extracts. Both specific activity and pI were found to be altered in the in vivo NO-treated purified enzyme, but no effect was detected by the in vivo H2O2 treatment. Analytical chromatofocusing showed a single basic isoform (pI 8.8) in enzyme preparations from control and H2O2-treated cells. In contrast to this, three more acidic isoforms (pIs, 8.6, 8.0 and 7.3) were resolved in purified fractions from SNP-treated cells, suggesting post-translational modification of the enzyme by NO. Nevertheless, a decrease of GAPDH activity by H2O2 and NO, mainly due to a decrease in its Vmax without apparent change in substrate affinity, was observed in vitro in the whole enzyme population. The increase of GAPDH protein level found in vivo suggests a cell response in order to compensate for the inhibitory effect on activity observed in the purified enzyme. This is the first report of NO- and H2O2-dependent effects on GAPDH of T. pyriformis, and identifies this key protein of central carbon metabolism as a physiological target of oxidative and nitrosative stress in this ciliated protozoan.
Descripción Journal of Eukaryotic Microbiology,54(4) p.338-346
Versión del editorhttp://dx.doi.org/10.1111/j.1550-7408.2007.00275.x
URI http://hdl.handle.net/10261/9405
ISSN1550-7408 (Online)
1066-5234 (Print)
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