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S-nitrosylation and S-glutathionylation of GAPDH: Similarities, differences, and relationships.
Medvedeva, M V; Kleimenov, S Yu; Samygina, V R; Muronetz, V I; Schmalhausen, E V.
Afiliación
  • Medvedeva MV; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 119991, Russia.
  • Kleimenov SY; Bach Institute of Biochemistry, Research Center of Biotechnology of Russian Academy of Sciences, Leninsky prospect 33, bld. 2, Moscow 119071, Russia; Koltzov Institute of Developmental Biology of Russian Academy of Sciences, ul. Vavilova 26, Moscow 119334, Russia.
  • Samygina VR; Shubnikov Institute of Crystallography of Federal Scientific Research Centre Crystallography and Photonics of Russian Academy of Sciences, Leninsky prospect 59, Moscow 119333, Russia.
  • Muronetz VI; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 119991, Russia; Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119991, Russia.
  • Schmalhausen EV; Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119991, Russia. Electronic address: shmal@belozersky.msu.ru.
Biochim Biophys Acta Gen Subj ; 1867(9): 130418, 2023 09.
Article en En | MEDLINE | ID: mdl-37355052
The aim of this work was to compare the effect of reversible post-translational modifications, S-nitrosylation and S-glutathionylation, on the properties of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and to reveal the mechanism of the relationship between these modifications. Comparison of S-nitrosylated and S-glutathionylated GAPDH showed that both modifications inactivate the enzyme and change its spatial structure, decreasing the thermal stability of the protein and increasing its sensitivity to trypsin cleavage. Both modifications are reversible in the presence of dithiothreitol, however, in the presence of reduced glutathione and glutaredoxin 1, the reactivation of S-glutathionylated GAPDH is much slower (10% in 2 h) compared to S-nitrosylated GAPDH (60% in 10 min). This suggests that S-glutathionylation is a much less reversible modification compared to S-nitrosylation. Incubation of HEK 293 T cells in the presence of H2O2 or with the NO donor diethylamine NONOate results in accumulation of sulfenated GAPDH (by data of Western blotting) and S-glutathionylated GAPDH (by data of immunoprecipitation with anti-GSH antibodies). Besides GAPDH, a protein of 45 kDa was found to be sulfenated and S-glutathionylated in the cells treated with H2O2 or NO. This protein was identified as beta-actin. The results of this study confirm the previously proposed hypothesis based on in vitro investigations, according to which S-nitrosylation of the catalytic cysteine residue (Cys152) of GAPDH with subsequent formation of cysteine sulfenic acid at Cys152 may promote its S-glutathionylation in the presence of cellular GSH. Presumably, the mechanism may be valid in the case of beta-actin.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cisteína / Peróxido de Hidrógeno Límite: Humans Idioma: En Revista: Biochim Biophys Acta Gen Subj Año: 2023 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Países Bajos
Texto completo
Añadir a Mi BVS
Imprimir
XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cisteína / Peróxido de Hidrógeno Límite: Humans Idioma: En Revista: Biochim Biophys Acta Gen Subj Año: 2023 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Países Bajos