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Homeostasis of the ER redox state subsequent to proteasome inhibition.
Oku, Yuki; Kariya, Masahiro; Fujimura, Takaaki; Hoseki, Jun; Sakai, Yasuyoshi.
Afiliação
  • Oku Y; Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, 606-8502, Japan.
  • Kariya M; Graduate School of Advanced Integrated Studies in Human Survivability, Kyoto University, Kyoto, 606-8306, Japan.
  • Fujimura T; Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, 606-8502, Japan.
  • Hoseki J; Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, 606-8502, Japan.
  • Sakai Y; Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, 606-8502, Japan. hoseki.jun@kuas.ac.jp.
Sci Rep ; 11(1): 8655, 2021 04 21.
Article em En | MEDLINE | ID: mdl-33883613
Endoplasmic reticulum (ER) maintains within, an oxidative redox state suitable for disulfide bond formation. We monitored the ER redox dynamics subsequent to proteasome inhibition using an ER redox probe ERroGFP S4. Proteasomal inhibition initially led to oxidation of the ER, but gradually the normal redox state was recovered that further led to a reductive state. These events were found to be concomitant with the increase in the both oxidized and reduced glutathione in the microsomal fraction, with a decrease of total intracellular glutathione. The ER reduction was suppressed by pretreatment of a glutathione synthesis inhibitor or by knockdown of ATF4, which induces glutathione-related genes. These results suggested cellular adaptation of ER redox homeostasis: (1) inhibition of proteasome led to accumulation of misfolded proteins and oxidative state in the ER, and (2) the oxidative ER was then reduced by ATF4 activation, followed by influx of glutathione into the ER.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Oxirredução / Complexo de Endopeptidases do Proteassoma / Retículo Endoplasmático / Homeostase Limite: Humans Idioma: En Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Oxirredução / Complexo de Endopeptidases do Proteassoma / Retículo Endoplasmático / Homeostase Limite: Humans Idioma: En Ano de publicação: 2021 Tipo de documento: Article