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Inactivation of genes encoding superoxide dismutase modifies yeast response to S-nitrosoglutathione-induced stress

机译:编码超氧化物歧化酶的基因的失活修饰了酵母对S-亚硝基谷胱甘肽诱导的应激的反应

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摘要

Antioxidant enzymes can modify cell response to nitrosative stress induced, for example, by nitric oxide or compounds decomposing with its formation. Therefore, we investigated the effects of S-nitrosoglutathione (GSNO) on cell survival, activity of antioxidant enzymes, and concentrations of reduced and oxidized glutathione in parental and isogenic strains defective in Cu,Zn- or Mn-superoxide dismutases (Cu,Zn-SOD and Mn-SOD, respectively), or in both of them. Stress was induced by incubation of the yeast with 1-20 mM GSNO. The strains used demonstrated different sensitivity to GSNO. A Cu,Zn-SOD-defective strain survived the stress better than the parental strain, while the double mutant was the most sensitive to GSNO. The ·NO-donor at low concentrations (1-5 mM) increased SOD activity, but its high concentrations (10 and 20 mM) decreased it. The activity of catalase in all strains was enhanced by GSNO. Inhibition of protein synthesis by cycloheximide did not prevent the activation of SOD, but it prevented the activation of catalase. These facts suggest that SOD was activated at a posttranslational level and catalase activity was enhanced via de novo synthesis. A GSNO-induced increase in oxidized glutathione level in the studied yeast strains might account for cell killing by GSNO due to the development of oxidativeitrosative stress. [PUBLICATION ABSTRACT]
机译:抗氧化酶可以改变细胞对亚硝基化应激的反应,例如,由一氧化氮或化合物分解形成的亚硝化应激。因此,我们研究了S-亚硝基谷胱甘肽(GSNO)对铜,锌或锰超氧化物歧化酶(Cu,Zn--)缺陷的亲本和同基因菌株中细胞存活,抗氧化酶活性以及还原型和氧化型谷胱甘肽浓度的影响。分别是SOD和Mn-SOD),或两者都包含。通过将酵母与1-20 mM GSNO孵育来诱导应激。使用的菌株对GSNO表现出不同的敏感性。 Cu,Zn-SOD缺陷菌株比亲本菌株更好地承受了压力,而双突变体对GSNO最敏感。低浓度(1-5 mM)的·NO供体增加了SOD活性,但高浓度(10和20 mM)降低了SOD活性。 GSNO提高了所有菌株中过氧化氢酶的活性。环己酰亚胺对蛋白质合成的抑制不会阻止SOD的激活,但会阻止过氧化氢酶的激活。这些事实表明,SOD在翻译后水平被激活,过氧化氢酶活性通过从头合成得到增强。在研究的酵母菌株中,GSNO诱导的氧化型谷胱甘肽水平升高可能是由于GSNO氧化/亚硝化应激的发展而杀死细胞的原因。 [出版物摘要]

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