由氧化型谷胱甘肽增强的微粒体蛋白合成抑制剂的作用机制。
Mechanism of action of a microsomal inhibitor of protein synthesis potentiated by oxidized glutathione.
作者信息
Rupniak H T, Quincey R V
出版信息
Biochem J. 1973 Oct;136(2):335-42. doi: 10.1042/bj1360335.
Extracts of microsomal fractions cause an inhibition of protein synthesis that is most pronounced in the presence of 0.1mm-GSSG and 0.01mm-GTP, and is abolished by thiol or 0.4mm-GTP (Scornik et al., 1967). Fractionation of microsomal extracts showed that this inhibition of protein synthesis was caused by an enzyme, nucleoside diphosphate phosphohydrolase. Direct inhibition of protein synthesis on detergent-treated polyribosomes by 0.1mm-GSSG was observed under conditions of GTP limitation induced by omission of a GTP-regenerating system, or addition of a nucleoside triphosphate diphosphohydrolase. Thus GSSG potentiated the inhibition of protein synthesis caused by an enzyme that promoted removal of GTP. The inhibition was abolished by adding 4mm-2-mercaptoethanol or 0.4mm-GTP. Nucleoside diphosphate phosphohydrolase was thought also to act by promoting removal of GTP, thus causing an inhibition of protein synthesis that was potentiated by GSSG.
微粒体部分的提取物会导致蛋白质合成受到抑制，这种抑制在存在0.1mM - GSSG和0.01mM - GTP时最为明显，并且会被硫醇或0.4mM - GTP消除（斯科尔尼茨克等人，1967年）。微粒体提取物的分级分离表明，这种蛋白质合成的抑制是由一种酶，即核苷二磷酸磷酸水解酶引起的。在因省略GTP再生系统或添加核苷三磷酸二磷酸水解酶而导致GTP受限的条件下，观察到0.1mM - GSSG对经去污剂处理的多核糖体上的蛋白质合成有直接抑制作用。因此，GSSG增强了由促进GTP去除的酶所引起的蛋白质合成抑制。通过添加4mM - 2 - 巯基乙醇或0.4mM - GTP，这种抑制作用被消除。核苷二磷酸磷酸水解酶也被认为是通过促进GTP的去除来发挥作用的，从而导致蛋白质合成受到抑制，而GSSG会增强这种抑制作用。
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