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谷胱甘肽化使良性超氧化物歧化酶 1 变体转化为与肌萎缩侧索硬化症相关的毒性形式。

Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis.

机构信息

1] Illawarra Health and Medical Research Institute, Northfields Avenue, Wollongong NSW, Australia 2522 [2] School of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong NSW, Australia 2522.

出版信息

Sci Rep. 2013 Nov 20;3:3275. doi: 10.1038/srep03275.

Abstract

Dissociation of superoxide dismutase 1 dimers is enhanced by glutathionylation, although the dissociation constants reported to date are imprecise. We have quantified the discreet dissociation constants for wild-type superoxide dismutase 1 and six naturally occurring sequence variants, in their unmodified and glutathionylated forms, at the ratios expressed. Unmodified superoxide dismutase 1 variants that shared similar dissociation constants with SOD1(WT) had disproportionately increased dissociation constants when glutathionylated. This defines a key role for glutathionylation in superoxide dismutase 1 associated familial amyotrophic lateral sclerosis.

摘要

超氧化物歧化酶 1 二聚体的解离通过谷胱甘肽化增强,尽管迄今为止报道的解离常数并不精确。我们已经定量了野生型超氧化物歧化酶 1 和六种天然存在的序列变体在其表达比例的未修饰和谷胱甘肽化形式下的离散解离常数。具有与 SOD1(WT)相似解离常数的未修饰超氧化物歧化酶 1 变体在谷胱甘肽化时解离常数不成比例地增加。这定义了谷胱甘肽化在超氧化物歧化酶 1 相关家族性肌萎缩侧索硬化症中的关键作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/491c/3834562/8a02d5b11a50/srep03275-f1.jpg

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