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SOD1 in Amyotrophic Lateral Sclerosis: "Ambivalent" Behavior Connected to the Disease.

Abstract：

:In 1993, Rosen and collaborators discovered that the gene encoding SOD1 has mutations in amyotrophic lateral sclerosis (ALS) patients; moreover, these mutations are found in the exon regions, suggesting that their toxic effects are the consequence of protein dysfunction with an increase of oxidative stress. While a clear genetic picture has been delineated, a more complex scenario has been ascribed to the SOD1 protein. On the one hand, some evidence sustains the hypothesis of an additionally toxic role for wild-type SOD1 (WT-SOD1) in the pathogenesis of sporadic ALS. On the other hand, our group identified a discrepancy among WT-SOD1 protein expression levels and mRNA in ALS sporadic patients, thus providing the hypothesis of a re-localization of the “missing” SOD1 in a different sub-cellular compartment, i.e., nucleus, or an aggregation/precipitation in the insoluble fraction. Moreover, our data also indicate an association between longer disease duration and higher amounts of soluble SOD1 within the nucleus, suggesting a possible defensive role of the protein in this compartment. Starting from this evidence, in this review we will attempt to resolve the “ambivalent” behavior of SOD1 in ALS disease and we will try to classify sporadic ALS patients according to a novel biological signature, i.e., SOD localization.

journal_name

Int J Mol Sci

journal_title

International journal of molecular sciences

authors

Pansarasa O,Bordoni M,Diamanti L,Sproviero D,Gagliardi S,Cereda C

doi

10.3390/ijms19051345

subject

Has Abstract

pub_date

2018-05-03 00:00:00

issue

5

issn

1422-0067

pii

ijms19051345

journal_volume

19

pub_type

杂志文章,评审

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