
Perspective on SOD1 mediated toxicity in Amyotrophic Lateral Sclerosis
Author(s) -
Smriti Sangwan,
David Eisenberg
Publication year - 2016
Publication title -
postępy biochemii
Language(s) - English
Resource type - Journals
ISSN - 0032-5422
DOI - 10.18388/pb.2016_37
Subject(s) - amyotrophic lateral sclerosis , sod1 , toxicity , perspective (graphical) , neuroscience , medicine , biology , disease , computer science , artificial intelligence
A myotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by the progressive degeneration of spinal motor neurons. Although mutations in dozens of proteins have been associated with ALS, the enzyme, superoxide dismutase 1 (SOD1) was the first protein identified with the development of ALS and accounts for ~20% of familial cases. In experimental animals and patient samples, mutant SOD1 is found in cytoplasmic deposits implicating SOD1 aggregates as the toxic entities. Here we discuss the various biochemical and structure-based hypotheses proposed for mutant SOD1-associated ALS. Although much remains to be discovered about the molecular mechanism of SOD1 mediated toxicity, these hypotheses offer new avenues for therapeutic development.