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Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS
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Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS
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Journal Article
Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS
2010
Overview
Could similar changes in SOD1 underlie both familial and sporadic ALS? Here, Bosco
et al
. find that wild-type SOD1 from sporadic ALS tissues shows conformational changes similar to those seen in familial ALS and that aberrant wild-type SOD1 can be pathogenic, potentially as a result of the same SOD1-dependent mechanism seen in familial ALS.
Many mutations confer one or more toxic function(s) on copper/zinc superoxide dismutase 1 (SOD1) that impair motor neuron viability and cause familial amyotrophic lateral sclerosis (FALS). Using a conformation-specific antibody that detects misfolded SOD1 (C4F6), we found that oxidized wild-type SOD1 and mutant SOD1 share a conformational epitope that is not present in normal wild-type SOD1. In a subset of human sporadic ALS (SALS) cases, motor neurons in the lumbosacral spinal cord were markedly C4F6 immunoreactive, indicating that an aberrant wild-type SOD1 species was present. Recombinant, oxidized wild-type SOD1 and wild-type SOD1 immunopurified from SALS tissues inhibited kinesin-based fast axonal transport in a manner similar to that of FALS-linked mutant SOD1. Our findings suggest that wild-type SOD1 can be pathogenic in SALS and identify an SOD1-dependent pathogenic mechanism common to FALS and SALS.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Adult
/ Aged
/ Amyotrophic lateral sclerosis
/ Amyotrophic Lateral Sclerosis - etiology
/ Amyotrophic Lateral Sclerosis - genetics
/ Amyotrophic Lateral Sclerosis - pathology
/ Animal Genetics and Genomics
/ Biomedical and Life Sciences
/ Crystallography, X-Ray - methods
/ Female
/ Humans
/ Kinases
/ Male
/ Mutation
/ Neurons
/ Proteins
/ Proteostasis Deficiencies - complications
/ Proteostasis Deficiencies - genetics
/ Proteostasis Deficiencies - pathology
/ Superoxide Dismutase - chemistry
/ Superoxide Dismutase - genetics
