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Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients

PloS one, 2010-07, Vol.5 (7), p.e11552-e11552 [Peer Reviewed Journal]

COPYRIGHT 2010 Public Library of Science ;COPYRIGHT 2010 Public Library of Science ;2010 Forsberg et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;Forsberg et al. 2010 ;ISSN: 1932-6203 ;EISSN: 1932-6203 ;DOI: 10.1371/journal.pone.0011552 ;PMID: 20644736

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Title:
Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients
Author: Forsberg, Karin ; Jonsson, P Andreas ; Andersen, Peter M ; Bergemalm, Daniel ; Graffmo, Karin S ; Hultdin, Magnus ; Jacobsson, Johan ; Rosquist, Roland ; Marklund, Stefan L ; Brännström, Thomas
Westermark, Per
Subjects: Aged ; Aged, 80 and over ; Amyotrophic lateral sclerosis ; Amyotrophic Lateral Sclerosis - metabolism ; Animals ; Antibodies ; Antibodies - immunology ; Atrophy ; Blotting, Western ; Chickens ; Confocal microscopy ; Deoxyribonucleic acid ; DNA ; DNA-Binding Proteins - metabolism ; Endoplasmic reticulum ; Enzyme-Linked Immunosorbent Assay ; Enzymes ; Female ; Humans ; Immunohistochemistry ; Inclusion Bodies - immunology ; Inclusion Bodies - metabolism ; Inclusions ; Lysosomes ; Male ; Markers ; Medical research ; MEDICIN ; MEDICINE ; Medicine, Experimental ; Microscopy ; Microscopy, Fluorescence ; Middle Aged ; Mitochondria ; Motor neurons ; Mutation ; Neurological Disorders ; Neurological Disorders/Movement Disorders ; Neurological Disorders/Spinal Disorders ; Neuroscience ; Neuroscience/Neurobiology of Disease and Regeneration ; Pathogenesis ; Patients ; Peptides ; Phagosomes ; Protein binding ; Rabbits ; Rodents ; Spinal and bulbar muscular atrophy ; Spinal cord ; Spinal Cord - metabolism ; Superoxide ; Superoxide dismutase ; Superoxide Dismutase - genetics ; Superoxide Dismutase - immunology ; Superoxide Dismutase - metabolism ; Superoxide Dismutase-1 ; Superoxides ; Ubiquitin ; Ubiquitin - metabolism ; Viral antibodies
Is Part Of: PloS one, 2010-07, Vol.5 (7), p.e11552-e11552
Description: Mutations in CuZn-superoxide dismutase (SOD1) cause amyotrophic lateral sclerosis (ALS) and are found in 6% of ALS patients. Non-native and aggregation-prone forms of mutant SOD1s are thought to trigger the disease. Two sets of novel antibodies, raised in rabbits and chicken, against peptides spaced along the human SOD1 sequence, were by enzyme-linked immunosorbent assay and an immunocapture method shown to be specific for denatured SOD1. These were used to examine SOD1 in spinal cords of ALS patients lacking mutations in the enzyme. Small granular SOD1-immunoreactive inclusions were found in spinal motoneurons of all 37 sporadic and familial ALS patients studied, but only sparsely in 3 of 28 neurodegenerative and 2 of 19 non-neurological control patients. The granular inclusions were by confocal microscopy found to partly colocalize with markers for lysosomes but not with inclusions containing TAR DNA binding protein-43, ubiquitin or markers for endoplasmic reticulum, autophagosomes or mitochondria. Granular inclusions were also found in carriers of SOD1 mutations and in spinobulbar muscular atrophy (SBMA) patients and they were the major type of inclusion detected in ALS patients homozygous for the wild type-like D90A mutation. The findings suggest that SOD1 may be involved in ALS pathogenesis in patients lacking mutations in the enzyme.
Publisher: United States: Public Library of Science
Language: English
Identifier: ISSN: 1932-6203
EISSN: 1932-6203
DOI: 10.1371/journal.pone.0011552
PMID: 20644736
Source: Geneva Foundation Free Medical Journals at publisher websites
PLoS
MEDLINE
PubMed Central
SWEPUB Freely available online
ProQuest Central
DOAJ Directory of Open Access Journals

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Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients

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