Cited by 419Amyotrophic Lateral Sclerosis ResearchAlzheimer's disease research and treatmentsHereditary Neurological Disorders

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Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis

Urushitani, Makoto, Sik, Attila, Sakurai, Takashi, Nukina, Nobuyuki, Takahashi, Ryosuke, Julien, Jean-Pierre·2006·Nature Neuroscience

DOI 10.1038/nn1603

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Abstract

Here we report that chromogranins, components of neurosecretory vesicles, interact with mutant forms of superoxide dismutase (SOD1) that are linked to amyotrophic lateral sclerosis (ALS), but not with wild-type SOD1. This interaction was confirmed by yeast two-hybrid screen and by co-immunoprecipitation assays using either lysates from Neuro2a cells coexpressing chromogranins and SOD1 mutants or lysates from spinal cord of ALS mice. Confocal and immunoelectron microscopy revealed a partial colocalization of mutant SOD1 with chromogranins in spinal cord of ALS mice. Mutant SOD1 was also found in immuno-isolated trans-Golgi network and in microsome preparations, suggesting that it can be secreted. Indeed we report evidence that chromogranins may act as chaperone-like proteins to promote secretion of SOD1 mutants. From these results, and our finding that extracellular mutant SOD1 can trigger microgliosis and neuronal death, we propose a new ALS pathogenic model based on the toxicity of secreted SOD1 mutants.

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Authors: Urushitani, M., Sik, A., Sakurai, T., Nukina, N., Takahashi, R., & Julien, J.-P.
Affiliations: Centre hospitalier de l'Université Laval (CA)
Université Laval (CA)
RIKEN Center for Brain Science (JP)
Corresponding author: Julien, Jean-Pierre
ORCID: Urushitani, Makoto
Sik, Attila
Sakurai, Takashi
Nukina, Nobuyuki
Julien, Jean-Pierre
Venue: Nature Neuroscience
Publisher: Springer Science and Business Media LLC
Published: 2005-12-20
Volume: 9
Issue: 1
Pages: 108-118
ISSN: 1097-6256 (ISSN-L)
1546-1726
DOI: 10.1038/nn1603
OpenAlex: W2034651824
Semantic Scholar: 6da103b1c172cd68887144303844e02b0c5552ff
Cited by: 419
References: 47
Citations by year: 2026: 4 · 2025: 8 · 2024: 12 · 2023: 10 · 2022: 8 · 2021: 9 · 2020: 14 · 2019: 10 · 2018: 13 · 2017: 16 · 2016: 20 · 2015: 25 · 2014: 23 · 2013: 35 · 2012: 28
FWCI: 15.58
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Neuroscience (publishedVersion)
PubMed (publishedVersion)
University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
Topics: Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
Keywords: chromogranin, superoxide dismutase 1, SOD1 mutations, amyotrophic lateral sclerosis, protein secretion, neurosecretory granules, chaperone-like protein, trans-Golgi network, microglial activation, neuronal cell death, ALS pathogenesis, spinal cord
MeSH terms: Superoxide Dismutase-1, Amyotrophic Lateral Sclerosis, Animals, Astrocytes, Cells, Cultured, Chlorocebus aethiops, Chromogranins, Fluorescent Antibody Technique, Gliosis, Humans, Interneurons, Mice, Transgenic, Microsomes, Motor Neurons, Mutation, Plasmids, Spinal Cord, Subcellular Fractions, Superoxide Dismutase, Blotting, Western, Microscopy, Immunoelectron, 3T3 Cells, Protein Folding, Molecular Chaperones, COS Cells, Immunoprecipitation, Mice, Chromogranin A, Proteasome Inhibitors

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Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis

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