Metallothionein-I protects against pathological aggregation of SOD1 associated with amyotrophic lateral sclerosis
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- TOKUDA Eiichi
- School of Pharmacy, Nihon University
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- KEIMA Maiko
- School of Pharmacy, Nihon University
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- IKEDA Chiako
- School of Pharmacy, Nihon University
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- ONO Shin-ichi
- School of Pharmacy, Nihon University Devison of Neurology, Akiru Medical Center
Bibliographic Information
- Other Title
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- 神経変性疾患ALSに対するメタロチオネインの防御作用: SOD1タンパク質の凝集化抑制
Abstract
<p>Amyotrophic lateral sclerosis (ALS) is a motor neuron disease with muscle atrophy and respiratory failure. Superoxide dismutase-1 (SOD1) is deposited as aggregates in motor neurons and glial cells of ALS. While natively folded SOD1 binds Cu/Zn that confer structural stability to the protein, SOD1 aggregates do not contain these metals. Thus, dissociation of Cu/Zn ions from SOD1 is required for its aggregation. Metallothionein-I (MT-I) is a Cu/Zn binding protein involved in the homeostasis of these ions. We hypothesize that MT-I has the potential to inhibit pathological conversion of SOD1 into aggregation. In this symposium, we will talk about that MT-I inhibits SOD1 aggregation at molecular and cellular levels.</p>
Journal
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- Annual Meeting of the Japanese Society of Toxicology
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Annual Meeting of the Japanese Society of Toxicology 48.1 (0), S25-3-, 2021
The Japanese Society of Toxicology
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Details 詳細情報について
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- CRID
- 1390007536268381696
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- NII Article ID
- 130008073891
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- Text Lang
- ja
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- Data Source
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- JaLC
- CiNii Articles
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- Abstract License Flag
- Disallowed