Heat‐shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: clues to a possible strategy for treating ALS

A dominant mutation in the gene for copper‐zinc superoxide dismutase (SOD1) is the most frequent cause of the inherited form of amyotrophic lateral sclerosis. Mutant SOD1 provokes progressive degeneration of motor neurons by an unidentified acquired toxicity. Exploiting both affinity purification an...

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Veröffentlicht in:Journal of neurochemistry 2007-09, Vol.102 (5), p.1497-1505
Hauptverfasser: Yamashita, Hirofumi, Kawamata, Jun, Okawa, Katsuya, Kanki, Rie, Nakamizo, Tomoki, Hatayama, Takumi, Yamanaka, Koji, Takahashi, Ryosuke, Shimohama, Shun
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container_end_page 1505
container_issue 5
container_start_page 1497
container_title Journal of neurochemistry
container_volume 102
creator Yamashita, Hirofumi
Kawamata, Jun
Okawa, Katsuya
Kanki, Rie
Nakamizo, Tomoki
Hatayama, Takumi
Yamanaka, Koji
Takahashi, Ryosuke
Shimohama, Shun
description A dominant mutation in the gene for copper‐zinc superoxide dismutase (SOD1) is the most frequent cause of the inherited form of amyotrophic lateral sclerosis. Mutant SOD1 provokes progressive degeneration of motor neurons by an unidentified acquired toxicity. Exploiting both affinity purification and mass spectrometry, we identified a novel interaction between heat‐shock protein 105 (Hsp105) and mutant SOD1. We detected this interaction both in spinal cord extracts of mutant SOD1G93A transgenic mice and in cultured neuroblastoma cells. Expression of Hsp105, which is found in mouse motor neurons, was depressed in the spinal cords of SOD1G93A mice as disease progressed, while levels of expression of two other heat‐shock proteins, Hsp70 and Hsp27, were elevated. Moreover, Hsp105 suppressed the formation of mutant SOD1‐containing aggregates in cultured cells. These results suggest that techniques that raise levels of Hsp105 might be promising tools for alleviation of the mutant SOD1 toxicity.
doi_str_mv 10.1111/j.1471-4159.2007.04534.x
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Mutant SOD1 provokes progressive degeneration of motor neurons by an unidentified acquired toxicity. Exploiting both affinity purification and mass spectrometry, we identified a novel interaction between heat‐shock protein 105 (Hsp105) and mutant SOD1. We detected this interaction both in spinal cord extracts of mutant SOD1G93A transgenic mice and in cultured neuroblastoma cells. Expression of Hsp105, which is found in mouse motor neurons, was depressed in the spinal cords of SOD1G93A mice as disease progressed, while levels of expression of two other heat‐shock proteins, Hsp70 and Hsp27, were elevated. Moreover, Hsp105 suppressed the formation of mutant SOD1‐containing aggregates in cultured cells. 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Prion diseases ; Gene Expression Regulation - physiology ; Genetics ; heat‐shock protein 105 ; HSP110 Heat-Shock Proteins - metabolism ; Humans ; Immunoprecipitation ; Mass Spectrometry ; Medical sciences ; Mice ; Mice, Transgenic ; Motor Neurons - metabolism ; Mutation ; Mutation - physiology ; Neuroblastoma ; Neurology ; Proteins ; Spinal Cord - cytology ; Spinal Cord - metabolism ; Superoxide Dismutase - genetics ; Superoxide Dismutase - metabolism ; Transfection ; Tumors of the nervous system. 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Prion diseases</subject><subject>Gene Expression Regulation - physiology</subject><subject>Genetics</subject><subject>heat‐shock protein 105</subject><subject>HSP110 Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Mass Spectrometry</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>Mice, Transgenic</subject><subject>Motor Neurons - metabolism</subject><subject>Mutation</subject><subject>Mutation - physiology</subject><subject>Neuroblastoma</subject><subject>Neurology</subject><subject>Proteins</subject><subject>Spinal Cord - cytology</subject><subject>Spinal Cord - metabolism</subject><subject>Superoxide Dismutase - genetics</subject><subject>Superoxide Dismutase - metabolism</subject><subject>Transfection</subject><subject>Tumors of the nervous system. 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subjects Age Factors
Amyotrophic lateral sclerosis
Analysis of Variance
Animals
Biochemistry
Biological and medical sciences
Cell Line
Cellular biology
Cu/Zn superoxide dismutase (or superoxide dismutase 1)
Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases
Gene Expression Regulation - physiology
Genetics
heat‐shock protein 105
HSP110 Heat-Shock Proteins - metabolism
Humans
Immunoprecipitation
Mass Spectrometry
Medical sciences
Mice
Mice, Transgenic
Motor Neurons - metabolism
Mutation
Mutation - physiology
Neuroblastoma
Neurology
Proteins
Spinal Cord - cytology
Spinal Cord - metabolism
Superoxide Dismutase - genetics
Superoxide Dismutase - metabolism
Transfection
Tumors of the nervous system. Phacomatoses
title Heat‐shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: clues to a possible strategy for treating ALS
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