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

Yamashita H; Kawamata J; Okawa K; Kanki R; Nakamizo T; Hatayama T; Yamanaka K; Takahashi R; Shimohama S

doi:10.1111/j.1471-4159.2007.04534.x

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

Affiliations

1. Department of Neurology, Kyoto University Graduate School of Medicine, Kyoto, JapanYamanaka Research Unit, RIKEN Brain Science Institute, Wako, JapanHorizontal Medical Research Organization, Kyoto University Graduate School of Medicine, Kyoto, JapanDepartment of Biochemistry, Kyoto Pharmaceutical University, Kyoto, JapanDepartment of Neurology, Sapporo Medical University School of Medicine, Sapporo, Japan.
Authors
Yamashita H¹
Kawamata J¹
Okawa K¹
Kanki R¹
Nakamizo T¹
Hatayama T¹
Yamanaka K¹
Takahashi R¹
Shimohama S¹
(9 authors)

ORCIDs linked to this article

Journal of Neurochemistry, 30 Mar 2007, 102(5):1497-1505
https://doi.org/10.1111/j.1471-4159.2007.04534.x PMID: 17403032

Abstract

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 SOD1(G93A) transgenic mice and in cultured neuroblastoma cells. Expression of Hsp105, which is found in mouse motor neurons, was depressed in the spinal cords of SOD1(G93A) 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.

Full text links

Read article at publisher's site: https://doi.org/10.1111/j.1471-4159.2007.04534.x

Read article for free, from open access legal sources, via Unpaywall: https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/j.1471-4159.2007.04534.x

References

Articles referenced by this article (47)

Autosomal recessive adult-onset amyotrophic lateral sclerosis associated with homozygosity for Asp90Ala CuZn-superoxide dismutase mutation. A clinical and genealogical study of 36 patients.
Andersen PM, Forsgren L, Binzer M, Nilsson P, Ala-Hurula V, Keranen ML, Bergmark L, Saarinen A, Haltia T, Tarvainen I, Kinnunen E, Udd B, Marklund SL
Brain, 1153-1172 1996
MED: 8813280
The gene disrupted in Marinesco-Sjogren syndrome encodes SIL1, an HSPA5 cochaperone.
Anttonen AK, Mahjneh I, Hamalainen RH, Lagier-Tourenne C, Kopra O, Waris L, Anttonen M, Joensuu T, Kalimo H, Paetau A, Tranebjaerg L, Chaigne D, Koenig M, Eeg-Olofsson O, Udd B, Somer M, Somer H, Lehesjoki AE
Nat Genet, (12):1309-1311 2005
MED: 16282978
High threshold for induction of the stress response in motor neurons is associated with failure to activate HSF1.
Batulan Z, Shinder GA, Minotti S, He BP, Doroudchi MM, Nalbantoglu J, Strong MJ, Durham HD
J Neurosci, (13):5789-5798 2003
MED: 12843283
Lessons from models of SOD1-linked familial ALS.
Bendotti C, Carri MT
Trends Mol Med, (8):393-400 2004
MED: 15310460
Onset and progression in inherited ALS determined by motor neurons and microglia.
Boillee S, Yamanaka K, Lobsiger CS, Copeland NG, Jenkins NA, Kassiotis G, Kollias G, Cleveland DW
Science, (5778):1389-1392 2006
MED: 16741123
Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis.
Bruening W, Roy J, Giasson B, Figlewicz DA, Mushynski WE, Durham HD
J Neurochem, (2):693-699 1999
MED: 9930742
ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions.
Bruijn LI, Becher MW, Lee MK, Anderson KL, Jenkins NA, Copeland NG, Sisodia SS, Rothstein JD, Borchelt DR, Price DL, Cleveland DW
Neuron, (2):327-338 1997
MED: 9052802
Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1.
Bruijn LI, Houseweart MK, Kato S, Anderson KL, Anderson SD, Ohama E, Reaume AG, Scott RW, Cleveland DW
Science, (5384):1851-1854 1998
MED: 9743498
Unraveling the mechanisms involved in motor neuron degeneration in ALS.
Bruijn LI, Miller TM, Cleveland DW
Annu Rev Neurosci, 723-749 2004
MED: 15217349
Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication.
Buchberger A, Theyssen H, Schroder H, McCarty JS, Virgallita G, Milkereit P, Reinstein J, Bukau B
J Biol Chem, (28):16903-16910 1995
MED: 7622507

Show 10 more references (10 of 47)

Citations & impact

Impact metrics

Citations

Jump to Citations

Citations of article over time

Article citations

Comprehensive expression analysis with cell-type-specific transcriptome in ALS-linked mutant SOD1 mice: Revisiting the active role of glial cells in disease.
Yamashita H, Komine O, Fujimori-Tonou N, Yamanaka K
Front Cell Neurosci, 16:1045647, 04 Jan 2023
Cited by: 3 articles | PMID: 36687517 | PMCID: PMC9846815
This article is in the Europe PMC Open access subset. Refer to the copyright information in the article for licensing details.
Free full text in Europe PMC
Proteostasis disturbance in amyotrophic lateral sclerosis.
Medinas DB, Valenzuela V, Hetz C
Hum Mol Genet, 26(r2):R91-R104, 01 Oct 2017
Cited by: 24 articles | PMID: 28977445
Review
The heat shock response in neurons and astroglia and its role in neurodegenerative diseases.
San Gil R, Ooi L, Yerbury JJ, Ecroyd H
Mol Neurodegener, 12(1):65, 18 Sep 2017
Cited by: 37 articles | PMID: 28923065 | PMCID: PMC5604514
Review
This article is in the Europe PMC Open access subset. Refer to the copyright information in the article for licensing details.
Free full text in Europe PMC
Intracerebroventricular administration of Cystatin C ameliorates disease in SOD1-linked amyotrophic lateral sclerosis mice.
Watanabe S, Komine O, Endo F, Wakasugi K, Yamanaka K
J Neurochem, 145(1):80-89, 07 Feb 2018
Cited by: 13 articles | PMID: 29282717 | PMCID: PMC5947136
This article is in the Europe PMC Open access subset. Refer to the copyright information in the article for licensing details.
Free full text in Europe PMC
A Metadata Analysis of Oxidative Stress Etiology in Preclinical Amyotrophic Lateral Sclerosis: Benefits of Antioxidant Therapy.
Bond L, Bernhardt K, Madria P, Sorrentino K, Scelsi H, Mitchell CS
Front Neurosci, 12:10, 24 Jan 2018
Cited by: 26 articles | PMID: 29416499 | PMCID: PMC5787557
This article is in the Europe PMC Open access subset. Refer to the copyright information in the article for licensing details.
Free full text in Europe PMC

Go to all (32) article citations

Search life-sciences literature (45,104,206 articles, preprints and more)

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

Affiliations

Authors

ORCIDs linked to this article

Abstract

Full text links

References

Autosomal recessive adult-onset amyotrophic lateral sclerosis associated with homozygosity for Asp90Ala CuZn-superoxide dismutase mutation. A clinical and genealogical study of 36 patients.

The gene disrupted in Marinesco-Sjogren syndrome encodes SIL1, an HSPA5 cochaperone.

High threshold for induction of the stress response in motor neurons is associated with failure to activate HSF1.

Lessons from models of SOD1-linked familial ALS.

Onset and progression in inherited ALS determined by motor neurons and microglia.

Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis.

ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions.

Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1.

Unraveling the mechanisms involved in motor neuron degeneration in ALS.

Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication.

Citations & impact

Impact metrics

Citations of article over time

Article citations

Comprehensive expression analysis with cell-type-specific transcriptome in ALS-linked mutant SOD1 mice: Revisiting the active role of glial cells in disease.

Proteostasis disturbance in amyotrophic lateral sclerosis.

The heat shock response in neurons and astroglia and its role in neurodegenerative diseases.

Intracerebroventricular administration of Cystatin C ameliorates disease in SOD1-linked amyotrophic lateral sclerosis mice.

A Metadata Analysis of Oxidative Stress Etiology in Preclinical Amyotrophic Lateral Sclerosis: Benefits of Antioxidant Therapy.

Similar Articles

Over-expression of Hsp27 does not influence disease in the mutant SOD1(G93A) mouse model of amyotrophic lateral sclerosis.

Overexpression of Abeta is associated with acceleration of onset of motor impairment and superoxide dismutase 1 aggregation in an amyotrophic lateral sclerosis mouse model.

Amyotrophic lateral sclerosis-related mutant superoxide dismutase 1 aggregates inhibit 14-3-3-mediated cell survival by sequestration into the JUNQ compartment.

Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues.

Partnerships & funding

Similar Articles

Over-expression of Hsp27 does not influence disease in the mutant SOD1(G93A) mouse model of amyotrophic lateral sclerosis.
J Neurochem, 106(5):2170-2183, 04 Jul 2008

Overexpression of Abeta is associated with acceleration of onset of motor impairment and superoxide dismutase 1 aggregation in an amyotrophic lateral sclerosis mouse model.
Aging Cell, 5(2):153-165, 01 Apr 2006

Amyotrophic lateral sclerosis-related mutant superoxide dismutase 1 aggregates inhibit 14-3-3-mediated cell survival by sequestration into the JUNQ compartment.
Hum Mol Genet, 26(18):3615-3629, 01 Sep 2017

Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues.
Neurobiol Dis, 8(6):933-941, 01 Dec 2001

Search life-sciences literature (45,104,206 articles, preprints and more)

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

Author information

Affiliations

Authors

ORCIDs linked to this article

Abstract

Full text links

References

Citations & impact

Impact metrics

Citations of article over time

Article citations

Similar Articles

Partnerships & funding