JBC Origene Your Gene Company

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M010759200 on January 22, 2001

J. Biol. Chem., Vol. 276, Issue 16, 12791-12796, April 20, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/16/12791    most recent
M010759200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Shinder, G. A.
Right arrow Articles by Durham, H. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shinder, G. A.
Right arrow Articles by Durham, H. D.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Mutant Cu/Zn-Superoxide Dismutase Proteins Have Altered Solubility and Interact with Heat Shock/Stress Proteins in Models of Amyotrophic Lateral Sclerosis*

Gayle A. Shinder, Marie-Claude Lacourse, Sandra Minotti, and Heather D. DurhamDagger

From the Department of Neurology/Neurosurgery and Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada

Mutations in the Cu/Zn-superoxide dismutase (SOD-1) gene are responsible for a familial form of amyotrophic lateral sclerosis. In humans and experimental models, death of motor neurons is preceded by formation of cytoplasmic aggregates containing mutant SOD-1 protein. In our previous studies, heat shock protein 70 (HSP70) prolonged viability of cultured motor neurons expressing mutant human SOD-1 and reduced formation of aggregates. In this paper, we report that mutant SOD-1 proteins have altered solubility in cells relative to wild-type SOD-1 and can form a direct association with HSP70 and other stress proteins. Whereas wild-type human and endogenous mouse SOD-1 were detergent-soluble, a portion of mutant SOD-1 was detergent-insoluble in protein extracts of NIH3T3 transfected with SOD-1 gene constructs, spinal cord cultures established from G93A SOD-1 transgenic mouse embryos, and lumbar spinal cord from adult G93A transgenic mice. A direct association of HSP70, HSP40, and alpha B-crystallin with mutant SOD-1 (G93A or G41S), but not wild-type or endogenous mouse SOD-1, was demonstrated by coimmunoprecipitation. Mutant SOD-1·HSP70 complexes were predominantly in the detergent-insoluble fraction. However, only a small percentage of total cellular mutant SOD-1 was detergent-insoluble, suggesting that mutation-induced alteration of protein conformation may not in itself be sufficient for direct interaction with heat shock proteins.

* This research was supported by the Amyotrophic Lateral Sclerosis Association, the Amyotrophic Lateral Sclerosis Society of Canada, the Muscular Dystrophy Associations of Canada and the United States, and the Canadian Institutes for Health Research.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger A Killam Scholar. To whom correspondence should be addressed: Rm. 649, Montreal Neurological Institute, 3801 University St., Montreal, Quebec H3A 2B4, Canada. Tel.: 514-398-8509; Fax: 514-398-1509; E-mail: mddm@musica.mcgill.ca.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M. R. Watson, R. D. Lagow, K. Xu, B. Zhang, and N. M. Bonini
A Drosophila Model for Amyotrophic Lateral Sclerosis Reveals Motor Neuron Damage by Human SOD1
J. Biol. Chem., September 5, 2008; 283(36): 24972 - 24981.
[Abstract] [Full Text] [PDF]

Home page
 FASEB J.Home page
M. Urushitani, S. A. Ezzi, A. Matsuo, I. Tooyama, and J.-P. Julien
The endoplasmic reticulum-Golgi pathway is a target for translocation and aggregation of mutant superoxide dismutase linked to ALS
FASEB J, July 1, 2008; 22(7): 2476 - 2487.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
J. B. Proescher, M. Son, J. L. Elliott, and V. C. Culotta
Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS
Hum. Mol. Genet., June 15, 2008; 17(12): 1728 - 1737.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
H. Nishitoh, H. Kadowaki, A. Nagai, T. Maruyama, T. Yokota, H. Fukutomi, T. Noguchi, A. Matsuzawa, K. Takeda, and H. Ichijo
ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1
Genes & Dev., June 1, 2008; 22(11): 1451 - 1464.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. M. Karch and D. R. Borchelt
A Limited Role for Disulfide Cross-linking in the Aggregation of Mutant SOD1 Linked to Familial Amyotrophic Lateral Sclerosis
J. Biol. Chem., May 16, 2008; 283(20): 13528 - 13537.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
H. Witan, A. Kern, I. Koziollek-Drechsler, R. Wade, C. Behl, and A. M. Clement
Heterodimer formation of wild-type and amyotrophic lateral sclerosis-causing mutant Cu/Zn-superoxide dismutase induces toxicity independent of protein aggregation
Hum. Mol. Genet., May 15, 2008; 17(10): 1373 - 1385.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. F. Shaw, H. L. Lelie, A. Durazo, A. M. Nersissian, G. Xu, P. K. Chan, E. B. Gralla, A. Tiwari, L. J. Hayward, D. R. Borchelt, et al.
Detergent-insoluble Aggregates Associated with Amyotrophic Lateral Sclerosis in Transgenic Mice Contain Primarily Full-length, Unmodified Superoxide Dismutase-1
J. Biol. Chem., March 28, 2008; 283(13): 8340 - 8350.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
D. J. Gifondorwa, M. B. Robinson, C. D. Hayes, A. R. Taylor, D. M. Prevette, R. W. Oppenheim, J. Caress, and C. E. Milligan
Exogenous Delivery of Heat Shock Protein 70 Increases Lifespan in a Mouse Model of Amyotrophic Lateral Sclerosis
J. Neurosci., November 28, 2007; 27(48): 13173 - 13180.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
L. Ferraiuolo, P. R. Heath, H. Holden, P. Kasher, J. Kirby, and P. J. Shaw
Microarray Analysis of the Cellular Pathways Involved in the Adaptation to and Progression of Motor Neuron Injury in the SOD1 G93A Mouse Model of Familial ALS
J. Neurosci., August 22, 2007; 27(34): 9201 - 9219.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
L. Lu, L. Zheng, L. Viera, E. Suswam, Y. Li, X. Li, A. G. Estevez, and P. H. King
Mutant Cu/Zn-Superoxide Dismutase Associated with Amyotrophic Lateral Sclerosis Destabilizes Vascular Endothelial Growth Factor mRNA and Downregulates Its Expression
J. Neurosci., July 25, 2007; 27(30): 7929 - 7938.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. M. Taylor, B. F. Gibbs, E. Kabashi, S. Minotti, H. D. Durham, and J. N. Agar
Tryptophan 32 Potentiates Aggregation and Cytotoxicity of a Copper/Zinc Superoxide Dismutase Mutant Associated with Familial Amyotrophic Lateral Sclerosis
J. Biol. Chem., June 1, 2007; 282(22): 16329 - 16335.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
Y. Wang, X. Ou Mao, L. Xie, S. Banwait, H. H. Marti, D. A. Greenberg, and K. Jin
Vascular Endothelial Growth Factor Overexpression Delays Neurodegeneration and Prolongs Survival in Amyotrophic Lateral Sclerosis Mice
J. Neurosci., January 10, 2007; 27(2): 304 - 307.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Basso, T. Massignan, G. Samengo, C. Cheroni, S. De Biasi, M. Salmona, C. Bendotti, and V. Bonetto
Insoluble Mutant SOD1 Is Partly Oligoubiquitinated in Amyotrophic Lateral Sclerosis Mice
J. Biol. Chem., November 3, 2006; 281(44): 33325 - 33335.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. D. Atkin, M. A. Farg, B. J. Turner, D. Tomas, J. A. Lysaght, J. Nunan, A. Rembach, P. Nagley, P. M. Beart, S. S. Cheema, et al.
Induction of the Unfolded Protein Response in Familial Amyotrophic Lateral Sclerosis and Association of Protein-disulfide Isomerase with Superoxide Dismutase 1
J. Biol. Chem., October 6, 2006; 281(40): 30152 - 30165.
[Abstract] [Full Text] [PDF]

Home page
 FASEB J.Home page
C. E-H. Moussa, Q. Fu, P. Kumar, A. Shtifman, J. R. Lopez, P. D. Allen, F. LaFerla, D. Weinberg, J. Magrane, T. Aprahamian, et al.
Transgenic expression of {beta}-APP in fast-twitch skeletal muscle leads to calcium dyshomeostasis and IBM-like pathology
FASEB J, October 1, 2006; 20(12): 2165 - 2167.
[Abstract] [Full Text] [PDF]

Home page
 BrainHome page
P. A. Jonsson, K. S. Graffmo, P. M. Andersen, T. Brannstrom, M. Lindberg, M. Oliveberg, and S. L. Marklund
Disulphide-reduced superoxide dismutase-1 in CNS of transgenic amyotrophic lateral sclerosis models
Brain, February 1, 2006; 129(2): 451 - 464.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
M. Perluigi, H. F. Poon, W. Maragos, W. M. Pierce, J. B. Klein, V. Calabrese, C. Cini, C. De Marco, and D. A. Butterfield
Proteomic Analysis of Protein Expression and Oxidative Modification in R6/2 Transgenic Mice: A Model of Huntington Disease
Mol. Cell. Proteomics, December 1, 2005; 4(12): 1849 - 1861.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
J. Zhai, H. Lin, R. Canete-Soler, and W. W. Schlaepfer
HoxB2 binds mutant SOD1 and is altered in transgenic model of ALS
Hum. Mol. Genet., September 15, 2005; 14(18): 2629 - 2640.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Tiwari, Z. Xu, and L. J. Hayward
Aberrantly Increased Hydrophobicity Shared by Mutants of Cu,Zn-Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis
J. Biol. Chem., August 19, 2005; 280(33): 29771 - 29779.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M. J. Lindberg, R. Bystrom, N. Boknas, P. M. Andersen, and M. Oliveberg
Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants
PNAS, July 12, 2005; 102(28): 9754 - 9759.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y.-J. Kim, R. Nakatomi, T. Akagi, T. Hashikawa, and R. Takahashi
Unsaturated Fatty Acids Induce Cytotoxic Aggregate Formation of Amyotrophic Lateral Sclerosis-linked Superoxide Dismutase 1 Mutants
J. Biol. Chem., June 3, 2005; 280(22): 21515 - 21521.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Tummala, C. Jung, A. Tiwari, C. M. J. Higgins, L. J. Hayward, and Z. Xu
Inhibition of Chaperone Activity Is a Shared Property of Several Cu,Zn-Superoxide Dismutase Mutants That Cause Amyotrophic Lateral Sclerosis
J. Biol. Chem., May 6, 2005; 280(18): 17725 - 17731.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
B. J. Turner, J. D. Atkin, M. A. Farg, D. W. Zang, A. Rembach, E. C. Lopes, J. D. Patch, A. F. Hill, and S. S. Cheema
Impaired Extracellular Secretion of Mutant Superoxide Dismutase 1 Associates with Neurotoxicity in Familial Amyotrophic Lateral Sclerosis
J. Neurosci., January 5, 2005; 25(1): 108 - 117.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M. J. Lindberg, J. Normark, A. Holmgren, and M. Oliveberg
Folding of human superoxide dismutase: Disulfide reduction prevents dimerization and produces marginally stable monomers
PNAS, November 9, 2004; 101(45): 15893 - 15898.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
H. Lin, J. Zhai, R. Canete-Soler, and W. W. Schlaepfer
3' Untranslated Region in a Light Neurofilament (NF-L) mRNA Triggers Aggregation of NF-L and Mutant Superoxide Dismutase 1 Proteins in Neuronal Cells
J. Neurosci., March 17, 2004; 24(11): 2716 - 2726.
[Abstract] [Full Text] [PDF]

Home page
 BrainHome page
P. A. Jonsson, K. Ernhill, P. M. Andersen, D. Bergemalm, T. Brannstrom, O. Gredal, P. Nilsson, and S. L. Marklund
Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis
Brain, January 1, 2004; 127(1): 73 - 88.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. B. Pedersen, P. Bross, V. S. Winter, T. J. Corydon, L. Bolund, K. Bartlett, J. Vockley, and N. Gregersen
Misfolding, Degradation, and Aggregation of Variant Proteins: THE MOLECULAR PATHOGENESIS OF SHORT CHAIN ACYL-CoA DEHYDROGENASE (SCAD) DEFICIENCY
J. Biol. Chem., November 28, 2003; 278(48): 47449 - 47458.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
J. Wang, H. Slunt, V. Gonzales, D. Fromholt, M. Coonfield, N. G. Copeland, N. A. Jenkins, and D. R. Borchelt
Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature
Hum. Mol. Genet., November 1, 2003; 12(21): 2753 - 2764.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
Z. Batulan, G. A. Shinder, S. Minotti, B. P. He, M. M. Doroudchi, J. Nalbantoglu, M. J. Strong, and H. D. Durham
High Threshold for Induction of the Stress Response in Motor Neurons Is Associated with Failure to Activate HSF1
J. Neurosci., July 2, 2003; 23(13): 5789 - 5798.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
P. B. Stathopulos, J. A. O. Rumfeldt, G. A. Scholz, R. A. Irani, H. E. Frey, R. A. Hallewell, J. R. Lepock, and E. M. Meiering
Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro
PNAS, June 10, 2003; 100(12): 7021 - 7026.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Son, C. D. Cloyd, J. D. Rothstein, B. Rajendran, and J. L. Elliott
Aggregate Formation in Cu,Zn Superoxide Dismutase-related Proteins
J. Biol. Chem., April 11, 2003; 278(16): 14331 - 14336.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Tiwari and L. J. Hayward
Familial Amyotrophic Lateral Sclerosis Mutants of Copper/Zinc Superoxide Dismutase Are Susceptible to Disulfide Reduction
J. Biol. Chem., February 14, 2003; 278(8): 5984 - 5992.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M. J. Lindberg, L. Tibell, and M. Oliveberg
Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: Decreased stability of the apo state
PNAS, December 24, 2002; 99(26): 16607 - 16612.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
J. Kirby, F. M. Menzies, M. R. Cookson, K. Bushby, and P. J. Shaw
Differential gene expression in a cell culture model of SOD1-related familial motor neurone disease
Hum. Mol. Genet., August 15, 2002; 11(17): 2061 - 2075.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. Okado-Matsumoto and I. Fridovich
Amyotrophic lateral sclerosis: A proposed mechanism
PNAS, June 25, 2002; 99(13): 9010 - 9014.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.