Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (51)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Stevanin, G.
Right arrow Articles by Brice, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stevanin, G.
Right arrow Articles by Brice, A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Human Molecular Genetics, Vol 5, 1887-1892, Copyright © 1996 by Oxford University Press

ARTICLES

Screening for proteins with polyglutamine expansions in autosomal dominant cerebellar ataxias

G Stevanin, Y Trottier, G Cancel, A Durr, G David, O Didierjean, K Burk, G Imbert, F Saudou, M Abada-Bendib, I Gourfinkel-An, A Benomar, N Abbas, T Klockgether, D Grid, Y Agid, JL Mandel and A Brice
INSERM U289, Hopital de la Salpetriere, Paris, France.

Expansion of trinucleotide CAG repeats coding for polyglutamine has been implicated in five neurodegenerative disorders, including spinocerebellar ataxia (SCA) 1 and SCA3 or Machado-Joseph disease (SCA3/MJD), two forms of type I autosomal dominant cerebellar ataxias (ADCA). Using the 1C2 antibody which specifically recognizes large polyglutamine tracts, particularly those that are expanded, we recently reported the detection of proteins with pathological glutamine expansions in lymphoblasts from another form of ADCA type I, SCA2, as well as from patients presenting with the distinct phenotype of ADCA type II. We now have screened a large series of patients with ADCA or isolated cases with cerebellar ataxia, for the presence of proteins with polyglutamine expansions. A 150 kDa SCA2 protein was detected in 16 out of 40 families with ADCA type I. This corresponds to 24% of all ADCA type I families, which is much more frequent than SCA1 in this series of patients (13%). The signal intensity of the SCA2 protein was negatively correlated to age at onset, as expected for an expanded and unstable trinucleotide repeat mutation. The disease segregated with markers closely linked to the SCA2 locus in all identified SCA2 families. In addition, a specific 130 kDa protein, which segregated with the disease, was detected in lymphoblasts of patients from nine families with ADCA type II. It was also visualized in the cerebral cortex of one of the patients, demonstrating its translation in the nervous system. Finally, no new disease-related proteins containing expanded polyglutamine tracts could be detected in lymphoblasts from the remaining patients with ADCA or isolated cases with cerebellar ataxia.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 FASEB J.Home page
M. Cyr, T. D. Sotnikova, R. R. Gainetdinov, and M. G. Caron
Dopamine enhances motor and neuropathological consequences of polyglutamine expanded huntingtin
FASEB J, December 1, 2006; 20(14): 2541 - 2543.
[Abstract] [Full Text] [PDF]

Home page
 Arch NeurolHome page
A. Brusco, C. Gellera, C. Cagnoli, A. Saluto, A. Castucci, C. Michielotto, V. Fetoni, C. Mariotti, N. Migone, S. Di Donato, et al.
Molecular Genetics of Hereditary Spinocerebellar Ataxia: Mutation Analysis of Spinocerebellar Ataxia Genes and CAG/CTG Repeat Expansion Detection in 225 Italian Families
Arch Neurol, May 1, 2004; 61(5): 727 - 733.
[Abstract] [Full Text] [PDF]

Home page
 BrainHome page
M.-y. Chung, Y.-C. Lu, N.-C. Cheng, and B.-W. Soong
A novel autosomal dominant spinocerebellar ataxia (SCA22) linked to chromosome 1p21-q23
Brain, June 1, 2003; 126(6): 1293 - 1299.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
J. C. Dorsman, B. Pepers, D. Langenberg, H. Kerkdijk, M. Ijszenga, J. T. den Dunnen, R.A.C. Roos, and G.-J. B. van Ommen
Strong aggregation and increased toxicity of polyleucine over polyglutamine stretches in mammalian cells
Hum. Mol. Genet., June 15, 2002; 11(13): 1487 - 1496.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
K. Nakamura, S.-Y. Jeong, T. Uchihara, M. Anno, K. Nagashima, T. Nagashima, S.-i. Ikeda, S. Tsuji, and I. Kanazawa
SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein
Hum. Mol. Genet., July 1, 2001; 10(14): 1441 - 1448.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
J. L. Marsh, H. Walker, H. Theisen, Y.-Z. Zhu, T. Fielder, J. Purcell, and L. M. Thompson
Expanded polyglutamine peptides alone are intrinsically cytotoxic and cause neurodegeneration in Drosophila
Hum. Mol. Genet., January 1, 2000; 9(1): 13 - 25.
[Abstract] [Full Text] [PDF]

Home page
 NeurologyHome page
G. Stevanin, A. Herman, A. Brice, and A. Durr
Clinical and MRI findings in spinocerebellar ataxia type 5
Neurology, October 1, 1999; 53(6): 1355 - 1355.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.