Skip Navigation

This Article
Right arrow Full Text (PDF)
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 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 arrowRequest Permissions
Google Scholar
Right arrow Articles by Jou, Y.-S.
Right arrow Articles by Myers, R. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jou, Y.-S.
Right arrow Articles by Myers, R. M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 1995 Oxford University Press

OTHER

Evidence from antibody studies that the CAG repeat in the Huntington disease gene is expressed in the protein

Yuh-Shan Jou and Richard M. Myers*

Department of Genetics, M-344, Stanford University, School of Medicine Stanford, CA 94305-5120, USA

*To whom correspondence should be addressed

Received November 8, 1994; Revised December 14, 1994; Accepted December 14, 1994

The neurodegenerative disorder Huntington disease (HD) appears to be caused by an increase in the number of repeats of the trinucleotide CAG located near the 5' end of the gene. The nucleotide sequences of the cDNA and the gene predict that the HD protein has a molecular weight of 347 000 (3144 amino acids) and that the CAG repeats encode a segment of polyglutamine beginning 17 amino acids from the amino terminus. Because the CAG repeat plays such a critical role in the etiology of the disease, we sought to obtain evidence that the polyglutamine segment is indeed present in the protein. We used two peptides, hd1-peptide (FESLKSFQQ), predicted to lie at amino acid positions 11–19, just amino-terminal to the polyglutamine segment, and hd2-peptide (QQPRNKPLK), predicted to lie at amino acid positions 2531–2539, to induce polyclonal antibodies in NZW rabbits. Both antibodies recognize a protein on Western blots of about 350 kDa in cell lysates from human brain tissue and human and monkey cell lines, including cells from individuals heterozygous and homozygous for the disease. These results suggest that the HD protein in these cells contains the predicted amino terminal segment, and by inference, the segment of polyglutamine, and that the protein is expressed even when only mutant copies of the gene are present. Interestingly, the antibody to hd1-peptide does not recognize the HD protein on Western blots containing lysates from rodent cell lines, whereas the antibody to hd2-peptide does. This discrimination provides a useful means to assay for the presence of the human HD protein in a rodent cell background.


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
 Nucleic Acids ResHome page
J. Lee, E. H. Park, G. Couture, I. Harvey, P. Garneau, and J. Pelletier
An upstream open reading frame impedes translation of the huntingtin gene
Nucleic Acids Res., December 1, 2002; 30(23): 5110 - 5119.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
V. Syed, E. Gomez, and N. B. Hecht
mRNAs Encoding a von Ebner's-like Protein and the Huntington Disease Protein Are Induced in Rat Male Germ Cells by Sertoli Cells
J. Biol. Chem., April 16, 1999; 274(16): 10737 - 10742.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. J. L. Cooper, K.-F. R. Sheu, J. R. Burke, O. Onodera, W. J. Strittmatter, A. D. Roses, and J. P. Blass
Transglutaminase-catalyzed inactivation of glyceraldehyde 3-phosphate dehydrogenase and alpha -ketoglutarate dehydrogenase complex by polyglutamine domains of pathological length
PNAS, November 11, 1997; 94(23): 12604 - 12609.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. A. Kalchman, R. K. Graham, G. Xia, H. B. Koide, J. G. Hodgson, K. C. Graham, Y. P. Goldberg, R. D. Gietz, C. M. Pickart, and M. R. Hayden
Huntingtin Is Ubiquitinated and Interacts with a Specific Ubiquitin-conjugating Enzyme
J. Biol. Chem., August 9, 1996; 271(32): 19385 - 19394.
[Abstract] [Full Text] [PDF]

Home page
 Cold Spring Harb Symp Quant BiolHome page
W.J. Strittmatter, J.R. Burke, V.S. DeSerrano, D.Y. Huang, W. Matthew, A.M. Saunders, B.L. Scott, J.M. Vance, K.H. Weisgraber, and A.D. Roses
Protein:Protein Interactions in Alzheimer's Disease and the CAG Triplet Repeat Diseases
Cold Spring Harb Symp Quant Biol, January 1, 1996; 61(0): 597 - 605.
[Abstract] [PDF]

Home page
 Cold Spring Harb Symp Quant BiolHome page
J.F. Gusella, S. McNeil, F. Persichetti, J. Srinidhi, A. Novelletto, E. Bird, P. Faber, J.-P. Vonsattel, R.H. Myers, and M.E. MacDonald
Huntington's Disease
Cold Spring Harb Symp Quant Biol, January 1, 1996; 61(0): 615 - 626.
[Abstract] [PDF]

Home page
 ScienceHome page
M. Duyao, A. Auerbach, A Ryan, F Persichetti, G. Barnes, S. McNeil, P Ge, J. Vonsattel, J. Gusella, A. Joyner, et al.
Inactivation of the mouse Huntington's disease gene homolog Hdh
Science, July 21, 1995; 269(5222): 407 - 410.
[Abstract] [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.