Access the full text.
Sign up today, get DeepDyve free for 14 days.
A. Muijsers, R. Stadt, A. Henrichs, H. Ament, J. Korst (1984)
D-penicillamine in patients with rheumatoid arthritis. Serum levels, pharmacokinetic aspects, and correlation with clinical course and side effects.Arthritis and rheumatism, 27 12
X. He, D. Carter (1993)
Atomic structure and chemistry of human serum albuminNature, 364
H. Deng, A. Hentati, J. Tainer, Zafar Iqbal, A. Cayabyab, W. Hung, E. Getzoff, Ping Hu, B. Herzfeldt, R. Roos, C. Warner, Gang Deng, Edwin Soriano, C. Smyth, H. Parge, Aftab Ahmed, A. Roses, R. Hallewell, M. Pericak-Vance, T. Siddique (1993)
Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase.Science, 261 5124
Lawyer (1953)
Amyotrophic lateral sclerosis: a clinicoanatomic study of 53 casesArch. Neurol., 69
S. Owen, G. Smart (1958)
Thyroid antibodies in myxoedema.Lancet, 2 7055
(1953)
Amyotrophic lateral sclerosis: a clinico
J. Belleroche, R. Orrell, L. Virgo (1996)
Amyotrophic Lateral Sclerosis: Recent Advances in Understanding Disease MechanismsJournal of Neuropathology and Experimental Neurology, 55
(1985)
Amyotrophic lateral sclerosis : part 1 . Clinical features , pathology , and ethical issues in management
P. Kennel, F. Finiels, F. Revah, J. Mallet (1996)
Neuromuscular function impairment is not caused by motor neurone loss in FALS mice: an electromyographic study.Neuroreport, 7 8
M. Canto, M. Gurney (1995)
Neuropathological changes in two lines of mice carrying a transgene for mutant human Cu,Zn SOD, and in mice overexpressing wild type human SOD: a model of familial amyotrophic lateral sclerosis (FALS)Brain Research, 676
T. Takeda, C. Yao, M. Irino, S. Tashiro, K. Yasuhira (1980)
D-Penicillamine toxicity in mice. I. Pathological findings.Toxicology and applied pharmacology, 55 2
D. Borchelt, Michael Lee, H. Slunt, M. Guarnieri, Zuoshang Xu, P. Wong, Robert Brown, D. Price, S. Sisodia, D. Cleveland (1994)
Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity.Proceedings of the National Academy of Sciences of the United States of America, 91 17
M. Gurney, Haifeng (Pu), A. Chiu, M. Canto, C. Polchow, D. Alexander, J. Caliendo, A. Hentati, Y. Kwon, H. Deng (1994)
Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation.Science, 264 5166
D. Cabelli, D. Allen, B. Bielski, J. Holcman (1989)
The interaction between Cu(I) superoxide dismutase and hydrogen peroxide.The Journal of biological chemistry, 264 17
S. Conradi, L. Ronnevi, G. Nise, O. Vesterberg (1982)
Long‐time penicillamine‐treatment in Amyotrophic Lateral Sclerosis with parallel determination of lead in blood, plasma and urineActa Neurologica Scandinavica, 65
M. Wiedau-Pazos, J. Goto, S. Rabizadeh, E. Gralla, J. Roe, Michael Lee, J. Valentine, D. Bredesen (1996)
Altered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral SclerosisScience, 271
S. Rabizadeh, E. Gralla, D. Borchelt, R. Gwinn, J. Valentine, S. Sisodia, P. Wong, Michael Lee, H. Hahn, D. Bredesen, D. Bredesen (1995)
Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells.Proceedings of the National Academy of Sciences of the United States of America, 92
D. Rosen, T. Siddique, D. Patterson, D. Figlewicz, P. Sapp, A. Hentati, D. Donaldson, J. Goto, J. O'Regan, H. Deng, Z. Rahmani, A. Krizus, D. McKenna-Yasek, A. Cayabyab, Sandra Gaston, R. Berger, Rudolph Tanzi, John Halperin, B. Herzfeldt, Raymond Bergh, W. Hung, T. Bird, G. Deng, Donald Mulder, C. Smyth, Nigel Laing, E. Soriano, M. Pericak-Vance, J. Haines, Guy Rouleau, James Gusella, H. Horvitz, Robert Brown (1993)
Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosisNature, 362
A. Jušić, M. Šoštarko (1977)
IMPROVEMENT OF SPINAL AMYOTROPHY BY PENICILLAMINE THERAPYThe Lancet, 310
(1993)
Mutations in CulZn superoxide dismutase gene
Rosen (1993)
Mutations in CulZn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosisNature, 364
A subpopulation of familial cases of amyotrophic lateral sclerosis has been linked to mutations in the gene encoding Cu/Zn superoxide dismutase (SOD1). There is in vitro evidence that certain SOD1 mutants, in addition to their normal dismutation function, show increased ability of the enzyme to act as a peroxidase. This reaction is sensitive to inhibition by copper chelators. To test this hypothesis in vivo, we administered the copper chelator d‐penicillamine to a transgenic mouse model of familial amyotrophic lateral sclerosis overexpressing a mutated form of human SOD1. We demonstrate that oral administration of d‐penicillamine is able to delay the onset of the disease and extend the survival of these mice. Histological studies also showed a decreased loss of facial motor neurons in d‐penicillamine‐treated transgenic mice, corroborating the slower evolution of the disease in these animals. These results suggest that copper chelators may benefit patients with familial amyotrophic lateral sclerosis linked to mutations in the SOD1 gene.
European Journal of Neuroscience – Wiley
Published: Jul 1, 1997
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.