Related Content
Search Google Scholar for:
|
|
Science 22 September 2006:
Vol. 313. no. 5794, pp. 1781 - 1784
DOI: 10.1126/science.1131864
|
|
Reports
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Melanie Meyer-Luehmann,1*
Janaky Coomaraswamy,1*
Tristan Bolmont,1,2*
Stephan Kaeser,1
Claudia Schaefer,1
Ellen Kilger,1
Anton Neuenschwander,3
Dorothee Abramowski,3
Peter Frey,3
Anneliese L. Jaton,3
Jean-Marie Vigouret,3
Paolo Paganetti,3
Dominic M. Walsh,4
Paul M. Mathews,5
Jorge Ghiso,6
Matthias Staufenbiel,3
Lary C. Walker,7
Mathias Jucker1,2
Protein aggregation is an established pathogenic mechanism in Alzheimer's disease, but little is known about the initiation of this process in vivo. Intracerebral injection of dilute, amyloid-ß (Aß)–containing brain extracts from humans with Alzheimer's disease or ß-amyloid precursor protein (APP) transgenic mice induced cerebral ß-amyloidosis and associated pathology in APP transgenic mice in a time- and concentration-dependent manner. The seeding activity of brain extracts was reduced or abolished by Aß immunodepletion, protein denaturation, or by Aß immunization of the host. The phenotype of the exogenously induced amyloidosis depended on both the host and the source of the agent, suggesting the existence of polymorphic Aß strains with varying biological activities reminiscent of prion strains.
1 Department of Cellular Neurology, Hertie-Institute for Clinical Brain Research, University of Tübingen, D-72076 Tübingen, Germany.
2 Institute of Pathology, University of Basel, CH-4003 Basel, Switzerland.
3 Novartis Institutes for Biomedical Research, CH-4002 Basel, Switzerland.
4 Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Dublin, Republic of Ireland.
5 Nathan Kline Institute, New York University School of Medicine, Orangeburg, NY 10962, USA.
6 Departments of Pathology and Psychiatry, New York University School of Medicine, New York, NY 10016, USA.
7 Yerkes National Primate Research Center and Department of Neurology, Emory University, Atlanta, GA 30322, USA.
* These authors contributed equally to this work.
 To whom correspondence should be addressed. E-mail: mathias.jucker{at}uni-tuebingen.de (M.J.); lary.walker{at}emory.edu (L.C.W.)
Read the Full Text
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
- Synapsin-I- and synapsin-II-null mice display an increased age-dependent cognitive impairment.
- A. Corradi, A. Zanardi, C. Giacomini, F. Onofri, F. Valtorta, M. Zoli, and F. Benfenati (2008)
J. Cell Sci.
121, 3042-3051
| Abstract »
| Full Text »
| PDF »
- Are cheetahs on the run from prion-like amyloidosis?.
- B. Caughey and G. S. Baron (2008)
PNAS
105, 7113-7114
| Full Text »
| PDF »
- Transmissible spongiform encephalopathy in the 21st century: Neuroscience for the clinical neurologist.
- P. Brown (2008)
Neurology
70, 713-722
| Full Text »
| PDF »
- Protein Misfolding and Neurodegeneration.
- C. Soto and L. D. Estrada (2008)
Arch Neurol
65, 184-189
| Abstract »
| Full Text »
| PDF »
- Unraveling prion strains with cell biology and organic chemistry.
- A. Aguzzi (2008)
PNAS
105, 11-12
| Full Text »
| PDF »
- Induction of Tau Pathology by Intracerebral Infusion of Amyloid- -Containing Brain Extract and by Amyloid- Deposition in APP x Tau Transgenic Mice.
- T. Bolmont, F. Clavaguera, M. Meyer-Luehmann, M. C. Herzig, R. Radde, M. Staufenbiel, J. Lewis, M. Hutton, M. Tolnay, and M. Jucker (2007)
Am. J. Pathol.
171, 2012-2020
| Abstract »
| Full Text »
| PDF »
- A General Model of Prion Strains and Their Pathogenicity.
- J. Collinge and A. R. Clarke (2007)
Science
318, 930-936
| Abstract »
| Full Text »
| PDF »
- Amyloid-specific fluorophores for the rapid, sensitive in situ detection of prion contamination on surgical instruments.
- I. P. Lipscomb, R. Herve, K. Harris, H. Pinchin, R. Collin, and C. W. Keevil (2007)
J. Gen. Virol.
88, 2619-2626
| Abstract »
| Full Text »
| PDF »
- Alzheimer's-Type Amyloidosis in Transgenic Mice Impairs Survival of Newborn Neurons Derived from Adult Hippocampal Neurogenesis.
- L. Verret, J. L. Jankowsky, G. M. Xu, D. R. Borchelt, and C. Rampon (2007)
J. Neurosci.
27, 6771-6780
| Abstract »
| Full Text »
| PDF »
- Accumulation of prion protein in the brain that is not associated with transmissible disease.
- P. Piccardo, J. C. Manson, D. King, B. Ghetti, and R. M. Barron (2007)
PNAS
104, 4712-4717
| Abstract »
| Full Text »
| PDF »
|
|
