- DOH-URA, Katsumi
- SAKASEGAWA, Yuji
- KURAHASHI, Hiroshi
Prion diseases are infectious, fatal neurodegenerative illness. The pathogen tolerates ordinary sterilization procedures and is called “prion”, which is free of genome and consists mainly of a host-encoded protein, prion protein. The nature of prion is still one of the most challenging mysteries in science. In addition, recent outbreaks of new types of prion diseases in animals and humans demonstrate that this mysterious pathogen is a real threat to world public health. Thus, developments of prophylactic and therapeutic interventions as well as early diagnostic measurements are seriously demanded in the world.
Our research scope is based on these circumstances and ranges from basic science to technology related to the following challenges.
- Development of prophylactic and therapeutic interventions, and search for novel drug targets and novel surrogate markers for prion diseases.
- Elucidation of molecular mechanism of prion infection and replication, by means of both the pharmacology of anti-prion compounds and the molecular biology of prion protein interacting cellular factors.
- Application of anti-prion compounds and other newly developed items to other incurable conformational diseases such as Alzheimer’s disease and amyloidoses.
The goal of our research is both disclosing the molecular mechanisms of prion diseases and other conformational diseases and making them curable.
Selected Awards, articles and books
1) Anti-prion activity of protein-bound polysaccharide K in prion-infected cells and animals. Biochem Biophys Res Commun. 2011; 405:285-90.
2) GABAA receptor subunit beta1 is involved in the formation of protease-resistant prion protein in prion-infected neuroblastoma cells. FEBS Lett. 2010; 584(6):1193-8.
3) In vivo detection of prion amyloid plaques using [(11)C]BF-227 PET. Eur J Nucl Med Mol Imaging. 2010; 37(5):934-41.
4) Amyloidophilic compounds for prion diseases. Infect Disord Drug Targets. 2009; 9(1):15-22.
5) Antiprion activity of functionalized 9-aminoacridines related to quinacrine. Bioorg Med Chem. 2008;16(14):6737-46.
transmissible spongiform encephalopathy, prion disease, neurodegenerative disease, conformational disease, therapy, diagnosis, pathogenesis, protein structure, pharmacology, chemistry
- doh-ura*med.tohoku.ac.jp (Please convert "*" into "@".)
- TEL +81-22-717-8232
- FAX +81-22-717-7656