Lysosomotropic Agents and Cysteine Protease Inhibitors Inhibit Scrapie-Associated Prion Protein Accumulation

Author:

Doh-ura Katsumi1,Iwaki Toru1,Caughey Byron2

Affiliation:

1. Department of Neuropathology, Neurological Institute, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan, 1 and

2. Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 59840 2

Abstract

We report that lysosomotropic agents and cysteine protease inhibitors inhibited protease-resistant prion protein accumulation in scrapie-infected neuroblastoma cells. The inhibition occurred without either apparent effects on normal prion protein biosynthesis or turnover or direct interactions with prion protein molecules. The findings introduce two new classes of inhibitors of the formation of protease-resistant prion protein.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Reference33 articles.

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3. Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells.;Borchelt D. R.;J. Cell Biol.,1990

4. Precise targeting of the pathology of the sialoglycoprotein, PrP, and vacuolar degeneration in mouse scrapie.;Bruce M. E.;Neurosci. Lett.,1989

5. Prion protein and the transmissible spongiform encephalopathies.;Caughey B.;Trends Cell Biol.,1997

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