Prions prevent neuronal cell-line death

Chieko Kuwahara, Alice M. Takeuchi, Takuya Nishimura, Keiko Haraguchi, Atsutaka Kubosaki, Yasunobu Matsumoto, Keiichi Saeki, Yoshitsugu Matsumoto, Takashi Yokoyama, Shigeyoshi Itohara and Takashi Onodera ()
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Chieko Kuwahara: School of Agricultural and Life Sciences, University of Tokyo
Alice M. Takeuchi: School of Agricultural and Life Sciences, University of Tokyo
Takuya Nishimura: School of Agricultural and Life Sciences, University of Tokyo
Keiko Haraguchi: School of Agricultural and Life Sciences, University of Tokyo
Atsutaka Kubosaki: School of Agricultural and Life Sciences, University of Tokyo
Yasunobu Matsumoto: School of Agricultural and Life Sciences, University of Tokyo
Keiichi Saeki: School of Agricultural and Life Sciences, University of Tokyo
Yoshitsugu Matsumoto: School of Agricultural and Life Sciences, University of Tokyo
Takashi Yokoyama: National Institute of Animal Health
Shigeyoshi Itohara: Laboratory for Behavioural Genetics, Brain Science Institute, RIKEN
Takashi Onodera: School of Agricultural and Life Sciences, University of Tokyo

Nature, 1999, vol. 400, issue 6741, 225-226

Abstract: Abstract Prion diseases, such as scrapie and bovine spongiform encephalopathy (BSE) in animals and Creutzfeldt-Jakob disease (CJD) in humans, are neurodegenerative conditions characterized by the accumulation of a post-transcriptionally modified, pathological form of a host-encoded glycoprotein, designated PrPSc. The physiological function of the normal cellular isoform, PrPC, is unknown, although studies of mice devoid of PrPC have indicated that it may be involved in normal synaptic function and survival of Purkinje cells, but findings have been inconsistent1,2,3,4,5,6. We find that serum removal from the cell culture causes apoptosis in Prnp −/− cells (in which a disrupted form of the prion protein is produced) but not in Prnp +/+ (wild-type) cells. Transduction of PrP or the Bcl-2 gene suppressed apoptosis of Prnp −/− cells under serum-free conditions. We also found that Prnp −/− cells extended shorter neurites than Prnp +/+ cells, but expression of PrPC increased their length. These findings support the idea that the loss of function of PrPC may partly underlie the pathogenesis of prion diseases.

Date: 1999
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DOI: 10.1038/22241

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