Grafting mouse brains: from neurocarcinogenesis to neurodegeneration

Aguzzi, Adriano

doi:10.1093/emboj/17.21.6107

Cited by 5 publications

(2 citation statements)

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“…36,58 Nonetheless, even 16 months after transplantation and infection with prions, no pathological changes were detected in the PrP c ‐deficient tissue, not even in the immediate vicinity of the grafts or the PrP c deposits. These results clearly suggest that PrP Sc is inherently nontoxic, and PrP Sc plaques found in spongiform encephalopathies may be an epiphenomenon rather than a cause of neuronal damage 59. Maybe the PrP Sc ‐containing plaques have to be formed and localized intracellularly in order to act neurotoxic.…”

Section: Neurografts In Prion Researchmentioning

confidence: 92%

“…These results clearly suggest that PrP Sc is inherently nontoxic, and PrP Sc plaques found in spongiform encephalopathies may be an epiphenomenon rather than a cause of neuronal damage. 59 Maybe the PrP Sc -containing plaques have to be formed and localized intracellularly in order to act neurotoxic. If this is the case, plaques that are localized extracellularly might not be toxic.…”

Section: Neurografts In Prion Researchmentioning

confidence: 99%

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Prions: Pathogenesis and Reverse Genetics

Aguzzi

Klein

Montrasio

et al. 2000

Annals of the New York Academy of Sciences

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Spongiform encephalopathies are a group of infectious neurodegenerative diseases. The infectious agent that causes transmissible spongiform encephalopathies was termed prion by Stanley Prusiner. The prion hypothesis states that the partially protease‐resistant and detergent‐insoluble prion protein (PrPsc) is identical with the infectious agent, and lacks any detectable nucleic acids. Since the latter discovery, transgenic mice have contributed many important insights into the field of prion biology. The prion protein (PrPc) is encoded by the Prnp gene, and disruption of Prnp leads to resistance to infection by prions. Introduction of mutant PrPc genes into PrPc‐deficient mice was used to investigate structure‐activity relationships of the PrPc gene with regard to scrapie susceptibility. Ectopic expression of PrPc in PrPc knockout mice proved a useful tool for the identification of host cells competent for prion replication. Finally, the availability of PrPc knockout and transgenic mice overexpressing PrPc allowed selective reconstitution experiments aimed at expressing PrPc in neurografts or in specific populations of hemato‐ and lymphopoietic cells. The latter studies helped in elucidating some of the mechanisms of prion spread and disease pathogenesis.

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Section: Neurografts In Prion Researchmentioning

confidence: 92%

Section: Neurografts In Prion Researchmentioning

confidence: 99%