Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions.
Cell
; 93(2): 203-14, 1998 Apr 17.
Article
en En
| MEDLINE
| ID: mdl-9568713
ABSTRACT
The physiological role of prion protein (PrP) remains unknown. Mice devoid of PrP develop normally but are resistant to scrapie; introduction of a PrP transgene restores susceptibility to the disease. To identify the regions of PrP necessary for this activity, we prepared PrP knockout mice expressing PrPs with amino-proximal deletions. Surprisingly, PrP lacking residues 32-121 or 32-134, but not with shorter deletions, caused severe ataxia and neuronal death limited to the granular layer of the cerebellum as early as 1-3 months after birth. The defect was completely abolished by introducing one copy of a wild-type PrP gene. We speculate that these truncated PrPs may be nonfunctional and compete with some other molecule with a PrP-like function for a common ligand.
Search on Google
Banco de datos:
MEDLINE
Asunto principal:
Ataxia
/
Scrapie
/
Priones
/
Cerebelo
/
Eliminación de Secuencia
Tipo de estudio:
Prognostic_studies
Límite:
Animals
Idioma:
En
Año:
1998
Tipo del documento:
Article