NR ABEI
AU Behrens,A.; Aguzzi,A.
TI Small is not beautiful: antagonizing functions for the prion protein PrPc and its homologue Dpl.
QU Trends in Neurosciences 2002 Mar; 25(3): 150-4
PT journal article; review; review, tutorial
AB A conformational variant of the normal prion protein PrPc is believed to be identical to PrPsc, the agent that causes prion diseases. Recently, a novel protein, named Doppel (Dpl), was identified that shares significant biochemical and structural homology with PrPc. In specific strains of PrPc-deficient mouse lines, Dpl is overexpressed and causes a neurological disease. Dpl neurotoxicity is counteracted and prevented by PrPc, but the mechanism of antagonistic PrPc-Dpl interaction remains elusive. In contrast to its homologue PrPc, initial studies suggest that Dpl is dispensable for prion disease progression and for the generation of PrPsc. Although we are only beginning to understand its function, the discovery of Dpl has already provided some answers to long-standing questions and is transforming our understanding of prion biology.
ZR 42
MH Animal; Cell Death/genetics; Central Nervous System/*metabolism/pathology/physiopathology; Gene Expression Regulation/*physiology; Human; Mice; Mice, Knockout; Models, Neurological; PrPc Proteins/*deficiency/genetics; Prion Diseases/genetics/*metabolism/physiopathology; Prions/genetics/*metabolism; Support, Non-U.S. Gov't
AD Mammalian Genetics Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London, UK
SP englisch
PO England