Small is not beautiful: antagonizing functions for the prion protein PrP(C) and its homologue Dpl

Trends Neurosci. 2002 Mar;25(3):150-4. doi: 10.1016/s0166-2236(00)02089-0.

Abstract

A conformational variant of the normal prion protein PrP(C) is believed to be identical to PrP(Sc), the agent that causes prion diseases. Recently, a novel protein, named Doppel (Dpl), was identified that shares significant biochemical and structural homology with PrP(C). In specific strains of PrP(C)-deficient mouse lines, Dpl is overexpressed and causes a neurological disease. Dpl neurotoxicity is counteracted and prevented by PrP(C), but the mechanism of antagonistic PrP(C)-Dpl interaction remains elusive. In contrast to its homologue PrP(C), initial studies suggest that Dpl is dispensable for prion disease progression and for the generation of PrP(Sc). 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cell Death / genetics
  • Central Nervous System / metabolism*
  • Central Nervous System / pathology
  • Central Nervous System / physiopathology
  • GPI-Linked Proteins
  • Gene Expression Regulation / physiology*
  • Humans
  • Mice
  • Mice, Knockout
  • Models, Neurological
  • PrPC Proteins / deficiency*
  • PrPC Proteins / genetics
  • Prion Diseases / genetics
  • Prion Diseases / metabolism*
  • Prion Diseases / physiopathology
  • Prions / genetics
  • Prions / metabolism*

Substances

  • GPI-Linked Proteins
  • PRND protein, human
  • PrPC Proteins
  • Prions
  • Prnd protein, mouse