The double life of the prion protein.

摘要: The function of the cellular prion protein PrPC, which is anchored to cell-surface by a glycolipid attachment, unknown. Its sequence highly conserved, usually implies that has some important function. But mild phenotype observed in PrP knockout mice — reduced long-term potentiation synaptic transmission, normally associated with learning, and sleep pattern abnormalities suggests whatever normal role it can be at least partially fulfilled other proteins.Point mutations gene lead inherited human neurological diseases resemble transmissible scrapie, such as Creutzfeldt–Jakob disease, Gerstmann–Straussler–Scheinker disease fatal familial insomnia. It difficult understand why only single mutation away from aggregation disaster should conserved. We propose solution this paradox. PrPC may require its controlled oligomerization under conditions prevent uncontrolled polymerization would PrPSc formation. oligomerized could involved cell–cell interactions, synapse formation or membrane recycling. elucidation hold key understanding pathogenesis scrapie related spongiform encephalopathies.