Abstract
The normal cellular prion protein (PrP(c)) is a membrane sialoglycoprotein of unknown function having the unique property of adopting an abnormal tertiary conformation. The pathological conformer PrP(sc) would be the agent of transmissible spongiform encephalopathies or prion diseases. They include scrapie and bovine spongiform encephalopathy in animals and Creutzfeldt-Jakob disease in humans. The conversion of PrP(c) into PrP(sc) in the brain governs the clinical phenotype of the disease. However, the three-dimensional structure change of PrP(c) can also take place outside the central nervous system, in nonneuronal cells particularly of lymphoid tissue where the agent replicates. In natural infection, PrP(c) in nonneuronal cells of peripheral extracerebral organs may play a key role as the receptor required to enable the entry of the infectious agent into the host. In the present review we have undertaken a first evaluation of compelling data concerning the PrP(c)-expressing cells of nonneuronal origin present in cerebral and extracerebral tissues. The analysis of tissue, cellular, and subcellular localization of PrP(c) may help us better understand the biological function of PrP(c) and provide some information on physiopathological processes underlying prion diseases.
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