title: Almost a century of prion protein(s): From pathology to physiology, and back to pathology.
abstract: Prions are one of the few pathogens whose name is renowned at all population levels, after the dramatic years pervaded by the fear of eating prion-infected food. If now this, somehow irrational, scare of bovine meat inexorably transmitting devastating brain disorders is largely subdued, several prion-related issues are still unsolved, precluding the design of therapeutic approaches that could slow, if not halt, prion diseases. One unsolved issue is, for example, the role of the prion protein (PrPC), whole conformational misfolding originates the prion but whose physiologic reason d'etre in neurons, and in cells at large, remains enigmatic. Preceded by a historical outline, the present review will discuss the functional pleiotropicity ascribed to PrPC, and whether this aspect could fall, at least in part, into a more concise framework. It will also be devoted to radically different perspectives for PrPC, which have been recently brought to the attention of the scientific world with unexpected force. Finally, it will discuss the possible reasons allowing an evolutionary conserved and benign protein, as PrPCis, to turn into a high affinity receptor for pathologic misfolded oligomers, and to transmit their toxic message into neurons.
authors: Department of Biomedical Sciences, University of Padova, Via Bassi 58/B, 35131 Padova, Italy. Electronic address: caterina.peggion@unipd.it.
authors: Caterina
authors: C
authors: Peggion
authors: Department of Biomedical Sciences, University of Padova, Via Bassi 58/B, 35131 Padova, Italy.
authors: Alessandro
authors: A
authors: Bertoli
authors: Department of Biomedical Sciences, University of Padova, Via Bassi 58/B, 35131 Padova, Italy; C.N.R. Institute of Neuroscience, University of Padova, Via Bassi 58/B, 35131 Padova, Italy. Electronic address: catia.sorgato@unipd.it.
authors: M Catia
authors: MC
authors: Sorgato
mesh_terms: D000818:Animals; D002417:Cattle; D006801:Humans; D018384:Oxidative Stress; D018621:PrPC Proteins / Q000378:metabolism*; D017096:Prion Diseases / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology; D015398:Signal Transduction
chemical_list: D018621:PrPC Proteins
keywords: Alzheimer's disease; Calcium; Prion disease; Prion protein; Protein misfolding; Signaling pathways