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A plausible function of the prion protein: conjectures and a hypothesis
Author(s) -
Abdulla Yousef H.
Publication year - 2001
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.1064
Subject(s) - prion protein , biology , microbiology and biotechnology , function (biology) , cleavage (geology) , amyloid precursor protein secretase , amyloid precursor protein , neuroscience , biochemistry , alzheimer's disease , medicine , paleontology , disease , fracture (geology)
Amyloid beta precursor protein (APP) and prion protein (PrP) are cell membrane elements implicated in neurodegenerative diseases. Both proteins undergo endoproteolysis. Evidence is adduced from the literature hinting that the process in the two proteins could be related, their functions may overlap and their distributions coincide. It is proposed that PrP catalyses its own cleavage, the C‐terminal fragment functions as an α secretase and the N‐terminal segment chaperones the active site; the α secretase releases anticoagulant and neurotrophic ectodomains from APP. The proposals explain some features of spongiform encephalopathies. BioEssays 23:456–462, 2001. © 2001 John Wiley & Sons, Inc.