NR AVYX
AU Sorgato,M.C.; Bertoli,A.
TI Physiopathologic implications of the structural and functional domains of the prion protein
QU Italian Journal of Biochemistry 2006 Sep-Dec; 55(3-4): 222-31
PT journal article; research support, non-u.s. gov't; review
AB Prion diseases are invariably fatal neurodegenerative disorders affecting man and various animal species. A large body of evidence supports the notion that the causative agent of these diseases is the prion, which, devoid of nucleic acids, is composed largely, if not entirely, of a conformationally abnormal isoform (PrPsc of the cellular prion protein (PrPc). PrPc is a highly conserved and ubiquitously expressed sialoglycoprotein, the normal function of which is, however, still ill defined. Several modules have been recognised in PrPc structure. Their extensive analysis by different experimental approaches, including transgenic animal models, has allowed to assigning to several modules a putative role in PrPc physiology. Concurrently, it has underscored the possibility that alteration of specific domains may determine the switching from a beneficial role of PrPc into one that becomes detrimental to neurons, and/or promote the conversion of PrPc into the pathogenic PrPsc conformer.
ZR 78
MH Amino Acid Sequence; Animals; Conserved Sequence; Copper/metabolism; Humans; Membrane Microdomains/physiology; PrPc Proteins/*chemistry/*physiology; PrPsc Proteins/metabolism; Prions/physiology; Protein Structure, Tertiary; Repetitive Sequences, Nucleic Acid
AD Dipartimento di Chimica Biologica, Istituto CNR di Neuroscienze, Universita di Padova, Padova, Italia. catia.sorgato@unipd.it
SP englisch
PO Italien