NR AWVE
AU Tatzelt,J.; Schätzl,H.M.
TI Molecular basis of cerebral neurodegeneration in prion diseases
QU The FEBS Journal 2007 Feb; 274(3): 606-11
IA http://www.blackwell-synergy.com/doi/abs/10.1111/j.1742-4658.2007.05633.x
PT journal article; research support, non-u.s. gov't
AB The biochemical nature and the replication of infectious prions have been intensively studied in recent years. Much less is known about the cellular events underlying neuronal dysfunction and cell death. As the cellular function of the normal cellular isoform of prion protein is not exactly known, the impact of gain of toxic function or loss of function, or a combination of both, in prion pathology is still controversial. There is increasing evidence that the normal cellular isoform of the prion protein is a key mediator in prion pathology. Transgenic models were instrumental in dissecting propagation of prions, disease-associated isoforms of prion protein and amyloid production, and induction of neurodegeneration. Four experimental avenues will be discussed here which address scenarios of inappropriate trafficking, folding, or targeting of the prion protein.
ZR 49
MH Animals; Brain/*metabolism/pathology; Humans; Models, Biological; Nerve Degeneration/genetics/metabolism/pathology; Prion Diseases/genetics/*metabolism/pathology; Prions/genetics/*metabolism
AD Jörg Tatzelt (joerg.tatzelt@med.uni-muenchen.de), Department of Biochemistry, Neurobiochemistry, Ludwig-Maximilians-University Munich, Schillerstrasse 44, 80336, München, Germany; Hermann M. Schätzl (schaetzl@lrz.tum.de), Institute of Virology, Technical University of Munich, Trogerstraße 30, 81675 München, Germany
SP englisch
PO England