NR AINR
AU Moore,R.C.; Lee,I.Y.; Silverman,G.L.; Harrison,P.M.; Strome,R.; Heinrich,C.; Karunaratne,A.; Pasternak,S.H.; Chishti,M.A.; Liang,Y.; Mastrangelo,P.; Wang,K.; Smit,A.F.; Katamine,S.; Carlson,G.A.; Cohen,F.E.; Prusiner,S.B.; Melton,D.W.; Tremblay,P.; Hood,L.E.; Westaway,D.
TI Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel
QU Journal of Molecular Biology 1999 Oct 1; 292(4): 797-817
PT journal article
AB The novel locus Prnd is 16 kb downstream of the mouse prion protein (PrP) gene Prnp and encodes a 179 residue PrP-like protein designated doppel (Dpl). Prnd generates major transcripts of 1.7 and 2.7 kb as well as some unusual chimeric transcripts generated by intergenic splicing with Prnp. Like PrP, Dpl mRNA is expressed during embryogenesis but, in contrast to PrP, it is expressed minimally in the CNS. Unexpectedly, Dpl is upregulated in the CNS of two PrP-deficient (Prnp(0/0)) lines of mice, both of which develop late-onset ataxia, suggesting that Dpl may provoke neurodegeneration. Dpl is the first PrP-like protein to be described in mammals, and since Dpl seems to cause neurodegeneration similar to PrP, the linked expression of the Prnp and Prnd genes may play a previously unrecognized role in the pathogenesis of prion diseases or other illnesses.
ZR 75 Zitate
MH Amino Acid Motifs; Amino Acid Sequence; Animal; Ataxia/*genetics; Base Sequence; Cell Line; Central Nervous System/cytology/metabolism/pathology; Cloning, Molecular; Embryo/metabolism; Gene Deletion; Glycosylation; Male; Mice; Mice, Inbred BALB C; Mice, Transgenic; Molecular Sequence Data; Prions/chemistry/*genetics/metabolism/physiology; Purkinje Cells/metabolism/pathology; RNA, Messenger/analysis/genetics; Sequence Alignment; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Trans-Splicing/genetics; Up-Regulation
AD Institute for Neurodegenerative Diseases, Departments of Neurology.
SP englisch
PO England