NR AFDX
AU Harris,D.A.; Falls,D.L.; Johnson,F.A.; Fischbach,G.D.
TI A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity
QU Proceedings of the National Academy of Sciences of the United States of America 1991 Sep 1; 88(17): 7664-8
PT journal article
AB The mammalian prion protein (PrPc) is a cellular protein of unknown function, an altered isoform of which (PrPsc) is a component of the infectious particle (prion) thought to be responsible for spongiform encephalopathies in humans and animals. We report here the isolation of a cDNA that encodes a chicken protein that is homologous to PrPc. This chicken prion-like protein (ch-PrLP) is identical to the mouse PrP at 33% of its amino acid positions, including an uninterrupted stretch of 24 identical residues, and it displays the same structural domains. In addition, ch-PrLP, like its mammalian counterpart, is attached to the cell surface by a glycosyl-phosphatidylinositol anchor. We find that ch-PrLP is the major protein in preparations of an acetylcholine receptor-inducing activity that has been purified greater than 10(6)-fold from brain on the basis of its ability to stimulate synthesis of nicotinic receptors by cultured myotubes. The ch-PrLP gene is expressed in the spinal cord and brain as early as embryonic day 6; and in the spinal cord, the protein appears to be concentrated in motor neurons. Our results therefore raise the possibility that prion proteins serve normally to regulate the chemoreceptor number at the neuromuscular junction and perhaps in the central nervous system as well.
IN Eine Hühner-cDNA für ein Prionprotein wurde isoliert und sequenziert. Das Hühnerprionprotein stimmt an 33% der Positionen und auf einer Strecke von 24 Aminosäuren vollständig mit dem bereits bekannten Mausprionprotein überein. Das Muster der Domänen und der Glycosylphosphatidylinositol-Anker sind gleich. Das Hühnerprionprotein scheint eine acetylcholinerezeptorinduzierende Wirkung zu besitzen. Das Hühnerprionprotein wird im Gehirn und im Rückenmark schon am 6. Tag der Embryogenese exprimiert. Im Rückenmark scheint es besonders auf Motoneuronen vorzukommen und reguliert möglicherweise die Zahl der postsynaptischen Rezeptoren.
MH Amino Acid Sequence; Animal; Base Sequence; Blotting, Northern; Brain/*physiology; Cells, Cultured; Chick Embryo; Chickens; Comparative Study; DNA/genetics/isolation & purification; Gene Library; Mice; Molecular Sequence Data; Muscles/*physiology; Oligonucleotide Probes; Polymerase Chain Reaction/methods; PrPsc Proteins; Prions/genetics/isolation & purification; RNA/genetics/isolation & purification; RNA, Messenger/analysis/genetics; Receptors, Nicotinic/*biosynthesis; Restriction Mapping; Sequence Homology, Nucleic Acid; Spinal Cord/physiology; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Transfection; Viral Proteins/genetics/*isolation & purification
AD Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, MO 63110.
SP englisch
PO USA
OR Prion-Krankheiten H
ZF kritische Zusammenfassung von Roland Heynkes