NR AFDV
AU Harris,D.A.; Lele,P.; Snider,W.D.
TI Localization of the mRNA for a chicken prion protein by in situ hybridization
QU Proceedings of the National Academy of Sciences of the United States of America 1993 May 1; 90(9): 4309-13
PT journal article
AB The infectious agent (prion) responsible for transmissible spongiform encephalopathies in humans and animals is composed primarily of a 33- to 35-kDa glycoprotein called PrPsc (scrapie isoform of prion protein), which is a posttranslationally modified form of the normal cell-surface protein PrPc. Little is known about the function of PrPc. Interestingly, chPrP, the chicken homologue of PrPc, copurifies with a factor from brain that stimulates synthesis of acetylcholine receptors on skeletal muscle cells. Using in situ hybridization, we report here that chPrP mRNA is widely distributed in cholinergic and noncholinergic neurons throughout the adult central nervous system, including those in the telencephalic striata, thalamus and hypothalamus, optic tectum, medulla, cerebellum, and spinal cord. The mRNA is present in the brain and spinal cord as early as embryonic day 6 and is also found in dorsal root ganglia, retina, intestine, and heart. Our data suggest that if chPrP serves to regulate acetylcholine receptor number on postsynaptic targets, this is not its only function. It is likely that the protein plays a more widespread role in the central nervous system and perhaps elsewhere, possibly one related to intercellular communication, adhesion, or recognition. The chicken embryo represents an attractive experimental system in which to investigate the normal developmental function of PrPc.
IN Das infektiöse Agens, das bei Mensch und Tier spongiforme Encephalopathien überträgt, besteht hauptsächlich aus dem glykosylierten Prionprotein mit einem scheinbaren Molekulargewicht von 33-35 kDalton bei der Scrapieisoform. Es handelt sich um eine posttranslational modifizierte Form eines Membranproteins, welches bei Hühnern in cholinergen und nichtcholinergen Neuronen im gesamten Zentralnervensystem vorkommt. Seine mRNA ist schon in Gehirn und Rückenmark 6 Tage alter Embryonen und auch in Rückenmarksganglien, Retina, Dünndarm und Herz ist sie zu finden. Möglicherweise stimuliert das Hühnerprionprotein die Synthese von Acetylcholinrezeptoren auf Skelettmuskelzellen.
MH Animal; Antisense Elements (Genetics); Brain/cytology/*physiology; Cerebellum/cytology/physiology; Chick Embryo; Chickens; Diencephalon/cytology/physiology; Human; In Situ Hybridization; Medulla Oblongata/cytology/physiology; Prions/analysis/*genetics; RNA Probes; RNA, Messenger/*analysis/genetics; Spinal Cord/cytology/*physiology; Superior Colliculus/cytology/physiology; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Telencephalon/cytology/physiology
AD Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110.
SP englisch
PO USA