NR ABTK
AU Brown,H.R.; Goller,N.L.; Rudelli,R.D.; Merz,G.S.; Wolfe,G.C.; Wisniewski,H.M.; Robakis,N.K.
TI The mRNA encoding the scrapie agent protein is present in a variety of non-neuronal cells
QU Acta Neuropathologica 1990; 80(1): 1-6
PT journal article
AB PrP 27-30, a unique protease-resistant protein associated with scrapie infectivity, derives from the proteolytic cleavage of a larger precursor encoded by a host gene. To identify sites of PrP biosynthesis, in situ hybridization was done using cloned PrP cDNA as a probe. In rodent brain, PrP mRNA was expressed in neurons, ependymal cells, choroid plexus epithelium, astrocytes, pericytes, endothelial cells and meninges of both scrapie-infected and uninfected animals. PrP mRNA was also detected in vitro in isolated brain microglia cells. Pulmonary cells and heart muscle cells contained high levels of this mRNA. Hybridization was not detected in spleen, confirming earlier RNA blot experiments indicating extremely low levels of PrP mRNA in this tissue. Results indicate that PrP mRNA is a normal component in a variety of non-neuronal tissues and may explain the origin of the amyloid plaques present in the subependymal region of scrapie-infected brain.
IN Die mRNA des Prionproteins wurde in Nagergehirnen in Nervenzellen, ependymalen (auskleidenden) Gliazellen, im Epithelium der Augenadernhaut, Astrozyten, Perizyten, Endothelzellen and äußeren Hirnhäuten gefunden. Aber auch Lungen- und Herzmuskelzellen enthalten große Mengen dieser mRNA.
MH Animal; Brain/*metabolism/pathology; DNA/metabolism; *Gene Expression Regulation; Mice; Mice, Inbred C57BL; Nucleic Acid Hybridization; PrP 27-30 Protein; RNA, Messenger/*genetics/metabolism; Scrapie/*metabolism/pathology; Support, Non-U.S. Gov't; Viral Proteins/*genetics/metabolism
AD New York State Institute for Basic Research in Developmental Disabilities, Staten Island 10314.
SP englisch
PO Westdeutschland