NR AVGL
AU Schwarz,A.; Burwinkel,M.; Riemer,C.; Schultz,J.; Baier,M.
TI Unchanged scrapie pathology in brain tissue of tyrosine kinase Fyn-deficient mice
QU Neuro-degenerative Diseases 2004; 1(6): 266-8
PT journal article
AB Fyn is a 59-kDa member of the Src family of tyrosine kinases synthesized on cytosolic polysomes and then targeted to the plasma membrane where it clusters in caveolae-like membrane microdomains. The cellular isoform of the prion protein (PrP) has also been identified to be a caveolar constituent and to participate in signal transduction events concerning cell survival and differentiation via recruitment of Fyn. We studied the scrapie infection of mice deficient for Fyn (Fyn(-/-)) to clarify the role of Fyn in an in vivo model of transmissible spongiforme encephalopathies. Fyn(-/-) mice died on average 9 days earlier than wild-type control mice, but no differences were seen regarding activation of astrocytes, vacuolization of the neuropil, and accumulation of misfolded prion protein. The experimental model suggests that a deficiency for Fyn is detrimental in prion diseases, although it has no major effect on the clinical course of an experimental prion infection of the CNS.
MH Animals; Biological Markers/metabolism; Brain/*enzymology/pathology; Female; Genetic Predisposition to Disease/*genetics; Glial Fibrillary Acidic Protein/metabolism; Gliosis/genetics/metabolism/pathology; Mice; Mice, Inbred C57BL; Mice, Knockout; Neuropil/enzymology/pathology; PrPsc Proteins/*metabolism; Proto-Oncogene Proteins c-fyn/*genetics; Research Support, Non-U.S. Gov't; Scrapie/*enzymology/*genetics/pathology
AD Project Neurodegenerative Diseases, Robert Koch Institute, Berlin, Germany.
SP englisch
PO Schweiz