NR AEZU
AU Haeberle,A.M.; Ribaut-Barassin,C.; Bombarde,G.; Mariani,J.; Hunsmann,G.; Grassi,J.; Bailly,Y.
TI Synaptic prion protein immuno-reactivity in the rodent cerebellum
QU Microscopy Research and Technique 2000 Jul 1; 50(1): 66-75
PT journal article
AB The cellular prion protein PrPc is a neurolemmal glycoprotein essential for the development of the transmissible spongiform encephalopathies. In these neurodegenerative diseases, host PrPc is converted to infectious protease-resistant isoforms PrPres or prions. Prions provoque predictable and distinctive patterns of PrPres accumulation and neurodegeneration depending on the prion strain and on regional cell-specific properties modulating PrPc affinity for infectious PrPres in the host brain. Synaptolysis and synaptic accumulation of PrPres during PrP-related diseases suggests that the synapses could be primary sites able to propagate PrPres and neurodegeneration in the central nervous system. In the rodent cerebellum, the present light and electron microscopic immuno-cytochemical analysis shows that distinct types of synapses display differential expression of PrPc, suggesting that synapse-specific parameters could influence neuroinvasion and neurodegeneration following cerebral infection by prions. Although the physiological functions of PrPc remain unknown, the concentration of PrPc almost exclusively at the Purkinje cell synapses in the cerebellum suggests its critical involvement in the synaptic relationships between cerebellar neurons in agreement with their known vulnerability to PrP deficiencies.
MH Animal; Antibodies, Monoclonal; Cerebellum/*metabolism/ultrastructure; Fixatives; Hamsters; Immunohistochemistry/methods; Mesocricetus; Mice; Mice, Inbred C57BL; Microscopy, Immunoelectron; PrPc Proteins/*analysis/deficiency; Prion Diseases/metabolism; Protein Isoforms/analysis; Support, Non-U.S. Gov't; Synapses/*metabolism/ultrastructure
AD Laboratoire de Neurobiologie Cellulaire UPR 9009 CNRS 5, rue Blaise Pascal, 67084 Strasbourg, France.
SP englisch
PO USA