Premium
Synaptic prion protein immuno‐reactivity in the rodent cerebellum
Author(s) -
Haeberlé A.M.,
RibautBarassin C.,
Bombarde G.,
Mariani J.,
Hunsmann G.,
Grassi J.,
Bailly Y.
Publication year - 2000
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/1097-0029(20000701)50:1<66::aid-jemt10>3.0.co;2-3
Subject(s) - neurodegeneration , cerebellum , biology , purkinje cell , prion protein , gene isoform , neuroscience , synapse , microbiology and biotechnology , virology , biochemistry , pathology , disease , medicine , gene
The cellular prion protein PrP c is a neurolemmal glycoprotein essential for the development of the transmissible spongiform encephalopathies. In these neurodegenerative diseases, host PrP c is converted to infectious protease‐resistant isoforms PrP res or prions. Prions provoque predictable and distinctive patterns of PrP res accumulation and neurodegeneration depending on the prion strain and on regional cell‐specific properties modulating PrP c affinity for infectious PrP res in the host brain. Synaptolysis and synaptic accumulation of PrP res during PrP‐related diseases suggests that the synapses could be primary sites able to propagate PrP res 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 PrP c , suggesting that synapse‐specific parameters could influence neuroinvasion and neurodegeneration following cerebral infection by prions. Although the physiological functions of PrP c remain unknown, the concentration of PrP c 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. Microsc. Res. Tech. 50:66–75, 2000. © 2000 Wiley‐Liss, Inc.