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Titolo:
Synaptic prion protein immuno-reactivity in the rodent cerebellum
Autore:
Haeberle, AM; Ribaut-Barassin, C; Bombarde, G; Mariani, J; Hunsmann, G; Grassi, J; Bailly, Y;
Indirizzi:
UPR 9009 CNRS, Lab Neurobiol Cellulaire, F-67084 Strasbourg, France UPR 9009 CNRS Strasbourg France F-67084 aire, F-67084 Strasbourg, France Univ Paris 06, Inst Neurosci, Lab DVSM, F-75005 Paris, France Univ Paris 06 Paris France F-75005 osci, Lab DVSM, F-75005 Paris, France UMR CNRS 7624, F-75005 Paris, France UMR CNRS 7624 Paris France F-75005UMR CNRS 7624, F-75005 Paris, France Deutsch Primate Zentrum GMBH, D-37077 Gottingen, Germany Deutsch Primate Zentrum GMBH Gottingen Germany D-37077 ottingen, Germany CEA, Serv Pharmacol & Immunol, F-91191 Gif Sur Yvette, France CEA Gif SurYvette France F-91191 mmunol, F-91191 Gif Sur Yvette, France
Titolo Testata:
MICROSCOPY RESEARCH AND TECHNIQUE
fascicolo: 1, volume: 50, anno: 2000,
pagine: 66 - 75
SICI:
1059-910X(20000701)50:1<66:SPPIIT>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
CREUTZFELDT-JAKOB-DISEASE; SCRAPIE-INFECTED MICE; NULL MICE; ULTRASTRUCTURAL-LOCALIZATION; SPONGIFORM ENCEPHALOPATHIES; MONOCLONAL-ANTIBODIES; NERVOUS-SYSTEM; MOUSE SCRAPIE; PRP0/0 MICE; BRAIN;
Keywords:
PrPc; synapse; Purkinje cell; immuno-cytochemistry; ultrastructure; mouse; hamster;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
77
Recensione:
Indirizzi per estratti:
Indirizzo: Bailly, Y UPR 9009 CNRS, Lab Neurobiol Cellulaire, 5 Rue Blaise Pascal, F-67084 Strasbourg, France UPR 9009 CNRS 5 Rue Blaise Pascal Strasbourg France F-67084 nce
Citazione:
A.M. Haeberle et al., "Synaptic prion protein immuno-reactivity in the rodent cerebellum", MICROSC RES, 50(1), 2000, pp. 66-75

Abstract

The cellular prion protein PrPc is a neurolemmal glycoprotein essential far the development of the transmissible spongiform encephalapathies. 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. Ln the rodent cerebellum, the present Light andelectron microscopic immuno-cytochemical analysis shows that distinct types of synapses display differential expression of PrPc, suggesting that synapse-specific parameters could influence neuro-invasion and neurodegeneration following cerebral infection by prions. Although the physiological functions of PrPc remain unknown, the concentration of PrPc almost exclusively atthe 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. (C) 2000 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 02:43:01