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Titolo:
Cellular and subcellular morphological localization of normal prion protein in rodent cerebellum
Autore:
Laine, J; Marc, ME; Sy, MS; Axelrad, H;
Indirizzi:
Univ Paris 06, Lab Cerebellar Neurobiol, F-75013 Paris, France Univ Paris 06 Paris France F-75013 llar Neurobiol, F-75013 Paris, France Case Western Reserve Univ, Sch Med, Inst Pathol, Cleveland, OH 44106 USA Case Western Reserve Univ Cleveland OH USA 44106 Cleveland, OH 44106 USA
Titolo Testata:
EUROPEAN JOURNAL OF NEUROSCIENCE
fascicolo: 1, volume: 14, anno: 2001,
pagine: 47 - 56
SICI:
0953-816X(200107)14:1<47:CASMLO>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
IN-SITU HYBRIDIZATION; GPI-ANCHORED PROTEINS; CULTURED-CELLS; MESSENGER-RNA; ULTRASTRUCTURAL-LOCALIZATION; SCRAPIE INFECTION; MURINE SCRAPIE; PRP; BRAIN; MICE;
Keywords:
cellular prion protein; electron microscopy; preembedding immunocytochemistry;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
58
Recensione:
Indirizzi per estratti:
Indirizzo: Laine, J Univ Paris 06, Lab Cerebellar Neurobiol, 91 Bd Hop, F-75013 Paris, France Univ Paris 06 91 Bd Hop Paris France F-75013 75013 Paris, France
Citazione:
J. Laine et al., "Cellular and subcellular morphological localization of normal prion protein in rodent cerebellum", EUR J NEURO, 14(1), 2001, pp. 47-56

Abstract

Normal cellular prion protein, a necessary protagonist in fatal neurodegenerative prion diseases, was mapped in rodent cerebellum to establish its cellular and ultrastuctural localization. Existing morphological data about native prion protein distribution in brain tissues remain, indeed, contradictory and do not fit with biochemical and cell biological results. Using ultrastructural preembedding immunocytochemistry and a monoclonal anti-mouse prion protein antibody, this report shows that cellular prion protein is present in all cortico-cerebellar and deep nuclei neuronal cell types, as wellas in all glial cell types. The heaviest expression appears on parallel fibres and astrocytic processes. The protein is exclusively located on the outer cell membrane and in Golgi and endosomal intracytoplasmic organelles, with no cytoplasmic or synaptic vesicle labelling. Most important, and in contrast with previous ultrastructural data, cellular prion protein is shown to be distributed on all portions of neurons, without any preferential synaptic targeting. The present morphological report shows, for the first time in vivo, that the cellular prion protein is present on the entire cell surface membrane of all neuronal and glial cell types of the rat cerebellum. This ubiquitous presence supports the notion that prion protein has a generalized cellular function in brain tissue rather than a specialized role restricted to synaptic transmission.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 12:59:54