Data/hora: 06/06/2024 02:26:06

Provedor de dados: 	56	
País: 	Brazil	
Título: 	A receptor for infectious and cellular prion protein	
Autores: 	Martins,V.R.	
Data: 	1999-07-01	
Ano: 	1999	
Palavras-chave: 	Prion; Transmissible spongiform encephalopathies; PrPc; Receptor.	
Resumo: 	Prions are an unconventional form of infectious agents composed only of protein and involved in transmissible spongiform encephalopathies in humans and animals. The infectious particle is composed by PrPsc which is an isoform of a normal cellular glycosyl-phosphatidylinositol (GPI) anchored protein, PrPc, of unknown function. The two proteins differ only in conformation, PrPc is composed of 40% &lt;FONT FACE="Symbol"&gt;a&lt;/FONT&gt; helix while PrPsc has 60% ß-sheet and 20% &lt;FONT FACE="Symbol"&gt;a&lt;/FONT&gt; helix structure. The infection mechanism is trigged by interaction of PrPsc with cellular prion protein causing conversion of the latter's conformation. Therefore, the infection spreads because new PrPsc molecules are generated exponentially from the normal PrPc. The accumulation of insoluble PrPsc is probably one of the events that lead to neuronal death. Conflicting data in the literature showed that PrPc internalization is mediated either by clathrin-coated pits or by caveolae-like membranous domains. However, both pathways seem to require a third protein (a receptor or a prion-binding protein) either to make the connection between the GPI-anchored molecule to clathrin or to convert PrPc into PrPsc. We have recently characterized a 66-kDa membrane receptor which binds PrPc in vitro and in vivo and mediates the neurotoxicity of a human prion peptide. Therefore, the receptor should have a role in the pathogenesis of prion-related diseases and in the normal cellular process. Further work is necessary to clarify the events triggered by the association of PrPc/PrPsc with the receptor.	
Tipo: 	Info:eu-repo/semantics/article	
Idioma: 	Inglês	
Identificador: 	http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000700009	
Editor: 	Associação Brasileira de Divulgação Científica	
Relação: 	10.1590/S0100-879X1999000700009	
Formato: 	text/html	
Fonte: 	Brazilian Journal of Medical and Biological Research  v.32 n.7 1999	
Fonte: 	info:eu-repo/semantics/openAccess