Caracterização de um receptor para o prion atraves da teoria da hidropaticidade complementar dos amino acidos : evidencias da inteprion-laminina

AUTOR(ES)
DATA DE PUBLICAÇÃO

1996

RESUMO

Prions are slow infectious pathogens which cause transmissible neurodegenerative Jackob disease, diseases in both humans (kuru, Creutzfeldt-Gerstmann-Straussler-Scheinker syndrome and familial fatal insomnia) and animals (scrapie, bovine spongiform encephalopaty, transmissible mink encephalopaty and chronic wasting disease). The infectious prion protein (Prpsc) is an isoform of a cell membrane glycoprotein (Prpc) with unknown function. Prpsc probably induces conformational changes in Prpc resulting in intra and extracellular deposition of insoluble proteinaceous material. This material contains both protease resistant PrP (PrP 27-30) and PrPsc, shows amyloid properties (Congo red staining and birefringence under polarization microscopy) and induces vacuolar degeneration of the brain (PRUSINER, 1991). In this work we demonstrated the existence of a 60-66 neuron surface protein that binds prions in vitro, using the complementary hydropathy concept (BLALOCK e SMITH, 1984). This protein was detected in mouse and rat brain, by immunoperoxidase technique, in the tha1amus, hippocampus and Purkinje cells of the cerebellum, regions of the brain where PrPsc accumulates in prion diseases both infectious or inherited. This fact suggests a role for the 60-66 kDa protein in the pathogenesisof prion diseases. The same regions of the brain were strongly positive for the basement membrane glycoprotein laminin. In addition, we demonstrated that purified PrPsc binds to nondenaturated laminin in ligand blot assays. Our results suggest that the 60-66 kDa cell surface protein can play a role in the prion internalization and that laminin possibly mediates the PrP amyloid formation and deposition

ASSUNTO(S)

sistema nervoso - degeneração receptores nervosos

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