Regulation of Amyloid β oligomer binding to neurons and neurotoxicity by the complex prion protein/mGluR5.

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Autor(es): dc.creatorPaiva, Flávio Henrique Beraldo de-
Autor(es): dc.creatorOstapchenko, Valeriy G.-
Autor(es): dc.creatorCaetano, Fabiana Andrade-
Autor(es): dc.creatorGuimarães, André Luiz Sena-
Autor(es): dc.creatorFerretti, Giulia Diniz da Silva-
Autor(es): dc.creatorDaude, Nathalie-
Autor(es): dc.creatorBertram, Lisa-
Autor(es): dc.creatorNogueira, Katiane de Oliveira Pinto Coelho-
Autor(es): dc.creatorSilva, Jerson Lima da-
Autor(es): dc.creatorWestaway, David-
Autor(es): dc.creatorCashman, Neil R.-
Autor(es): dc.creatorMartins, Vilma Regina-
Autor(es): dc.creatorPrado, Vânia Ferreira-
Autor(es): dc.creatorPrado, Marco Antônio Maximo-
Data de aceite: dc.date.accessioned2025-08-21T15:58:25Z-
Data de disponibilização: dc.date.available2025-08-21T15:58:25Z-
Data de envio: dc.date.issued2017-11-29-
Data de envio: dc.date.issued2017-11-29-
Data de envio: dc.date.issued2016-
Fonte completa do material: dc.identifierhttp://www.repositorio.ufop.br/handle/123456789/9205-
Fonte completa do material: dc.identifierhttp://www.jbc.org/content/291/42/21945.long-
Fonte completa do material: dc.identifierhttps://doi.org/10.1074/jbc.M116.738286-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1028965-
Descrição: dc.descriptionThe prion protein (PrPC) has been suggested to operate as a scaffold/ receptor protein in neurons, participating in both physiological and pathological associated events. PrPC, laminin, and metabotropic glutamate receptor 5 (mGluR5) form a protein complex on the plasma membrane that can trigger signaling pathways involved in neuronal differentiation. PrPC and mGluR5 are co-receptors also for -amyloid oligomers(A Os)andhavebeenshowntomodulate toxicity and neuronal death in Alzheimer’s disease. In the present work, we addressed the potential crosstalk between these two signaling pathways, laminin-PrPC-mGluR5 or A O-PrPC- mGluR5, as well as their interplay. Herein, we demonstrated that an existing complex containing PrPC-mGluR5 has an important role in A Obinding and activity in neurons. A peptide mimicking the binding site of laminin onto PrPC (Ln- 1) binds to PrPC and induces intracellular Ca2 increase in neurons via the complex PrPC-mGluR5. Ln- 1 promotes internalization of PrPC and mGluR5 and transiently decreases A O biding to neurons; however, the peptide does not impactA Otoxicity.GiventhatmGluR5 is critical for toxic signaling by A Os and in prion diseases, we tested whether mGlur5 knock-out mice would be susceptible to prion infection. Our results show mild, but significant, effects on disease progression, without affecting survival of mice after infection. These results suggest that PrPC-mGluR5 form a functional response unit by which multiple ligands can trigger signaling. We propose that trafficking of PrPC-mGluR5 may modulate signaling intensity by different PrPC ligands.-
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Idioma: dc.languageen-
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Título: dc.titleRegulation of Amyloid β oligomer binding to neurons and neurotoxicity by the complex prion protein/mGluR5.-
Aparece nas coleções:Repositório Institucional - UFOP

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