Role of lipid rafts and GM1 in the segregation and processing of prion protein.

The prion protein (PrPC) is highly expressed within the nervous system. Similar to other GPI-anchored proteins, PrPC is found in lipid rafts, membrane domains enriched in cholesterol and sphingolipids. PrPC raft association, together with raft lipid composition, appears essential for the conversion...

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Autores principales:	Laura Botto, Diana Cunati, Silvia Coco, Silvia Sesana, Alessandra Bulbarelli, Emiliano Biasini, Laura Colombo, Alessandro Negro, Roberto Chiesa, Massimo Masserini, Paola Palestini
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c783cfa3e4df47d18f9db75a79038017
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spelling	oai:doaj.org-article:c783cfa3e4df47d18f9db75a790380172021-11-18T08:18:09ZRole of lipid rafts and GM1 in the segregation and processing of prion protein.1932-620310.1371/journal.pone.0098344https://doaj.org/article/c783cfa3e4df47d18f9db75a790380172014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24859148/?tool=EBIhttps://doaj.org/toc/1932-6203The prion protein (PrPC) is highly expressed within the nervous system. Similar to other GPI-anchored proteins, PrPC is found in lipid rafts, membrane domains enriched in cholesterol and sphingolipids. PrPC raft association, together with raft lipid composition, appears essential for the conversion of PrPC into the scrapie isoform PrPSc, and the development of prion disease. Controversial findings were reported on the nature of PrPC-containing rafts, as well as on the distribution of PrPC between rafts and non-raft membranes. We investigated PrPC/ganglioside relationships and their influence on PrPC localization in a neuronal cellular model, cerebellar granule cells. Our findings argue that in these cells at least two PrPC conformations coexist: in lipid rafts PrPC is present in the native folding (α-helical), stabilized by chemico-physical condition, while it is mainly present in other membrane compartments in a PrPSc-like conformation. We verified, by means of antibody reactivity and circular dichroism spectroscopy, that changes in lipid raft-ganglioside content alters PrPC conformation and interaction with lipid bilayers, without modifying PrPC distribution or cleavage. Our data provide new insights into the cellular mechanism of prion conversion and suggest that GM1-prion protein interaction at the cell surface could play a significant role in the mechanism predisposing to pathology.Laura BottoDiana CunatiSilvia CocoSilvia SesanaAlessandra BulbarelliEmiliano BiasiniLaura ColomboAlessandro NegroRoberto ChiesaMassimo MasseriniPaola PalestiniPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 5, p e98344 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Laura Botto Diana Cunati Silvia Coco Silvia Sesana Alessandra Bulbarelli Emiliano Biasini Laura Colombo Alessandro Negro Roberto Chiesa Massimo Masserini Paola Palestini Role of lipid rafts and GM1 in the segregation and processing of prion protein.
description	The prion protein (PrPC) is highly expressed within the nervous system. Similar to other GPI-anchored proteins, PrPC is found in lipid rafts, membrane domains enriched in cholesterol and sphingolipids. PrPC raft association, together with raft lipid composition, appears essential for the conversion of PrPC into the scrapie isoform PrPSc, and the development of prion disease. Controversial findings were reported on the nature of PrPC-containing rafts, as well as on the distribution of PrPC between rafts and non-raft membranes. We investigated PrPC/ganglioside relationships and their influence on PrPC localization in a neuronal cellular model, cerebellar granule cells. Our findings argue that in these cells at least two PrPC conformations coexist: in lipid rafts PrPC is present in the native folding (α-helical), stabilized by chemico-physical condition, while it is mainly present in other membrane compartments in a PrPSc-like conformation. We verified, by means of antibody reactivity and circular dichroism spectroscopy, that changes in lipid raft-ganglioside content alters PrPC conformation and interaction with lipid bilayers, without modifying PrPC distribution or cleavage. Our data provide new insights into the cellular mechanism of prion conversion and suggest that GM1-prion protein interaction at the cell surface could play a significant role in the mechanism predisposing to pathology.
format	article
author	Laura Botto Diana Cunati Silvia Coco Silvia Sesana Alessandra Bulbarelli Emiliano Biasini Laura Colombo Alessandro Negro Roberto Chiesa Massimo Masserini Paola Palestini
author_facet	Laura Botto Diana Cunati Silvia Coco Silvia Sesana Alessandra Bulbarelli Emiliano Biasini Laura Colombo Alessandro Negro Roberto Chiesa Massimo Masserini Paola Palestini
author_sort	Laura Botto
title	Role of lipid rafts and GM1 in the segregation and processing of prion protein.
title_short	Role of lipid rafts and GM1 in the segregation and processing of prion protein.
title_full	Role of lipid rafts and GM1 in the segregation and processing of prion protein.
title_fullStr	Role of lipid rafts and GM1 in the segregation and processing of prion protein.
title_full_unstemmed	Role of lipid rafts and GM1 in the segregation and processing of prion protein.
title_sort	role of lipid rafts and gm1 in the segregation and processing of prion protein.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/c783cfa3e4df47d18f9db75a79038017
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Role of lipid rafts and GM1 in the segregation and processing of prion protein.

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