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dc.contributor.authorMukherjee A., Morales-Scheihing D., Moreno-Gonzalez I., Gonzalez C., Taylor-Presse K., Mendez N., Shahnawaz M., Gaber A.O., Sabek O.M., Fraga D.W., Soto C.es_CL
dc.contributor.authorSalvadores, Natalia [Centro de Biología Integrativa, Universidad Mayor, Chile]es_CL
dc.date.accessioned2020-08-12T14:11:55Z
dc.date.accessioned2020-08-12T18:13:28Z
dc.date.available2020-08-12T14:11:55Z
dc.date.available2020-08-12T18:13:28Z
dc.date.issued2017es_CL
dc.identifier.citationMukherjee, A., Morales-Scheihing, D., Salvadores, N., Moreno-Gonzalez, I., Gonzalez, C., Taylor-Presse, K., ... & Fraga, D. W. (2017). Induction of IAPP amyloid deposition and associated diabetic abnormalities by a prion-like mechanism. Journal of Experimental Medicine, 214(9), 2591-2610.es_CL
dc.identifier.issn0022-1007es_CL
dc.identifier.issn1540-9538es_CL
dc.identifier.urihttps://rupress.org/jem/article/214/9/2591/42496/Induction-of-IAPP-amyloid-deposition-andes_CL
dc.identifier.urihttps://doi.org/10.1084/jem.20161134es_CL
dc.identifier.urihttp://repositorio.umayor.cl/xmlui/handle/sibum/6931
dc.description.abstractAlthough a large proportion of patients with type 2 diabetes (T2D) accumulate misfolded aggregates composed of the islet amyloid polypeptide (IAPP), its role in the disease is unknown. Here, we show that pancreatic IAPP aggregates can promote the misfolding and aggregation of endogenous IAPP in islet cultures obtained from transgenic mouse or healthy human pancreas. Islet homogenates immunodepleted with anti-IAPP-specific antibodies were not able to induce IAPP aggregation. Importantly, intraperitoneal inoculation of pancreatic homogenates containing IAPP aggregates into transgenic mice expressing human IAPP dramatically accelerates IAPP amyloid deposition, which was accompanied by clinical abnormalities typical of T2D, including hyperglycemia, impaired glucose tolerance, and a substantial reduction on beta cell number and mass. Finally, induction of IAPP deposition and diabetic abnormalities were also induced in vivo by administration of IAPP aggregates prepared in vitro using pure, synthetic IAPP. Our findings suggest that some of the pathologic and clinical alterations of T2D might be transmissible through a similar mechanism by which prions propagate in prion diseases.es_CL
dc.description.sponsorshipThe Integrated Microscopy Core was provided with funding from the Dan L. Duncan Cancer Center, Baylor College of Medicine, and the John S. Dunn Gulf Coast Consortium for Chemical Genomics for providing the electron microscopy micrographs. This study was supported in part by the Jeane B. Kempner postdoctoral fellowship awarded to A. Mukherjee.es_CL
dc.format.extentArtículo original
dc.language.isoeses_CL
dc.publisherRockefeller University Presses_CL
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourceJournal of Experimental Medicine, 2017. 214(9): p: 2591-2610
dc.titleInduction of IAPP amyloid deposition and associated diabetic abnormalities by a prion-like mechanismes_CL
dc.typeArtículo o paperes_CL
umayor.facultadFacultad de Ciencias
umayor.indizadorCOT
umayor.politicas.sherpa/romeoRoMEO GREEN journal (Se puede archivar el pre-print y el post-print o versión de editor/PDF). Disponible en: http://sherpa.ac.uk/romeo/index.phpes_CL
umayor.indexadoWOSes_CL
umayor.indexadoSCOPUSes_CL
dc.identifier.doiDOI: 10.1084/jem.20161134es_CL]
umayor.indicadores.wos-(cuartil)Q1es_CL
umayor.indicadores.scopus-(scimago-sjr)7,76es_CL
umayor.indicadores.scopus-(scimago-sjr)ÍNDICE H: 5es_CL


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