Protein misfolding, signaling abnormalities and altered fast axonal transport: Implications for Alzheimer and Prion diseases
- Autores
- Zamponi, Emiliano; Pigino, Gustavo Fernando
- Año de publicación
- 2019
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Histopathological studies revealed that progressive neuropathies including Alzheimer, and Prion diseases among others, include accumulations of misfolded proteins intracellularly, extracellularly, or both. Experimental evidence suggests that among the accumulated misfolded proteins, small soluble oligomeric conformers represent the most neurotoxic species. Concomitant phenomena shared by different protein misfolding diseases includes alterations in phosphorylation-based signaling pathways synaptic dysfunction, and axonal pathology, but mechanisms linking these pathogenic features to aggregated neuropathogenic proteins remain unknown. Relevant to this issue, results from recent work revealed inhibition of fast axonal transport (AT) as a novel toxic effect elicited by oligomeric forms of amyloid beta and cellular prion protein PrPC, signature pathological proteins associated with Alzheimer and Prion diseases, respectively. Interestingly, the toxic effect of these oligomers was fully prevented by pharmacological inhibitors of casein kinase 2 (CK2), a remarkable discovery with major implications for the development of pharmacological target-driven therapeutic intervention for Alzheimer and Prion diseases.
Fil: Zamponi, Emiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Pigino, Gustavo Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina - Materia
-
CASEIN KINASE 2
FAST AXONAL TRANSPORT
KINESIN-1
PRION PROTEIN
PROTEIN MISFOLDING
SIGNALING
SYNAPTIC DYSFUCTION - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/128428
Ver los metadatos del registro completo
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Protein misfolding, signaling abnormalities and altered fast axonal transport: Implications for Alzheimer and Prion diseasesZamponi, EmilianoPigino, Gustavo FernandoCASEIN KINASE 2FAST AXONAL TRANSPORTKINESIN-1PRION PROTEINPROTEIN MISFOLDINGSIGNALINGSYNAPTIC DYSFUCTIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Histopathological studies revealed that progressive neuropathies including Alzheimer, and Prion diseases among others, include accumulations of misfolded proteins intracellularly, extracellularly, or both. Experimental evidence suggests that among the accumulated misfolded proteins, small soluble oligomeric conformers represent the most neurotoxic species. Concomitant phenomena shared by different protein misfolding diseases includes alterations in phosphorylation-based signaling pathways synaptic dysfunction, and axonal pathology, but mechanisms linking these pathogenic features to aggregated neuropathogenic proteins remain unknown. Relevant to this issue, results from recent work revealed inhibition of fast axonal transport (AT) as a novel toxic effect elicited by oligomeric forms of amyloid beta and cellular prion protein PrPC, signature pathological proteins associated with Alzheimer and Prion diseases, respectively. Interestingly, the toxic effect of these oligomers was fully prevented by pharmacological inhibitors of casein kinase 2 (CK2), a remarkable discovery with major implications for the development of pharmacological target-driven therapeutic intervention for Alzheimer and Prion diseases.Fil: Zamponi, Emiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Pigino, Gustavo Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFrontiers Media S.A.2019-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/128428Zamponi, Emiliano; Pigino, Gustavo Fernando; Protein misfolding, signaling abnormalities and altered fast axonal transport: Implications for Alzheimer and Prion diseases; Frontiers Media S.A.; Frontiers in Cellular Neuroscience; 13; 7-2019; 1-51662-5102CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/article/10.3389/fncel.2019.00350/fullinfo:eu-repo/semantics/altIdentifier/doi/10.3389/fncel.2019.00350info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:08:08Zoai:ri.conicet.gov.ar:11336/128428instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:08:08.251CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Protein misfolding, signaling abnormalities and altered fast axonal transport: Implications for Alzheimer and Prion diseases |
title |
Protein misfolding, signaling abnormalities and altered fast axonal transport: Implications for Alzheimer and Prion diseases |
spellingShingle |
Protein misfolding, signaling abnormalities and altered fast axonal transport: Implications for Alzheimer and Prion diseases Zamponi, Emiliano CASEIN KINASE 2 FAST AXONAL TRANSPORT KINESIN-1 PRION PROTEIN PROTEIN MISFOLDING SIGNALING SYNAPTIC DYSFUCTION |
title_short |
Protein misfolding, signaling abnormalities and altered fast axonal transport: Implications for Alzheimer and Prion diseases |
title_full |
Protein misfolding, signaling abnormalities and altered fast axonal transport: Implications for Alzheimer and Prion diseases |
title_fullStr |
Protein misfolding, signaling abnormalities and altered fast axonal transport: Implications for Alzheimer and Prion diseases |
title_full_unstemmed |
Protein misfolding, signaling abnormalities and altered fast axonal transport: Implications for Alzheimer and Prion diseases |
title_sort |
Protein misfolding, signaling abnormalities and altered fast axonal transport: Implications for Alzheimer and Prion diseases |
dc.creator.none.fl_str_mv |
Zamponi, Emiliano Pigino, Gustavo Fernando |
author |
Zamponi, Emiliano |
author_facet |
Zamponi, Emiliano Pigino, Gustavo Fernando |
author_role |
author |
author2 |
Pigino, Gustavo Fernando |
author2_role |
author |
dc.subject.none.fl_str_mv |
CASEIN KINASE 2 FAST AXONAL TRANSPORT KINESIN-1 PRION PROTEIN PROTEIN MISFOLDING SIGNALING SYNAPTIC DYSFUCTION |
topic |
CASEIN KINASE 2 FAST AXONAL TRANSPORT KINESIN-1 PRION PROTEIN PROTEIN MISFOLDING SIGNALING SYNAPTIC DYSFUCTION |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Histopathological studies revealed that progressive neuropathies including Alzheimer, and Prion diseases among others, include accumulations of misfolded proteins intracellularly, extracellularly, or both. Experimental evidence suggests that among the accumulated misfolded proteins, small soluble oligomeric conformers represent the most neurotoxic species. Concomitant phenomena shared by different protein misfolding diseases includes alterations in phosphorylation-based signaling pathways synaptic dysfunction, and axonal pathology, but mechanisms linking these pathogenic features to aggregated neuropathogenic proteins remain unknown. Relevant to this issue, results from recent work revealed inhibition of fast axonal transport (AT) as a novel toxic effect elicited by oligomeric forms of amyloid beta and cellular prion protein PrPC, signature pathological proteins associated with Alzheimer and Prion diseases, respectively. Interestingly, the toxic effect of these oligomers was fully prevented by pharmacological inhibitors of casein kinase 2 (CK2), a remarkable discovery with major implications for the development of pharmacological target-driven therapeutic intervention for Alzheimer and Prion diseases. Fil: Zamponi, Emiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina Fil: Pigino, Gustavo Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina |
description |
Histopathological studies revealed that progressive neuropathies including Alzheimer, and Prion diseases among others, include accumulations of misfolded proteins intracellularly, extracellularly, or both. Experimental evidence suggests that among the accumulated misfolded proteins, small soluble oligomeric conformers represent the most neurotoxic species. Concomitant phenomena shared by different protein misfolding diseases includes alterations in phosphorylation-based signaling pathways synaptic dysfunction, and axonal pathology, but mechanisms linking these pathogenic features to aggregated neuropathogenic proteins remain unknown. Relevant to this issue, results from recent work revealed inhibition of fast axonal transport (AT) as a novel toxic effect elicited by oligomeric forms of amyloid beta and cellular prion protein PrPC, signature pathological proteins associated with Alzheimer and Prion diseases, respectively. Interestingly, the toxic effect of these oligomers was fully prevented by pharmacological inhibitors of casein kinase 2 (CK2), a remarkable discovery with major implications for the development of pharmacological target-driven therapeutic intervention for Alzheimer and Prion diseases. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-07 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/128428 Zamponi, Emiliano; Pigino, Gustavo Fernando; Protein misfolding, signaling abnormalities and altered fast axonal transport: Implications for Alzheimer and Prion diseases; Frontiers Media S.A.; Frontiers in Cellular Neuroscience; 13; 7-2019; 1-5 1662-5102 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/128428 |
identifier_str_mv |
Zamponi, Emiliano; Pigino, Gustavo Fernando; Protein misfolding, signaling abnormalities and altered fast axonal transport: Implications for Alzheimer and Prion diseases; Frontiers Media S.A.; Frontiers in Cellular Neuroscience; 13; 7-2019; 1-5 1662-5102 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/article/10.3389/fncel.2019.00350/full info:eu-repo/semantics/altIdentifier/doi/10.3389/fncel.2019.00350 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Frontiers Media S.A. |
publisher.none.fl_str_mv |
Frontiers Media S.A. |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1846781407541592064 |
score |
13.179806 |