Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies

Autores
Borroni, Maria Virginia; Barrantes, Francisco Jose
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Alzheimer´s disease is the most widespread form of dementia in the elderly. One of the characteristics of this disease is the profound functional deficit of the cholinergic system as a consequence of synaptic loss. Amyloid precursor protein (APP) is a type-I transmembrane protein present in brain synapses and at the neuromuscular junction in the peripheral nervous system. It is developmentally regulated and affects synapse formation and cholinergic transmission. Misprocessing of APP leads to the generation of a highly fibrillogenic peptide, amyloid beta (Aβ), which aggregates and forms amyloid plaques, one of the histological hallmarks of Alzheimer's disease. Aβ can also aggregate at a peripheral synapse, the neuromuscular junction, in the form of intracellular lesions characteristic of the degenerative muscle disease termed sporadic inclusion body myositis. The relationship between the increased production and aggregation of Aβ and the synaptic dysfunction observed in the two disorders is not clear, but the similarities point to the important role of APP in cholinergic synapses. Here we review the biological functions of APP under normal conditions and their dysfunctional counterparts in an attempt to explain the involvement of this protein in cholinergic synaptopathies in general.
Fil: Borroni, Maria Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Unesco; Argentina
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Unesco; Argentina
Materia
Amyloid Precursor Protein
Acetylcholine Receptor
Alzheimer Disease
Amyloid Peptide
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/42475
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Amyloid Precursor Protein in Central and Peripheral Cholinergic SynaptopathiesBorroni, Maria VirginiaBarrantes, Francisco JoseAmyloid Precursor ProteinAcetylcholine ReceptorAlzheimer DiseaseAmyloid Peptidehttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Alzheimer´s disease is the most widespread form of dementia in the elderly. One of the characteristics of this disease is the profound functional deficit of the cholinergic system as a consequence of synaptic loss. Amyloid precursor protein (APP) is a type-I transmembrane protein present in brain synapses and at the neuromuscular junction in the peripheral nervous system. It is developmentally regulated and affects synapse formation and cholinergic transmission. Misprocessing of APP leads to the generation of a highly fibrillogenic peptide, amyloid beta (Aβ), which aggregates and forms amyloid plaques, one of the histological hallmarks of Alzheimer's disease. Aβ can also aggregate at a peripheral synapse, the neuromuscular junction, in the form of intracellular lesions characteristic of the degenerative muscle disease termed sporadic inclusion body myositis. The relationship between the increased production and aggregation of Aβ and the synaptic dysfunction observed in the two disorders is not clear, but the similarities point to the important role of APP in cholinergic synapses. Here we review the biological functions of APP under normal conditions and their dysfunctional counterparts in an attempt to explain the involvement of this protein in cholinergic synaptopathies in general.Fil: Borroni, Maria Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Unesco; ArgentinaFil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Unesco; ArgentinaNova Science Publishers2011-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/42475Borroni, Maria Virginia; Barrantes, Francisco Jose; Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies; Nova Science Publishers; Alzheimer's Disease Research Journal; 3; 1; 5-2011; 11-281935-2514CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.novapublishers.com/catalog/product_info.php?products_id=22186info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:49:19Zoai:ri.conicet.gov.ar:11336/42475instacron: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:34982025-09-03 09:49:19.94CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies
title Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies
spellingShingle Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies
Borroni, Maria Virginia
Amyloid Precursor Protein
Acetylcholine Receptor
Alzheimer Disease
Amyloid Peptide
title_short Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies
title_full Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies
title_fullStr Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies
title_full_unstemmed Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies
title_sort Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies
dc.creator.none.fl_str_mv Borroni, Maria Virginia
Barrantes, Francisco Jose
author Borroni, Maria Virginia
author_facet Borroni, Maria Virginia
Barrantes, Francisco Jose
author_role author
author2 Barrantes, Francisco Jose
author2_role author
dc.subject.none.fl_str_mv Amyloid Precursor Protein
Acetylcholine Receptor
Alzheimer Disease
Amyloid Peptide
topic Amyloid Precursor Protein
Acetylcholine Receptor
Alzheimer Disease
Amyloid Peptide
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Alzheimer´s disease is the most widespread form of dementia in the elderly. One of the characteristics of this disease is the profound functional deficit of the cholinergic system as a consequence of synaptic loss. Amyloid precursor protein (APP) is a type-I transmembrane protein present in brain synapses and at the neuromuscular junction in the peripheral nervous system. It is developmentally regulated and affects synapse formation and cholinergic transmission. Misprocessing of APP leads to the generation of a highly fibrillogenic peptide, amyloid beta (Aβ), which aggregates and forms amyloid plaques, one of the histological hallmarks of Alzheimer's disease. Aβ can also aggregate at a peripheral synapse, the neuromuscular junction, in the form of intracellular lesions characteristic of the degenerative muscle disease termed sporadic inclusion body myositis. The relationship between the increased production and aggregation of Aβ and the synaptic dysfunction observed in the two disorders is not clear, but the similarities point to the important role of APP in cholinergic synapses. Here we review the biological functions of APP under normal conditions and their dysfunctional counterparts in an attempt to explain the involvement of this protein in cholinergic synaptopathies in general.
Fil: Borroni, Maria Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Unesco; Argentina
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Unesco; Argentina
description Alzheimer´s disease is the most widespread form of dementia in the elderly. One of the characteristics of this disease is the profound functional deficit of the cholinergic system as a consequence of synaptic loss. Amyloid precursor protein (APP) is a type-I transmembrane protein present in brain synapses and at the neuromuscular junction in the peripheral nervous system. It is developmentally regulated and affects synapse formation and cholinergic transmission. Misprocessing of APP leads to the generation of a highly fibrillogenic peptide, amyloid beta (Aβ), which aggregates and forms amyloid plaques, one of the histological hallmarks of Alzheimer's disease. Aβ can also aggregate at a peripheral synapse, the neuromuscular junction, in the form of intracellular lesions characteristic of the degenerative muscle disease termed sporadic inclusion body myositis. The relationship between the increased production and aggregation of Aβ and the synaptic dysfunction observed in the two disorders is not clear, but the similarities point to the important role of APP in cholinergic synapses. Here we review the biological functions of APP under normal conditions and their dysfunctional counterparts in an attempt to explain the involvement of this protein in cholinergic synaptopathies in general.
publishDate 2011
dc.date.none.fl_str_mv 2011-05
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/11336/42475
Borroni, Maria Virginia; Barrantes, Francisco Jose; Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies; Nova Science Publishers; Alzheimer's Disease Research Journal; 3; 1; 5-2011; 11-28
1935-2514
CONICET Digital
CONICET
url http://hdl.handle.net/11336/42475
identifier_str_mv Borroni, Maria Virginia; Barrantes, Francisco Jose; Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies; Nova Science Publishers; Alzheimer's Disease Research Journal; 3; 1; 5-2011; 11-28
1935-2514
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.novapublishers.com/catalog/product_info.php?products_id=22186
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 Nova Science Publishers
publisher.none.fl_str_mv Nova Science Publishers
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
_version_ 1842268967793590272
score 13.13397

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