Role of mitochondrial heat-shock proteins and immunophilins in neurodegenerative diseases

Autores
Daneri Becerra, Cristina del Rosario; Ciucci, Sol Micaela; Mazaira, Gisela Ileana; Galigniana, Mario Daniel
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Pathophysiologic conditions of neurodegenerative diseases are unquestionably related to protein misfolding. The accumulation of misfolded proteins into relatively ordered structures such as fibrillar intracellular and extracellular amyloids results in tissue lesions that lead to neuronal loss and brain damage. In these pathologies, the occurrence of protein aggregates suggests certain inefficient or insufficient cellular response of those molecular chaperones that should properly assist the folding of the client proteins. In this regard, all the experimental models for neurodegenerative diseases have demonstrated that the overexpression of molecular chaperones provide effective neuroprotection. A subset of these molecular chaperones corresponds to a group of proteins that exhibit peptidylprolyl isomerase enzymatic activity, the immunophilins. Most of the family members of the latter group were first described as responsible of the immunosuppressive response or they were reported as members of the chaperone complex associated with HSP90 in steroid receptor oligomers. In this article we review some aspects of the liaison between molecular chaperones and neurodegenerative diseases, in particular heat-shock proteins and immunophilins with demonstrated influence in the proper function of mitochondria. This article is intended to address a field that represents a yet critical unmet clinical need for the development of neuroprotective molecules focused on potentially novel molecular targets.
Fil: Daneri Becerra, Cristina del Rosario. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Ciucci, Sol Micaela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Mazaira, Gisela Ileana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Galigniana, Mario Daniel. Universidad de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Materia
CYCLOPHILIN-A
IMMUNOPHILINS
NEURODEGENERATION
HSP90
FKBP51
FKBP52
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:11336/137146
Acceder
id CONICETDig_7c74d2788eb595d8c6c81b20fe08a4ae
oai_identifier_str oai:ri.conicet.gov.ar:11336/137146
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Role of mitochondrial heat-shock proteins and immunophilins in neurodegenerative diseasesDaneri Becerra, Cristina del RosarioCiucci, Sol MicaelaMazaira, Gisela IleanaGaligniana, Mario DanielCYCLOPHILIN-AIMMUNOPHILINSNEURODEGENERATIONHSP90FKBP51FKBP52https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Pathophysiologic conditions of neurodegenerative diseases are unquestionably related to protein misfolding. The accumulation of misfolded proteins into relatively ordered structures such as fibrillar intracellular and extracellular amyloids results in tissue lesions that lead to neuronal loss and brain damage. In these pathologies, the occurrence of protein aggregates suggests certain inefficient or insufficient cellular response of those molecular chaperones that should properly assist the folding of the client proteins. In this regard, all the experimental models for neurodegenerative diseases have demonstrated that the overexpression of molecular chaperones provide effective neuroprotection. A subset of these molecular chaperones corresponds to a group of proteins that exhibit peptidylprolyl isomerase enzymatic activity, the immunophilins. Most of the family members of the latter group were first described as responsible of the immunosuppressive response or they were reported as members of the chaperone complex associated with HSP90 in steroid receptor oligomers. In this article we review some aspects of the liaison between molecular chaperones and neurodegenerative diseases, in particular heat-shock proteins and immunophilins with demonstrated influence in the proper function of mitochondria. This article is intended to address a field that represents a yet critical unmet clinical need for the development of neuroprotective molecules focused on potentially novel molecular targets.Fil: Daneri Becerra, Cristina del Rosario. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaFil: Ciucci, Sol Micaela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Mazaira, Gisela Ileana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Galigniana, Mario Daniel. Universidad de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaBentham Science Publishers2021info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/137146Daneri Becerra, Cristina del Rosario; Ciucci, Sol Micaela; Mazaira, Gisela Ileana; Galigniana, Mario Daniel; Role of mitochondrial heat-shock proteins and immunophilins in neurodegenerative diseases; Bentham Science Publishers; Current Drug Targets; 22; 2021; 1-211389-4501CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.eurekaselect.com/189662/articleinfo:eu-repo/semantics/altIdentifier/doi/10.2174/1389450121999201230204320info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:02:09Zoai:ri.conicet.gov.ar:11336/137146instacron: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 10:02:10.172CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Role of mitochondrial heat-shock proteins and immunophilins in neurodegenerative diseases
title Role of mitochondrial heat-shock proteins and immunophilins in neurodegenerative diseases
spellingShingle Role of mitochondrial heat-shock proteins and immunophilins in neurodegenerative diseases
Daneri Becerra, Cristina del Rosario
CYCLOPHILIN-A
IMMUNOPHILINS
NEURODEGENERATION
HSP90
FKBP51
FKBP52
title_short Role of mitochondrial heat-shock proteins and immunophilins in neurodegenerative diseases
title_full Role of mitochondrial heat-shock proteins and immunophilins in neurodegenerative diseases
title_fullStr Role of mitochondrial heat-shock proteins and immunophilins in neurodegenerative diseases
title_full_unstemmed Role of mitochondrial heat-shock proteins and immunophilins in neurodegenerative diseases
title_sort Role of mitochondrial heat-shock proteins and immunophilins in neurodegenerative diseases
dc.creator.none.fl_str_mv Daneri Becerra, Cristina del Rosario
Ciucci, Sol Micaela
Mazaira, Gisela Ileana
Galigniana, Mario Daniel
author Daneri Becerra, Cristina del Rosario
author_facet Daneri Becerra, Cristina del Rosario
Ciucci, Sol Micaela
Mazaira, Gisela Ileana
Galigniana, Mario Daniel
author_role author
author2 Ciucci, Sol Micaela
Mazaira, Gisela Ileana
Galigniana, Mario Daniel
author2_role author
author
author
dc.subject.none.fl_str_mv CYCLOPHILIN-A
IMMUNOPHILINS
NEURODEGENERATION
HSP90
FKBP51
FKBP52
topic CYCLOPHILIN-A
IMMUNOPHILINS
NEURODEGENERATION
HSP90
FKBP51
FKBP52
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Pathophysiologic conditions of neurodegenerative diseases are unquestionably related to protein misfolding. The accumulation of misfolded proteins into relatively ordered structures such as fibrillar intracellular and extracellular amyloids results in tissue lesions that lead to neuronal loss and brain damage. In these pathologies, the occurrence of protein aggregates suggests certain inefficient or insufficient cellular response of those molecular chaperones that should properly assist the folding of the client proteins. In this regard, all the experimental models for neurodegenerative diseases have demonstrated that the overexpression of molecular chaperones provide effective neuroprotection. A subset of these molecular chaperones corresponds to a group of proteins that exhibit peptidylprolyl isomerase enzymatic activity, the immunophilins. Most of the family members of the latter group were first described as responsible of the immunosuppressive response or they were reported as members of the chaperone complex associated with HSP90 in steroid receptor oligomers. In this article we review some aspects of the liaison between molecular chaperones and neurodegenerative diseases, in particular heat-shock proteins and immunophilins with demonstrated influence in the proper function of mitochondria. This article is intended to address a field that represents a yet critical unmet clinical need for the development of neuroprotective molecules focused on potentially novel molecular targets.
Fil: Daneri Becerra, Cristina del Rosario. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Ciucci, Sol Micaela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Mazaira, Gisela Ileana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Galigniana, Mario Daniel. Universidad de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
description Pathophysiologic conditions of neurodegenerative diseases are unquestionably related to protein misfolding. The accumulation of misfolded proteins into relatively ordered structures such as fibrillar intracellular and extracellular amyloids results in tissue lesions that lead to neuronal loss and brain damage. In these pathologies, the occurrence of protein aggregates suggests certain inefficient or insufficient cellular response of those molecular chaperones that should properly assist the folding of the client proteins. In this regard, all the experimental models for neurodegenerative diseases have demonstrated that the overexpression of molecular chaperones provide effective neuroprotection. A subset of these molecular chaperones corresponds to a group of proteins that exhibit peptidylprolyl isomerase enzymatic activity, the immunophilins. Most of the family members of the latter group were first described as responsible of the immunosuppressive response or they were reported as members of the chaperone complex associated with HSP90 in steroid receptor oligomers. In this article we review some aspects of the liaison between molecular chaperones and neurodegenerative diseases, in particular heat-shock proteins and immunophilins with demonstrated influence in the proper function of mitochondria. This article is intended to address a field that represents a yet critical unmet clinical need for the development of neuroprotective molecules focused on potentially novel molecular targets.
publishDate 2021
dc.date.none.fl_str_mv 2021
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/11336/137146
Daneri Becerra, Cristina del Rosario; Ciucci, Sol Micaela; Mazaira, Gisela Ileana; Galigniana, Mario Daniel; Role of mitochondrial heat-shock proteins and immunophilins in neurodegenerative diseases; Bentham Science Publishers; Current Drug Targets; 22; 2021; 1-21
1389-4501
CONICET Digital
CONICET
url http://hdl.handle.net/11336/137146
identifier_str_mv Daneri Becerra, Cristina del Rosario; Ciucci, Sol Micaela; Mazaira, Gisela Ileana; Galigniana, Mario Daniel; Role of mitochondrial heat-shock proteins and immunophilins in neurodegenerative diseases; Bentham Science Publishers; Current Drug Targets; 22; 2021; 1-21
1389-4501
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.eurekaselect.com/189662/article
info:eu-repo/semantics/altIdentifier/doi/10.2174/1389450121999201230204320
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
application/pdf
dc.publisher.none.fl_str_mv Bentham Science Publishers
publisher.none.fl_str_mv Bentham 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_ 1842269741284065280
score 13.13397

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