Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoes

Autores
Tellechea, Mariana Edith; Garcia Pardo Javier; Cotabarren, Juliana; Lufrano, Daniela; Avilés, Francesc Xavier; Obregon, Walter David; Lorenzo, Julia; Tanco, Sebastian
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Metallocarboxypeptidases (MCPs) are zinc-dependent exopeptidases that catalyze the hydrolysis of C-terminal amide bonds in proteins and peptides. MCPs are involved in a wide range of physiological processes and have recently emerged as relevant drug targets in biomedicine (Arolas et. al., 2007). In higher plants, small proteinaceous protease inhibitors are wound-induced molecules produced as a part of its defense system against insect attack (Graham et. al., 1981; Villanueva et. al. 1998). Among such inhibitors, only two are specific for MCPs, i.e. the potato carboxypeptidase inhibitor (PCI) and its close homologue found in tomato plants. In humans, MCP action is exquisitely regulated and dysregulation of their function might lead to disease or even to cell death (Arolas et. al., 2007). In this context, the discovery and characterization of new MCPs inhibitors constitute a valuable approach for the development of new therapeutic strategies. Over the last few decades, the presence of MCPs inhibitors in Solanaceae has been extensively reported, revealing potato (Solanum tuberosum) as one of the most important sources of MCPs inhibitors (Hass et. al.,1979; Lufrano et. al., 2015). In this context, potatos are native from the Andean region of South America, where thousands of different potato varieties coexist, constituting a natural reservoir for the discovery of novel MCP inhibitors (Figure 1). In this protocol, we describe an optimized, simple and accessible microplate method for the measure of the specific and dose-response carboxypeptidase A inhibitory activities present in Andean potatoes tubers.
Fil: Tellechea, Mariana Edith. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Universitat Autònoma de Barcelona; España
Fil: Garcia Pardo Javier. Universitat Autònoma de Barcelona; España
Fil: Cotabarren, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Lufrano, Daniela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Avilés, Francesc Xavier. Universitat Autònoma de Barcelona; España
Fil: Obregon, Walter David. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Lorenzo, Julia. Universitat Autònoma de Barcelona; España
Fil: Tanco, Sebastian. University of Ghent; Bélgica. VIB. Medical Biotechnology Center; Bélgica
Materia
POTATO
INHIBITOR
MICROPLATE ASSAY
CARBOXYPEPTIDASE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/55082
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/55082
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoesTellechea, Mariana EdithGarcia Pardo JavierCotabarren, JulianaLufrano, DanielaAvilés, Francesc XavierObregon, Walter DavidLorenzo, JuliaTanco, SebastianPOTATOINHIBITORMICROPLATE ASSAYCARBOXYPEPTIDASEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Metallocarboxypeptidases (MCPs) are zinc-dependent exopeptidases that catalyze the hydrolysis of C-terminal amide bonds in proteins and peptides. MCPs are involved in a wide range of physiological processes and have recently emerged as relevant drug targets in biomedicine (Arolas et. al., 2007). In higher plants, small proteinaceous protease inhibitors are wound-induced molecules produced as a part of its defense system against insect attack (Graham et. al., 1981; Villanueva et. al. 1998). Among such inhibitors, only two are specific for MCPs, i.e. the potato carboxypeptidase inhibitor (PCI) and its close homologue found in tomato plants. In humans, MCP action is exquisitely regulated and dysregulation of their function might lead to disease or even to cell death (Arolas et. al., 2007). In this context, the discovery and characterization of new MCPs inhibitors constitute a valuable approach for the development of new therapeutic strategies. Over the last few decades, the presence of MCPs inhibitors in Solanaceae has been extensively reported, revealing potato (Solanum tuberosum) as one of the most important sources of MCPs inhibitors (Hass et. al.,1979; Lufrano et. al., 2015). In this context, potatos are native from the Andean region of South America, where thousands of different potato varieties coexist, constituting a natural reservoir for the discovery of novel MCP inhibitors (Figure 1). In this protocol, we describe an optimized, simple and accessible microplate method for the measure of the specific and dose-response carboxypeptidase A inhibitory activities present in Andean potatoes tubers.Fil: Tellechea, Mariana Edith. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Universitat Autònoma de Barcelona; EspañaFil: Garcia Pardo Javier. Universitat Autònoma de Barcelona; EspañaFil: Cotabarren, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Lufrano, Daniela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Avilés, Francesc Xavier. Universitat Autònoma de Barcelona; EspañaFil: Obregon, Walter David. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Lorenzo, Julia. Universitat Autònoma de Barcelona; EspañaFil: Tanco, Sebastian. University of Ghent; Bélgica. VIB. Medical Biotechnology Center; BélgicaBio-protocol LLC2016-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/55082Tellechea, Mariana Edith; Garcia Pardo Javier; Cotabarren, Juliana; Lufrano, Daniela; Avilés, Francesc Xavier; et al.; Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoes; Bio-protocol LLC; Bio-Protocol; 6; 23; 8-2016; 1-122331-8325CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://bio-protocol.org/e2032info:eu-repo/semantics/altIdentifier/doi/10.21769/BioProtoc.2032info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:29:08Zoai:ri.conicet.gov.ar:11336/55082instacron: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:34982025-09-29 10:29:08.763CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoes
title Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoes
spellingShingle Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoes
Tellechea, Mariana Edith
POTATO
INHIBITOR
MICROPLATE ASSAY
CARBOXYPEPTIDASE
title_short Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoes
title_full Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoes
title_fullStr Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoes
title_full_unstemmed Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoes
title_sort Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoes
dc.creator.none.fl_str_mv Tellechea, Mariana Edith
Garcia Pardo Javier
Cotabarren, Juliana
Lufrano, Daniela
Avilés, Francesc Xavier
Obregon, Walter David
Lorenzo, Julia
Tanco, Sebastian
author Tellechea, Mariana Edith
author_facet Tellechea, Mariana Edith
Garcia Pardo Javier
Cotabarren, Juliana
Lufrano, Daniela
Avilés, Francesc Xavier
Obregon, Walter David
Lorenzo, Julia
Tanco, Sebastian
author_role author
author2 Garcia Pardo Javier
Cotabarren, Juliana
Lufrano, Daniela
Avilés, Francesc Xavier
Obregon, Walter David
Lorenzo, Julia
Tanco, Sebastian
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv POTATO
INHIBITOR
MICROPLATE ASSAY
CARBOXYPEPTIDASE
topic POTATO
INHIBITOR
MICROPLATE ASSAY
CARBOXYPEPTIDASE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Metallocarboxypeptidases (MCPs) are zinc-dependent exopeptidases that catalyze the hydrolysis of C-terminal amide bonds in proteins and peptides. MCPs are involved in a wide range of physiological processes and have recently emerged as relevant drug targets in biomedicine (Arolas et. al., 2007). In higher plants, small proteinaceous protease inhibitors are wound-induced molecules produced as a part of its defense system against insect attack (Graham et. al., 1981; Villanueva et. al. 1998). Among such inhibitors, only two are specific for MCPs, i.e. the potato carboxypeptidase inhibitor (PCI) and its close homologue found in tomato plants. In humans, MCP action is exquisitely regulated and dysregulation of their function might lead to disease or even to cell death (Arolas et. al., 2007). In this context, the discovery and characterization of new MCPs inhibitors constitute a valuable approach for the development of new therapeutic strategies. Over the last few decades, the presence of MCPs inhibitors in Solanaceae has been extensively reported, revealing potato (Solanum tuberosum) as one of the most important sources of MCPs inhibitors (Hass et. al.,1979; Lufrano et. al., 2015). In this context, potatos are native from the Andean region of South America, where thousands of different potato varieties coexist, constituting a natural reservoir for the discovery of novel MCP inhibitors (Figure 1). In this protocol, we describe an optimized, simple and accessible microplate method for the measure of the specific and dose-response carboxypeptidase A inhibitory activities present in Andean potatoes tubers.
Fil: Tellechea, Mariana Edith. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Universitat Autònoma de Barcelona; España
Fil: Garcia Pardo Javier. Universitat Autònoma de Barcelona; España
Fil: Cotabarren, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Lufrano, Daniela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Avilés, Francesc Xavier. Universitat Autònoma de Barcelona; España
Fil: Obregon, Walter David. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Lorenzo, Julia. Universitat Autònoma de Barcelona; España
Fil: Tanco, Sebastian. University of Ghent; Bélgica. VIB. Medical Biotechnology Center; Bélgica
description Metallocarboxypeptidases (MCPs) are zinc-dependent exopeptidases that catalyze the hydrolysis of C-terminal amide bonds in proteins and peptides. MCPs are involved in a wide range of physiological processes and have recently emerged as relevant drug targets in biomedicine (Arolas et. al., 2007). In higher plants, small proteinaceous protease inhibitors are wound-induced molecules produced as a part of its defense system against insect attack (Graham et. al., 1981; Villanueva et. al. 1998). Among such inhibitors, only two are specific for MCPs, i.e. the potato carboxypeptidase inhibitor (PCI) and its close homologue found in tomato plants. In humans, MCP action is exquisitely regulated and dysregulation of their function might lead to disease or even to cell death (Arolas et. al., 2007). In this context, the discovery and characterization of new MCPs inhibitors constitute a valuable approach for the development of new therapeutic strategies. Over the last few decades, the presence of MCPs inhibitors in Solanaceae has been extensively reported, revealing potato (Solanum tuberosum) as one of the most important sources of MCPs inhibitors (Hass et. al.,1979; Lufrano et. al., 2015). In this context, potatos are native from the Andean region of South America, where thousands of different potato varieties coexist, constituting a natural reservoir for the discovery of novel MCP inhibitors (Figure 1). In this protocol, we describe an optimized, simple and accessible microplate method for the measure of the specific and dose-response carboxypeptidase A inhibitory activities present in Andean potatoes tubers.
publishDate 2016
dc.date.none.fl_str_mv 2016-08
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/11336/55082
Tellechea, Mariana Edith; Garcia Pardo Javier; Cotabarren, Juliana; Lufrano, Daniela; Avilés, Francesc Xavier; et al.; Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoes; Bio-protocol LLC; Bio-Protocol; 6; 23; 8-2016; 1-12
2331-8325
CONICET Digital
CONICET
url http://hdl.handle.net/11336/55082
identifier_str_mv Tellechea, Mariana Edith; Garcia Pardo Javier; Cotabarren, Juliana; Lufrano, Daniela; Avilés, Francesc Xavier; et al.; Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoes; Bio-protocol LLC; Bio-Protocol; 6; 23; 8-2016; 1-12
2331-8325
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://bio-protocol.org/e2032
info:eu-repo/semantics/altIdentifier/doi/10.21769/BioProtoc.2032
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Bio-protocol LLC
publisher.none.fl_str_mv Bio-protocol LLC
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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score 13.070432

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