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

Autores
Tellechea, Mariana Edith; Garcia Pardo, Javier; Cotabarren, Juliana; Lufrano, Daniela; Bakás, Laura Susana; 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.
Centro de Investigación de Proteínas Vegetales
Materia
Bioquímica
Metallocarboxypeptidase
Inhibitor
Microplate assay
Carboxypeptidase A
Inhibitory activity
Potatoes
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/99436

id SEDICI_e0ad6ea149f1143f0c800c3eab5e7a10
oai_identifier_str oai:sedici.unlp.edu.ar:10915/99436
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Microplate assay for the determination of carboxypeptidase A inhibitory activity in Andean potatoesTellechea, Mariana EdithGarcia Pardo, JavierCotabarren, JulianaLufrano, DanielaBakás, Laura SusanaAvilés, Francesc XavierObregon, Walter DavidLorenzo, JuliaTanco, SebastianBioquímicaMetallocarboxypeptidaseInhibitorMicroplate assayCarboxypeptidase AInhibitory activityPotatoesMetallocarboxypeptidases (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.Centro de Investigación de Proteínas Vegetales2016-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf1-12http://sedici.unlp.edu.ar/handle/10915/99436enginfo:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/55082info:eu-repo/semantics/altIdentifier/url/https://bio-protocol.org/e2032info:eu-repo/semantics/altIdentifier/issn/2331-8325info:eu-repo/semantics/altIdentifier/doi/10.21769/BioProtoc.2032info:eu-repo/semantics/altIdentifier/hdl/11336/55082info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:20:11Zoai:sedici.unlp.edu.ar:10915/99436Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:20:12.01SEDICI (UNLP) - Universidad Nacional de La Platafalse
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
Bioquímica
Metallocarboxypeptidase
Inhibitor
Microplate assay
Carboxypeptidase A
Inhibitory activity
Potatoes
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
Bakás, Laura Susana
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
Bakás, Laura Susana
Avilés, Francesc Xavier
Obregon, Walter David
Lorenzo, Julia
Tanco, Sebastian
author_role author
author2 Garcia Pardo, Javier
Cotabarren, Juliana
Lufrano, Daniela
Bakás, Laura Susana
Avilés, Francesc Xavier
Obregon, Walter David
Lorenzo, Julia
Tanco, Sebastian
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Bioquímica
Metallocarboxypeptidase
Inhibitor
Microplate assay
Carboxypeptidase A
Inhibitory activity
Potatoes
topic Bioquímica
Metallocarboxypeptidase
Inhibitor
Microplate assay
Carboxypeptidase A
Inhibitory activity
Potatoes
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.
Centro de Investigación de Proteínas Vegetales
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
Articulo
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://sedici.unlp.edu.ar/handle/10915/99436
url http://sedici.unlp.edu.ar/handle/10915/99436
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/55082
info:eu-repo/semantics/altIdentifier/url/https://bio-protocol.org/e2032
info:eu-repo/semantics/altIdentifier/issn/2331-8325
info:eu-repo/semantics/altIdentifier/doi/10.21769/BioProtoc.2032
info:eu-repo/semantics/altIdentifier/hdl/11336/55082
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
1-12
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
_version_ 1844616076433817600
score 13.070432