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
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/99436
Ver los metadatos del registro completo
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 |