Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization

Autores
Godoy, Martín Sergio; Castro-Vazquez, Alfredo; Vega, Israel Aníbal
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Digestive proteases of the digestive tract of the apple snail Pomacea canaliculata were studied. Luminal protease activity was found in the crop, the style sac and the coiled gut and was significantly higher in the coiled gut. Several protease bands and their apparent molecular weights were identified in both tissue extracts and luminal contents by gel zymography: (1) a 125 kDa protease in salivary gland extracts and in the crop content; (2) a 30 kDa protease throughout all studied luminal contents and in extracts of the midgut gland and of the endosymbionts isolated from this gland; (3) two proteases of 145 and 198 kDa in the coiled gut content. All these proteases were inhibited by aprotinin, a serine-protease inhibitor, and showed maximum activity between 30C and 35C and pH between 8.5 and 9.5. Tissue L-alanine-N-aminopeptidase activity was determined in the wall of the crop, the style sac and the coiled gut and was significantly higher in the coiled gut. Our findings show that protein digestion in P. canaliculata is carried out through a battery of diverse proteases originated from the salivary glands and the endosymbionts lodged in the midgut gland and by proteases of uncertain origin that occur in the coiled gut lumen.
Fil: Godoy, Martín Sergio. Instituto Nacional de Tecnologia Agropecuaria. Centro Nacional de Inv. Agropecuarias. Centro de Inv. Agropecuarias. Instituto de Fisiologia y Recursos Geneticos Vegetales; Consejo Nacional de Invest.cientif.y Tecnicas. Centro Cientifico Tecnol.conicet - Mendoza. Instituto Histologia y Embriologia D/mend Dr.m.burgos;
Fil: Castro-Vasquez, Alfredo. Consejo Nacional de Invest.cientif.y Tecnicas. Centro Cientifico Tecnol.conicet - Mendoza. Instituto Histologia y Embriologia D/mend Dr.m.burgos; Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Instituto Nacional de Tecnologia Agropecuaria. Centro Nacional de Inv. Agropecuarias. Centro de Inv. Agropecuarias. Instituto de Fisiologia y Recursos Geneticos Vegetales;
Fil: Vega, Israel Aníbal. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Consejo Nacional de Invest.cientif.y Tecnicas. Centro Cientifico Tecnol.conicet - Mendoza. Instituto Histologia y Embriologia D/mend Dr.m.burgos; Instituto Nacional de Tecnologia Agropecuaria. Centro Nacional de Inv. Agropecuarias. Centro de Inv. Agropecuarias. Instituto de Fisiologia y Recursos Geneticos Vegetales;
Materia
SYMBIOSIS
SERINPROTEASES
AMINOPEPTIDAES
DIGESTION
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:11336/559
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/559
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterizationGodoy, Martín SergioCastro-Vazquez, AlfredoVega, Israel AníbalSYMBIOSISSERINPROTEASESAMINOPEPTIDAESDIGESTIONhttps://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.6Digestive proteases of the digestive tract of the apple snail Pomacea canaliculata were studied. Luminal protease activity was found in the crop, the style sac and the coiled gut and was significantly higher in the coiled gut. Several protease bands and their apparent molecular weights were identified in both tissue extracts and luminal contents by gel zymography: (1) a 125 kDa protease in salivary gland extracts and in the crop content; (2) a 30 kDa protease throughout all studied luminal contents and in extracts of the midgut gland and of the endosymbionts isolated from this gland; (3) two proteases of 145 and 198 kDa in the coiled gut content. All these proteases were inhibited by aprotinin, a serine-protease inhibitor, and showed maximum activity between 30C and 35C and pH between 8.5 and 9.5. Tissue L-alanine-N-aminopeptidase activity was determined in the wall of the crop, the style sac and the coiled gut and was significantly higher in the coiled gut. Our findings show that protein digestion in P. canaliculata is carried out through a battery of diverse proteases originated from the salivary glands and the endosymbionts lodged in the midgut gland and by proteases of uncertain origin that occur in the coiled gut lumen.Fil: Godoy, Martín Sergio. Instituto Nacional de Tecnologia Agropecuaria. Centro Nacional de Inv. Agropecuarias. Centro de Inv. Agropecuarias. Instituto de Fisiologia y Recursos Geneticos Vegetales; Consejo Nacional de Invest.cientif.y Tecnicas. Centro Cientifico Tecnol.conicet - Mendoza. Instituto Histologia y Embriologia D/mend Dr.m.burgos;Fil: Castro-Vasquez, Alfredo. Consejo Nacional de Invest.cientif.y Tecnicas. Centro Cientifico Tecnol.conicet - Mendoza. Instituto Histologia y Embriologia D/mend Dr.m.burgos; Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Instituto Nacional de Tecnologia Agropecuaria. Centro Nacional de Inv. Agropecuarias. Centro de Inv. Agropecuarias. Instituto de Fisiologia y Recursos Geneticos Vegetales;Fil: Vega, Israel Aníbal. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Consejo Nacional de Invest.cientif.y Tecnicas. Centro Cientifico Tecnol.conicet - Mendoza. Instituto Histologia y Embriologia D/mend Dr.m.burgos; Instituto Nacional de Tecnologia Agropecuaria. Centro Nacional de Inv. Agropecuarias. Centro de Inv. Agropecuarias. Instituto de Fisiologia y Recursos Geneticos Vegetales;Public Library Science2013-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/559Godoy, Martín Sergio; Castro-Vazquez, Alfredo; Vega, Israel Aníbal; Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization; Public Library Science; Plos One; 8; 6-2013; 1-10;1932-6203enginfo:eu-repo/semantics/altIdentifier/url/http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0066689#closeinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:14:09Zoai:ri.conicet.gov.ar:11336/559instacron: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:34982025-10-15 15:14:10.053CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization
title Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization
spellingShingle Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization
Godoy, Martín Sergio
SYMBIOSIS
SERINPROTEASES
AMINOPEPTIDAES
DIGESTION
title_short Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization
title_full Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization
title_fullStr Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization
title_full_unstemmed Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization
title_sort Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization
dc.creator.none.fl_str_mv Godoy, Martín Sergio
Castro-Vazquez, Alfredo
Vega, Israel Aníbal
author Godoy, Martín Sergio
author_facet Godoy, Martín Sergio
Castro-Vazquez, Alfredo
Vega, Israel Aníbal
author_role author
author2 Castro-Vazquez, Alfredo
Vega, Israel Aníbal
author2_role author
author
dc.subject.none.fl_str_mv SYMBIOSIS
SERINPROTEASES
AMINOPEPTIDAES
DIGESTION
topic SYMBIOSIS
SERINPROTEASES
AMINOPEPTIDAES
DIGESTION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.6
dc.description.none.fl_txt_mv Digestive proteases of the digestive tract of the apple snail Pomacea canaliculata were studied. Luminal protease activity was found in the crop, the style sac and the coiled gut and was significantly higher in the coiled gut. Several protease bands and their apparent molecular weights were identified in both tissue extracts and luminal contents by gel zymography: (1) a 125 kDa protease in salivary gland extracts and in the crop content; (2) a 30 kDa protease throughout all studied luminal contents and in extracts of the midgut gland and of the endosymbionts isolated from this gland; (3) two proteases of 145 and 198 kDa in the coiled gut content. All these proteases were inhibited by aprotinin, a serine-protease inhibitor, and showed maximum activity between 30C and 35C and pH between 8.5 and 9.5. Tissue L-alanine-N-aminopeptidase activity was determined in the wall of the crop, the style sac and the coiled gut and was significantly higher in the coiled gut. Our findings show that protein digestion in P. canaliculata is carried out through a battery of diverse proteases originated from the salivary glands and the endosymbionts lodged in the midgut gland and by proteases of uncertain origin that occur in the coiled gut lumen.
Fil: Godoy, Martín Sergio. Instituto Nacional de Tecnologia Agropecuaria. Centro Nacional de Inv. Agropecuarias. Centro de Inv. Agropecuarias. Instituto de Fisiologia y Recursos Geneticos Vegetales; Consejo Nacional de Invest.cientif.y Tecnicas. Centro Cientifico Tecnol.conicet - Mendoza. Instituto Histologia y Embriologia D/mend Dr.m.burgos;
Fil: Castro-Vasquez, Alfredo. Consejo Nacional de Invest.cientif.y Tecnicas. Centro Cientifico Tecnol.conicet - Mendoza. Instituto Histologia y Embriologia D/mend Dr.m.burgos; Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Instituto Nacional de Tecnologia Agropecuaria. Centro Nacional de Inv. Agropecuarias. Centro de Inv. Agropecuarias. Instituto de Fisiologia y Recursos Geneticos Vegetales;
Fil: Vega, Israel Aníbal. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Consejo Nacional de Invest.cientif.y Tecnicas. Centro Cientifico Tecnol.conicet - Mendoza. Instituto Histologia y Embriologia D/mend Dr.m.burgos; Instituto Nacional de Tecnologia Agropecuaria. Centro Nacional de Inv. Agropecuarias. Centro de Inv. Agropecuarias. Instituto de Fisiologia y Recursos Geneticos Vegetales;
description Digestive proteases of the digestive tract of the apple snail Pomacea canaliculata were studied. Luminal protease activity was found in the crop, the style sac and the coiled gut and was significantly higher in the coiled gut. Several protease bands and their apparent molecular weights were identified in both tissue extracts and luminal contents by gel zymography: (1) a 125 kDa protease in salivary gland extracts and in the crop content; (2) a 30 kDa protease throughout all studied luminal contents and in extracts of the midgut gland and of the endosymbionts isolated from this gland; (3) two proteases of 145 and 198 kDa in the coiled gut content. All these proteases were inhibited by aprotinin, a serine-protease inhibitor, and showed maximum activity between 30C and 35C and pH between 8.5 and 9.5. Tissue L-alanine-N-aminopeptidase activity was determined in the wall of the crop, the style sac and the coiled gut and was significantly higher in the coiled gut. Our findings show that protein digestion in P. canaliculata is carried out through a battery of diverse proteases originated from the salivary glands and the endosymbionts lodged in the midgut gland and by proteases of uncertain origin that occur in the coiled gut lumen.
publishDate 2013
dc.date.none.fl_str_mv 2013-06
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/11336/559
Godoy, Martín Sergio; Castro-Vazquez, Alfredo; Vega, Israel Aníbal; Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization; Public Library Science; Plos One; 8; 6-2013; 1-10;
1932-6203
url http://hdl.handle.net/11336/559
identifier_str_mv Godoy, Martín Sergio; Castro-Vazquez, Alfredo; Vega, Israel Aníbal; Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization; Public Library Science; Plos One; 8; 6-2013; 1-10;
1932-6203
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0066689#close
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 Public Library Science
publisher.none.fl_str_mv Public Library Science
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_ 1846083288822710272
score 13.22299

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