In silico analysis and effects of environmental salinity in the expression and activity of digestive α-amylase and trypsins from the euryhaline crab Neohelice granulata

Autores
Asaro, Antonela; Martos Sitcha, Juan Antonio; Martínez Rodríguez, Gonzalo; Mancera, Juan Miguel; Lopez Mañanes, Alejandra Antonia
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Studies on molecular characteristics and modulation of expression of α-amylase and trypsin in the hepatopancreas of intertidal euryhaline crabs are lacking. In this work, we cloned and studied by in silico approaches the characteristics of cDNA sequences for α-amylase and two trypsins isoforms, as well as the effect of environmental salinity, on gene expression and protein activities in the hepatopancreas of Neohelice granulata (Dana, 1851), which is a good invertebrate model species. The cDNA sequence of α-amylase is 1637 bp long, encoding 459 amino acid residues. Trypsin 1 and 2 are 689 and 1174 bp long, encoding 204 and 151 amino acid residues, respectively. Multiple sequence alignment of deduced protein sequences revealed the presence of conserved motifs found in other invertebrates. In crabs acclimated at 37 psu (hyporegulation), α-amylase mRNA level and total pancreatic amylase activity were higher than at 10 psu (hyperregulation) and 35 psu (osmoconformation). Trypsin 1 mRNA levels increased at 37 psu, while trypsin 2 levels decreased at 10 and 37 psu. Total trypsin activity was similar in all salinities. Our results showed a differential modulation of α-amylase and trypsin expression and total amylase activity by salinity acclimation, suggesting the occurrence of distinct mechanisms of regulation at different levels that could lead to digestive adjustments in relation to hyperregulation and (or) hyporegulation.
Fil: Asaro, Antonela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; Argentina
Fil: Martos Sitcha, Juan Antonio. Consejo Superior de Investigaciones Científicas; España. Universidad de Cádiz; España
Fil: Martínez Rodríguez, Gonzalo. Consejo Superior de Investigaciones Científicas; España
Fil: Mancera, Juan Miguel. Universidad de Cádiz; España
Fil: Lopez Mañanes, Alejandra Antonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; Argentina
Materia
Cloning
Digestive Flexibility
Hepatopancreas
Neohelice Granulata
Trypsin
Α-Amylase
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:11336/64508

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network_name_str CONICET Digital (CONICET)
spelling In silico analysis and effects of environmental salinity in the expression and activity of digestive α-amylase and trypsins from the euryhaline crab Neohelice granulataAsaro, AntonelaMartos Sitcha, Juan AntonioMartínez Rodríguez, GonzaloMancera, Juan MiguelLopez Mañanes, Alejandra AntoniaCloningDigestive FlexibilityHepatopancreasNeohelice GranulataTrypsinΑ-Amylasehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Studies on molecular characteristics and modulation of expression of α-amylase and trypsin in the hepatopancreas of intertidal euryhaline crabs are lacking. In this work, we cloned and studied by in silico approaches the characteristics of cDNA sequences for α-amylase and two trypsins isoforms, as well as the effect of environmental salinity, on gene expression and protein activities in the hepatopancreas of Neohelice granulata (Dana, 1851), which is a good invertebrate model species. The cDNA sequence of α-amylase is 1637 bp long, encoding 459 amino acid residues. Trypsin 1 and 2 are 689 and 1174 bp long, encoding 204 and 151 amino acid residues, respectively. Multiple sequence alignment of deduced protein sequences revealed the presence of conserved motifs found in other invertebrates. In crabs acclimated at 37 psu (hyporegulation), α-amylase mRNA level and total pancreatic amylase activity were higher than at 10 psu (hyperregulation) and 35 psu (osmoconformation). Trypsin 1 mRNA levels increased at 37 psu, while trypsin 2 levels decreased at 10 and 37 psu. Total trypsin activity was similar in all salinities. Our results showed a differential modulation of α-amylase and trypsin expression and total amylase activity by salinity acclimation, suggesting the occurrence of distinct mechanisms of regulation at different levels that could lead to digestive adjustments in relation to hyperregulation and (or) hyporegulation.Fil: Asaro, Antonela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; ArgentinaFil: Martos Sitcha, Juan Antonio. Consejo Superior de Investigaciones Científicas; España. Universidad de Cádiz; EspañaFil: Martínez Rodríguez, Gonzalo. Consejo Superior de Investigaciones Científicas; EspañaFil: Mancera, Juan Miguel. Universidad de Cádiz; EspañaFil: Lopez Mañanes, Alejandra Antonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; ArgentinaNational Research Council Canada-NRC Research Press2017-08-30info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/64508Asaro, Antonela; Martos Sitcha, Juan Antonio; Martínez Rodríguez, Gonzalo; Mancera, Juan Miguel; Lopez Mañanes, Alejandra Antonia; In silico analysis and effects of environmental salinity in the expression and activity of digestive α-amylase and trypsins from the euryhaline crab Neohelice granulata; National Research Council Canada-NRC Research Press; Canadian Journal of Zoology; 96; 2; 30-8-2017; 127-1390008-43011480-3283CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1139/cjz-2016-0324info:eu-repo/semantics/altIdentifier/url/http://www.nrcresearchpress.com/doi/10.1139/cjz-2016-0324#.W-yFLDgzbmginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:57:38Zoai:ri.conicet.gov.ar:11336/64508instacron: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 09:57:38.278CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv In silico analysis and effects of environmental salinity in the expression and activity of digestive α-amylase and trypsins from the euryhaline crab Neohelice granulata
title In silico analysis and effects of environmental salinity in the expression and activity of digestive α-amylase and trypsins from the euryhaline crab Neohelice granulata
spellingShingle In silico analysis and effects of environmental salinity in the expression and activity of digestive α-amylase and trypsins from the euryhaline crab Neohelice granulata
Asaro, Antonela
Cloning
Digestive Flexibility
Hepatopancreas
Neohelice Granulata
Trypsin
Α-Amylase
title_short In silico analysis and effects of environmental salinity in the expression and activity of digestive α-amylase and trypsins from the euryhaline crab Neohelice granulata
title_full In silico analysis and effects of environmental salinity in the expression and activity of digestive α-amylase and trypsins from the euryhaline crab Neohelice granulata
title_fullStr In silico analysis and effects of environmental salinity in the expression and activity of digestive α-amylase and trypsins from the euryhaline crab Neohelice granulata
title_full_unstemmed In silico analysis and effects of environmental salinity in the expression and activity of digestive α-amylase and trypsins from the euryhaline crab Neohelice granulata
title_sort In silico analysis and effects of environmental salinity in the expression and activity of digestive α-amylase and trypsins from the euryhaline crab Neohelice granulata
dc.creator.none.fl_str_mv Asaro, Antonela
Martos Sitcha, Juan Antonio
Martínez Rodríguez, Gonzalo
Mancera, Juan Miguel
Lopez Mañanes, Alejandra Antonia
author Asaro, Antonela
author_facet Asaro, Antonela
Martos Sitcha, Juan Antonio
Martínez Rodríguez, Gonzalo
Mancera, Juan Miguel
Lopez Mañanes, Alejandra Antonia
author_role author
author2 Martos Sitcha, Juan Antonio
Martínez Rodríguez, Gonzalo
Mancera, Juan Miguel
Lopez Mañanes, Alejandra Antonia
author2_role author
author
author
author
dc.subject.none.fl_str_mv Cloning
Digestive Flexibility
Hepatopancreas
Neohelice Granulata
Trypsin
Α-Amylase
topic Cloning
Digestive Flexibility
Hepatopancreas
Neohelice Granulata
Trypsin
Α-Amylase
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Studies on molecular characteristics and modulation of expression of α-amylase and trypsin in the hepatopancreas of intertidal euryhaline crabs are lacking. In this work, we cloned and studied by in silico approaches the characteristics of cDNA sequences for α-amylase and two trypsins isoforms, as well as the effect of environmental salinity, on gene expression and protein activities in the hepatopancreas of Neohelice granulata (Dana, 1851), which is a good invertebrate model species. The cDNA sequence of α-amylase is 1637 bp long, encoding 459 amino acid residues. Trypsin 1 and 2 are 689 and 1174 bp long, encoding 204 and 151 amino acid residues, respectively. Multiple sequence alignment of deduced protein sequences revealed the presence of conserved motifs found in other invertebrates. In crabs acclimated at 37 psu (hyporegulation), α-amylase mRNA level and total pancreatic amylase activity were higher than at 10 psu (hyperregulation) and 35 psu (osmoconformation). Trypsin 1 mRNA levels increased at 37 psu, while trypsin 2 levels decreased at 10 and 37 psu. Total trypsin activity was similar in all salinities. Our results showed a differential modulation of α-amylase and trypsin expression and total amylase activity by salinity acclimation, suggesting the occurrence of distinct mechanisms of regulation at different levels that could lead to digestive adjustments in relation to hyperregulation and (or) hyporegulation.
Fil: Asaro, Antonela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; Argentina
Fil: Martos Sitcha, Juan Antonio. Consejo Superior de Investigaciones Científicas; España. Universidad de Cádiz; España
Fil: Martínez Rodríguez, Gonzalo. Consejo Superior de Investigaciones Científicas; España
Fil: Mancera, Juan Miguel. Universidad de Cádiz; España
Fil: Lopez Mañanes, Alejandra Antonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; Argentina
description Studies on molecular characteristics and modulation of expression of α-amylase and trypsin in the hepatopancreas of intertidal euryhaline crabs are lacking. In this work, we cloned and studied by in silico approaches the characteristics of cDNA sequences for α-amylase and two trypsins isoforms, as well as the effect of environmental salinity, on gene expression and protein activities in the hepatopancreas of Neohelice granulata (Dana, 1851), which is a good invertebrate model species. The cDNA sequence of α-amylase is 1637 bp long, encoding 459 amino acid residues. Trypsin 1 and 2 are 689 and 1174 bp long, encoding 204 and 151 amino acid residues, respectively. Multiple sequence alignment of deduced protein sequences revealed the presence of conserved motifs found in other invertebrates. In crabs acclimated at 37 psu (hyporegulation), α-amylase mRNA level and total pancreatic amylase activity were higher than at 10 psu (hyperregulation) and 35 psu (osmoconformation). Trypsin 1 mRNA levels increased at 37 psu, while trypsin 2 levels decreased at 10 and 37 psu. Total trypsin activity was similar in all salinities. Our results showed a differential modulation of α-amylase and trypsin expression and total amylase activity by salinity acclimation, suggesting the occurrence of distinct mechanisms of regulation at different levels that could lead to digestive adjustments in relation to hyperregulation and (or) hyporegulation.
publishDate 2017
dc.date.none.fl_str_mv 2017-08-30
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/11336/64508
Asaro, Antonela; Martos Sitcha, Juan Antonio; Martínez Rodríguez, Gonzalo; Mancera, Juan Miguel; Lopez Mañanes, Alejandra Antonia; In silico analysis and effects of environmental salinity in the expression and activity of digestive α-amylase and trypsins from the euryhaline crab Neohelice granulata; National Research Council Canada-NRC Research Press; Canadian Journal of Zoology; 96; 2; 30-8-2017; 127-139
0008-4301
1480-3283
CONICET Digital
CONICET
url http://hdl.handle.net/11336/64508
identifier_str_mv Asaro, Antonela; Martos Sitcha, Juan Antonio; Martínez Rodríguez, Gonzalo; Mancera, Juan Miguel; Lopez Mañanes, Alejandra Antonia; In silico analysis and effects of environmental salinity in the expression and activity of digestive α-amylase and trypsins from the euryhaline crab Neohelice granulata; National Research Council Canada-NRC Research Press; Canadian Journal of Zoology; 96; 2; 30-8-2017; 127-139
0008-4301
1480-3283
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1139/cjz-2016-0324
info:eu-repo/semantics/altIdentifier/url/http://www.nrcresearchpress.com/doi/10.1139/cjz-2016-0324#.W-yFLDgzbmg
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 National Research Council Canada-NRC Research Press
publisher.none.fl_str_mv National Research Council Canada-NRC Research Press
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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