Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology

Trypsin enzymes have been studied in a wide variety of animal taxa due to their central role in protein digestion as well as in other important physiological and biotechnological processes. Crustacean trypsins exhibit a high number of isoforms. However, while differences in properties of isoenzymes...

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Autores: Perera, Erick, Rodríguez-Viera, Leandro, Perdomo-Morales, Rolando, Montero-Alejo, Vivian, Moyano, Francisco Javier, Martínez-Rodríguez, Gonzalo, Mancera, Juan Miguel
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2015
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/170952
Acceso en línea:http://hdl.handle.net/10261/170952
Access Level:acceso abierto
Palabra clave:Digestion biochemistry
Ecological physiology
Panulirus argus
Protein digestion
Trypsin polymorphism
Spiny lobster
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spelling Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiologyPerera, ErickRodríguez-Viera, LeandroPerdomo-Morales, RolandoMontero-Alejo, VivianMoyano, Francisco JavierMartínez-Rodríguez, GonzaloMancera, Juan MiguelDigestion biochemistryEcological physiologyPanulirus argusProtein digestionTrypsin polymorphismSpiny lobsterTrypsin enzymes have been studied in a wide variety of animal taxa due to their central role in protein digestion as well as in other important physiological and biotechnological processes. Crustacean trypsins exhibit a high number of isoforms. However, while differences in properties of isoenzymes are known to play important roles in regulating different physiological processes, there is little information on this aspect for decapod trypsins. The aim of this review is to integrate recent findings at the molecular level on trypsin enzymes of the spiny lobster Panulirus argus, into higher levels of organization (biochemical, organism) and to interpret those findings in relation to the feeding ecology of these crustaceans. Trypsin in lobster is a polymorphic enzyme, showing isoforms that differ in their biochemical features and catalytic efficiencies. Molecular studies suggest that polymorphism in lobster trypsins may be non-neutral. Trypsin isoenzymes are differentially regulated by dietary proteins, and it seems that some isoenzymes have undergone adaptive evolution coupled with a divergence in expression rate to increase fitness. This review highlights important but poorly studied issues in crustaceans in general, such as the relation among trypsin polymorphism, phenotypic (digestive) flexibility, digestion efficiency, and feeding ecology.Most of the work outlined on this topic was supported by the International Foundation for Science (No. A/4306-1 and No. A/4306-2) granted to EP, the Agencia Española de Cooperación Internacional/Asociación Universitaria Iberoamericana de Postgrado (AUIP/AECI) from Spain, and the Program ʻDoctorado Iberoamericano en Ciencias’ at the University of Cadiz, Spain.Peer reviewedSpringer NatureInternational Foundation for ScienceMinisterio de Asuntos Exteriores y Cooperación (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201820182015info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/170952reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttps://doi.org/10.1007/s00360-014-0851-ySíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1709522026-05-22T06:33:51Z
dc.title.none.fl_str_mv Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology
title Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology
spellingShingle Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology
Perera, Erick
Digestion biochemistry
Ecological physiology
Panulirus argus
Protein digestion
Trypsin polymorphism
Spiny lobster
title_short Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology
title_full Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology
title_fullStr Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology
title_full_unstemmed Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology
title_sort Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology
dc.creator.none.fl_str_mv Perera, Erick
Rodríguez-Viera, Leandro
Perdomo-Morales, Rolando
Montero-Alejo, Vivian
Moyano, Francisco Javier
Martínez-Rodríguez, Gonzalo
Mancera, Juan Miguel
author Perera, Erick
author_facet Perera, Erick
Rodríguez-Viera, Leandro
Perdomo-Morales, Rolando
Montero-Alejo, Vivian
Moyano, Francisco Javier
Martínez-Rodríguez, Gonzalo
Mancera, Juan Miguel
author_role author
author2 Rodríguez-Viera, Leandro
Perdomo-Morales, Rolando
Montero-Alejo, Vivian
Moyano, Francisco Javier
Martínez-Rodríguez, Gonzalo
Mancera, Juan Miguel
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv International Foundation for Science
Ministerio de Asuntos Exteriores y Cooperación (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Digestion biochemistry
Ecological physiology
Panulirus argus
Protein digestion
Trypsin polymorphism
Spiny lobster
topic Digestion biochemistry
Ecological physiology
Panulirus argus
Protein digestion
Trypsin polymorphism
Spiny lobster
description Trypsin enzymes have been studied in a wide variety of animal taxa due to their central role in protein digestion as well as in other important physiological and biotechnological processes. Crustacean trypsins exhibit a high number of isoforms. However, while differences in properties of isoenzymes are known to play important roles in regulating different physiological processes, there is little information on this aspect for decapod trypsins. The aim of this review is to integrate recent findings at the molecular level on trypsin enzymes of the spiny lobster Panulirus argus, into higher levels of organization (biochemical, organism) and to interpret those findings in relation to the feeding ecology of these crustaceans. Trypsin in lobster is a polymorphic enzyme, showing isoforms that differ in their biochemical features and catalytic efficiencies. Molecular studies suggest that polymorphism in lobster trypsins may be non-neutral. Trypsin isoenzymes are differentially regulated by dietary proteins, and it seems that some isoenzymes have undergone adaptive evolution coupled with a divergence in expression rate to increase fitness. This review highlights important but poorly studied issues in crustaceans in general, such as the relation among trypsin polymorphism, phenotypic (digestive) flexibility, digestion efficiency, and feeding ecology.
publishDate 2015
dc.date.none.fl_str_mv 2015
2018
2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/170952
url http://hdl.handle.net/10261/170952
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://doi.org/10.1007/s00360-014-0851-y
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Springer Nature
publisher.none.fl_str_mv Springer Nature
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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