Pancreatic and intestinal carbohydrases are matched to dietary starch level in wild passerine birds

Autores
Kohl, Kevin D.; Brzek, Pawel; Caviedes Vidal, Enrique Juan Raul; Karasov, William H.
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Evolutionary shifts in diet composition are presumably accompanied by simultaneous changes in digestive physiology. The adaptive modulation hypothesis predicts that activities of digestive enzymes should match the relative levels of their substrates in an animal’s diet so that available membrane space and synthetic energy are not wasted on enzymes in excess of need. However, previous studies on captive passerine birds showed high intraspecific phenotypic flexibility only in proteases but not in carbohydrases in response to varying diet composition. In this study, we measured the activities of pancreatic, intestinal, and hepatic enzymes in six wild-caught passerine species. We predicted that if the adaptive modulation hypothesis holds during evolutionary shifts in diet composition in birds, then mass-specific activities of digestive enzymes should be correlated positively with the content of their relevant substrates in species’ diets. Whereas mass-specific activities of proteases (aminopeptidase-N, trypsin, chymotrypsin, alanine aminotransferase) were not correlated with estimated dietary protein content, mass-specific activities of all studied carbohydrases (amylase, maltase, sucrase) were positively correlated with estimated dietary starch content. We conclude that activities of carbohydrases but not proteases are evolutionarily matched to diet composition in passerine birds. We hypothesize that the need for nitrogen and essential amino acids can prevent the evolution of a low activity of proteases, even in species feeding on a low-protein diet.
Fil: Kohl, Kevin D.. University of Wisconsin; Estados Unidos. University of Utah; Estados Unidos
Fil: Brzek, Pawel. University of Wisconsin; Estados Unidos. University of Bialystok. Department of Biology; Polonia
Fil: Caviedes Vidal, Enrique Juan Raul. Universidad Nacional de San Luis. Facultad de Quimica, Bioquimica y Farmacia. Departamento de Bioquímica y Ciencias Biológicas; Argentina. Universidad Nacional de San Luis. Facultad de Ciencias Humanas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Karasov, William H.. University of Wisconsin; Estados Unidos
Materia
Pancreatic Enzymes
Intestinal Enzymes
Dietary Adaptation
Comparative Method
Birds
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:11336/14628

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network_name_str CONICET Digital (CONICET)
spelling Pancreatic and intestinal carbohydrases are matched to dietary starch level in wild passerine birdsKohl, Kevin D.Brzek, PawelCaviedes Vidal, Enrique Juan RaulKarasov, William H.Pancreatic EnzymesIntestinal EnzymesDietary AdaptationComparative MethodBirdshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Evolutionary shifts in diet composition are presumably accompanied by simultaneous changes in digestive physiology. The adaptive modulation hypothesis predicts that activities of digestive enzymes should match the relative levels of their substrates in an animal‚Äôs diet so that available membrane space and synthetic energy are not wasted on enzymes in excess of need. However, previous studies on captive passerine birds showed high intraspecific phenotypic flexibility only in proteases but not in carbohydrases in response to varying diet composition. In this study, we measured the activities of pancreatic, intestinal, and hepatic enzymes in six wild-caught passerine species. We predicted that if the adaptive modulation hypothesis holds during evolutionary shifts in diet composition in birds, then mass-specific activities of digestive enzymes should be correlated positively with the content of their relevant substrates in species‚Äô diets. Whereas mass-specific activities of proteases (aminopeptidase-N, trypsin, chymotrypsin, alanine aminotransferase) were not correlated with estimated dietary protein content, mass-specific activities of all studied carbohydrases (amylase, maltase, sucrase) were positively correlated with estimated dietary starch content. We conclude that activities of carbohydrases but not proteases are evolutionarily matched to diet composition in passerine birds. We hypothesize that the need for nitrogen and essential amino acids can prevent the evolution of a low activity of proteases, even in species feeding on a low-protein diet.Fil: Kohl, Kevin D.. University of Wisconsin; Estados Unidos. University of Utah; Estados UnidosFil: Brzek, Pawel. University of Wisconsin; Estados Unidos. University of Bialystok. Department of Biology; PoloniaFil: Caviedes Vidal, Enrique Juan Raul. Universidad Nacional de San Luis. Facultad de Quimica, Bioquimica y Farmacia. Departamento de Bioquímica y Ciencias Biológicas; Argentina. Universidad Nacional de San Luis. Facultad de Ciencias Humanas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; ArgentinaFil: Karasov, William H.. University of Wisconsin; Estados UnidosUniversity of Chicago Press2011-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/14628Kohl, Kevin D.; Brzek, Pawel; Caviedes Vidal, Enrique Juan Raul; Karasov, William H.; Pancreatic and intestinal carbohydrases are matched to dietary starch level in wild passerine birds; University of Chicago Press; Physiological and Biochemical Zoology; 84; 2; 3-2011; 195-2031522-21521537-5293enginfo:eu-repo/semantics/altIdentifier/url/http://www.jstor.org/stable/10.1086/658146info:eu-repo/semantics/altIdentifier/doi/10.1086/658146info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:20:01Zoai:ri.conicet.gov.ar:11336/14628instacron: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:34982025-09-29 10:20:02.078CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Pancreatic and intestinal carbohydrases are matched to dietary starch level in wild passerine birds
title Pancreatic and intestinal carbohydrases are matched to dietary starch level in wild passerine birds
spellingShingle Pancreatic and intestinal carbohydrases are matched to dietary starch level in wild passerine birds
Kohl, Kevin D.
Pancreatic Enzymes
Intestinal Enzymes
Dietary Adaptation
Comparative Method
Birds
title_short Pancreatic and intestinal carbohydrases are matched to dietary starch level in wild passerine birds
title_full Pancreatic and intestinal carbohydrases are matched to dietary starch level in wild passerine birds
title_fullStr Pancreatic and intestinal carbohydrases are matched to dietary starch level in wild passerine birds
title_full_unstemmed Pancreatic and intestinal carbohydrases are matched to dietary starch level in wild passerine birds
title_sort Pancreatic and intestinal carbohydrases are matched to dietary starch level in wild passerine birds
dc.creator.none.fl_str_mv Kohl, Kevin D.
Brzek, Pawel
Caviedes Vidal, Enrique Juan Raul
Karasov, William H.
author Kohl, Kevin D.
author_facet Kohl, Kevin D.
Brzek, Pawel
Caviedes Vidal, Enrique Juan Raul
Karasov, William H.
author_role author
author2 Brzek, Pawel
Caviedes Vidal, Enrique Juan Raul
Karasov, William H.
author2_role author
author
author
dc.subject.none.fl_str_mv Pancreatic Enzymes
Intestinal Enzymes
Dietary Adaptation
Comparative Method
Birds
topic Pancreatic Enzymes
Intestinal Enzymes
Dietary Adaptation
Comparative Method
Birds
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Evolutionary shifts in diet composition are presumably accompanied by simultaneous changes in digestive physiology. The adaptive modulation hypothesis predicts that activities of digestive enzymes should match the relative levels of their substrates in an animal’s diet so that available membrane space and synthetic energy are not wasted on enzymes in excess of need. However, previous studies on captive passerine birds showed high intraspecific phenotypic flexibility only in proteases but not in carbohydrases in response to varying diet composition. In this study, we measured the activities of pancreatic, intestinal, and hepatic enzymes in six wild-caught passerine species. We predicted that if the adaptive modulation hypothesis holds during evolutionary shifts in diet composition in birds, then mass-specific activities of digestive enzymes should be correlated positively with the content of their relevant substrates in species’ diets. Whereas mass-specific activities of proteases (aminopeptidase-N, trypsin, chymotrypsin, alanine aminotransferase) were not correlated with estimated dietary protein content, mass-specific activities of all studied carbohydrases (amylase, maltase, sucrase) were positively correlated with estimated dietary starch content. We conclude that activities of carbohydrases but not proteases are evolutionarily matched to diet composition in passerine birds. We hypothesize that the need for nitrogen and essential amino acids can prevent the evolution of a low activity of proteases, even in species feeding on a low-protein diet.
Fil: Kohl, Kevin D.. University of Wisconsin; Estados Unidos. University of Utah; Estados Unidos
Fil: Brzek, Pawel. University of Wisconsin; Estados Unidos. University of Bialystok. Department of Biology; Polonia
Fil: Caviedes Vidal, Enrique Juan Raul. Universidad Nacional de San Luis. Facultad de Quimica, Bioquimica y Farmacia. Departamento de Bioquímica y Ciencias Biológicas; Argentina. Universidad Nacional de San Luis. Facultad de Ciencias Humanas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Karasov, William H.. University of Wisconsin; Estados Unidos
description Evolutionary shifts in diet composition are presumably accompanied by simultaneous changes in digestive physiology. The adaptive modulation hypothesis predicts that activities of digestive enzymes should match the relative levels of their substrates in an animal’s diet so that available membrane space and synthetic energy are not wasted on enzymes in excess of need. However, previous studies on captive passerine birds showed high intraspecific phenotypic flexibility only in proteases but not in carbohydrases in response to varying diet composition. In this study, we measured the activities of pancreatic, intestinal, and hepatic enzymes in six wild-caught passerine species. We predicted that if the adaptive modulation hypothesis holds during evolutionary shifts in diet composition in birds, then mass-specific activities of digestive enzymes should be correlated positively with the content of their relevant substrates in species’ diets. Whereas mass-specific activities of proteases (aminopeptidase-N, trypsin, chymotrypsin, alanine aminotransferase) were not correlated with estimated dietary protein content, mass-specific activities of all studied carbohydrases (amylase, maltase, sucrase) were positively correlated with estimated dietary starch content. We conclude that activities of carbohydrases but not proteases are evolutionarily matched to diet composition in passerine birds. We hypothesize that the need for nitrogen and essential amino acids can prevent the evolution of a low activity of proteases, even in species feeding on a low-protein diet.
publishDate 2011
dc.date.none.fl_str_mv 2011-03
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/11336/14628
Kohl, Kevin D.; Brzek, Pawel; Caviedes Vidal, Enrique Juan Raul; Karasov, William H.; Pancreatic and intestinal carbohydrases are matched to dietary starch level in wild passerine birds; University of Chicago Press; Physiological and Biochemical Zoology; 84; 2; 3-2011; 195-203
1522-2152
1537-5293
url http://hdl.handle.net/11336/14628
identifier_str_mv Kohl, Kevin D.; Brzek, Pawel; Caviedes Vidal, Enrique Juan Raul; Karasov, William H.; Pancreatic and intestinal carbohydrases are matched to dietary starch level in wild passerine birds; University of Chicago Press; Physiological and Biochemical Zoology; 84; 2; 3-2011; 195-203
1522-2152
1537-5293
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.jstor.org/stable/10.1086/658146
info:eu-repo/semantics/altIdentifier/doi/10.1086/658146
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 University of Chicago Press
publisher.none.fl_str_mv University of Chicago 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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