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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/14628
Ver los metadatos del registro completo
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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‚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 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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1844614176517914624 |
score |
13.070432 |