Higher insulin sensitivity in EDL muscle of rats fed a low-protein, high-carbohydrate diet inhibits the caspase-3 and ubiquitin-proteasome proteolytic systems but does not increase protein synthesis

Detalhes bibliográficos
Autor(a) principal: Santos, Maisa Pavani dos
Data de Publicação: 2016
Outros Autores: Batistela, Emanuele, Pereira, Mayara Peron, Paula-Gomes, Silvia, Zanon, Neusa Maria, Kettelhut, Isis do Carmo, Karatzaferi, Christina, Balbinotti Andrade, Claudia Marlise, Franca, Suelem Aparecida de, Baviera, Amanda Martins [UNESP], Kawashita, Nair Honda
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/j.jnutbio.2016.04.008
http://hdl.handle.net/11449/161762
Resumo: Compared with the extensor digitorum longus (EDL) muscle of control rats (C), the EDL muscle of rats fed a low-protein, high-carbohydrate diet (LPHC) showed a 36% reduction in mass. Muscle mass is determined by the balance between protein synthesis and proteolysis; thus, the aim of this work was to evaluate the components involved in these processes. Compared with the muscle from C rats, the EDL muscle from LPHC diet-fed rats showed a reduction (34%) in the in vitro basal protein synthesis and a 22% reduction in the in vitro basal proteolysis suggesting that the reduction in the mass can be associated with a change in the rate of the two processes. Soon after euthanasia, in the EDL muscles of the rats fed the LPHC diet for 15 days, the activity of caspase-3 and that of components of the ubiquitin-proteasome system (atrogin-1 content and chymotrypsin-like activity) were decreased. The phosphorylation of p70(S6K) and 4E-BP1, proteins involved in protein synthesis, was also decreased. We observed an increase in the insulin-stimulated protein content of p-Akt. Thus, the higher insulin sensitivity in the EDL muscle of LPHC rats seemed to contribute to the lower proteolysis in LPHC rats. However, even with the higher insulin sensitivity, the reduction in p-E4-BP1 and p70(S6K) indicates a reduction in protein synthesis, showing that factors other than insulin can have a greater effect on the control of protein synthesis. (C) 2016 Elsevier Inc. All rights reserved.
id UNSP_0a6ccdc760e6b56f18a500a7f761cbb0
oai_identifier_str oai:repositorio.unesp.br:11449/161762
network_acronym_str UNSP
network_name_str Repositório Institucional da UNESP
repository_id_str 2946
spelling Higher insulin sensitivity in EDL muscle of rats fed a low-protein, high-carbohydrate diet inhibits the caspase-3 and ubiquitin-proteasome proteolytic systems but does not increase protein synthesisLow-proteinhigh-carbohydrate dietProtein synthesisProteolytic pathwaysExtensor digitorum longusInsulin sensitivityGrowing ratsCompared with the extensor digitorum longus (EDL) muscle of control rats (C), the EDL muscle of rats fed a low-protein, high-carbohydrate diet (LPHC) showed a 36% reduction in mass. Muscle mass is determined by the balance between protein synthesis and proteolysis; thus, the aim of this work was to evaluate the components involved in these processes. Compared with the muscle from C rats, the EDL muscle from LPHC diet-fed rats showed a reduction (34%) in the in vitro basal protein synthesis and a 22% reduction in the in vitro basal proteolysis suggesting that the reduction in the mass can be associated with a change in the rate of the two processes. Soon after euthanasia, in the EDL muscles of the rats fed the LPHC diet for 15 days, the activity of caspase-3 and that of components of the ubiquitin-proteasome system (atrogin-1 content and chymotrypsin-like activity) were decreased. The phosphorylation of p70(S6K) and 4E-BP1, proteins involved in protein synthesis, was also decreased. We observed an increase in the insulin-stimulated protein content of p-Akt. Thus, the higher insulin sensitivity in the EDL muscle of LPHC rats seemed to contribute to the lower proteolysis in LPHC rats. However, even with the higher insulin sensitivity, the reduction in p-E4-BP1 and p70(S6K) indicates a reduction in protein synthesis, showing that factors other than insulin can have a greater effect on the control of protein synthesis. (C) 2016 Elsevier Inc. All rights reserved.Fundacao de Amparo a Pesquisa do Estado de Mato GrossoUniv Fed Mato Grosso, Dept Chem, Cuiaba, Mato Grosso, BrazilUniv Sao Paulo, Dept Biochem & Immunol, Sch Med, Sao Paulo, BrazilUniv St Mark & St John, Fac Sport & Hlth Sci, Plymouth, Devon, EnglandSao Paulo State Univ, Sch Pharmaceut Sci, Dept Clin Anal, Sao Paulo, BrazilSao Paulo State Univ, Sch Pharmaceut Sci, Dept Clin Anal, Sao Paulo, BrazilFundacao de Amparo a Pesquisa do Estado de Mato Grosso: FAPEMAT 286326/2010Fundacao de Amparo a Pesquisa do Estado de Mato Grosso: FAPEMAT 222560/2015Elsevier B.V.Universidade Federal de Mato Grosso do Sul (UFMS)Universidade de São Paulo (USP)Univ St Mark & St JohnUniversidade Estadual Paulista (Unesp)Santos, Maisa Pavani dosBatistela, EmanuelePereira, Mayara PeronPaula-Gomes, SilviaZanon, Neusa MariaKettelhut, Isis do CarmoKaratzaferi, ChristinaBalbinotti Andrade, Claudia MarliseFranca, Suelem Aparecida deBaviera, Amanda Martins [UNESP]Kawashita, Nair Honda2018-11-26T16:48:31Z2018-11-26T16:48:31Z2016-08-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article89-98application/pdfhttp://dx.doi.org/10.1016/j.jnutbio.2016.04.008Journal Of Nutritional Biochemistry. New York: Elsevier Science Inc, v. 34, p. 89-98, 2016.0955-2863http://hdl.handle.net/11449/16176210.1016/j.jnutbio.2016.04.008WOS:000380421700010WOS000380421700010.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal Of Nutritional Biochemistry1,678info:eu-repo/semantics/openAccess2024-06-21T15:18:57Zoai:repositorio.unesp.br:11449/161762Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T18:31:45.741643Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Higher insulin sensitivity in EDL muscle of rats fed a low-protein, high-carbohydrate diet inhibits the caspase-3 and ubiquitin-proteasome proteolytic systems but does not increase protein synthesis
title Higher insulin sensitivity in EDL muscle of rats fed a low-protein, high-carbohydrate diet inhibits the caspase-3 and ubiquitin-proteasome proteolytic systems but does not increase protein synthesis
spellingShingle Higher insulin sensitivity in EDL muscle of rats fed a low-protein, high-carbohydrate diet inhibits the caspase-3 and ubiquitin-proteasome proteolytic systems but does not increase protein synthesis
Santos, Maisa Pavani dos
Low-protein
high-carbohydrate diet
Protein synthesis
Proteolytic pathways
Extensor digitorum longus
Insulin sensitivity
Growing rats
title_short Higher insulin sensitivity in EDL muscle of rats fed a low-protein, high-carbohydrate diet inhibits the caspase-3 and ubiquitin-proteasome proteolytic systems but does not increase protein synthesis
title_full Higher insulin sensitivity in EDL muscle of rats fed a low-protein, high-carbohydrate diet inhibits the caspase-3 and ubiquitin-proteasome proteolytic systems but does not increase protein synthesis
title_fullStr Higher insulin sensitivity in EDL muscle of rats fed a low-protein, high-carbohydrate diet inhibits the caspase-3 and ubiquitin-proteasome proteolytic systems but does not increase protein synthesis
title_full_unstemmed Higher insulin sensitivity in EDL muscle of rats fed a low-protein, high-carbohydrate diet inhibits the caspase-3 and ubiquitin-proteasome proteolytic systems but does not increase protein synthesis
title_sort Higher insulin sensitivity in EDL muscle of rats fed a low-protein, high-carbohydrate diet inhibits the caspase-3 and ubiquitin-proteasome proteolytic systems but does not increase protein synthesis
author Santos, Maisa Pavani dos
author_facet Santos, Maisa Pavani dos
Batistela, Emanuele
Pereira, Mayara Peron
Paula-Gomes, Silvia
Zanon, Neusa Maria
Kettelhut, Isis do Carmo
Karatzaferi, Christina
Balbinotti Andrade, Claudia Marlise
Franca, Suelem Aparecida de
Baviera, Amanda Martins [UNESP]
Kawashita, Nair Honda
author_role author
author2 Batistela, Emanuele
Pereira, Mayara Peron
Paula-Gomes, Silvia
Zanon, Neusa Maria
Kettelhut, Isis do Carmo
Karatzaferi, Christina
Balbinotti Andrade, Claudia Marlise
Franca, Suelem Aparecida de
Baviera, Amanda Martins [UNESP]
Kawashita, Nair Honda
author2_role author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Federal de Mato Grosso do Sul (UFMS)
Universidade de São Paulo (USP)
Univ St Mark & St John
Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Santos, Maisa Pavani dos
Batistela, Emanuele
Pereira, Mayara Peron
Paula-Gomes, Silvia
Zanon, Neusa Maria
Kettelhut, Isis do Carmo
Karatzaferi, Christina
Balbinotti Andrade, Claudia Marlise
Franca, Suelem Aparecida de
Baviera, Amanda Martins [UNESP]
Kawashita, Nair Honda
dc.subject.por.fl_str_mv Low-protein
high-carbohydrate diet
Protein synthesis
Proteolytic pathways
Extensor digitorum longus
Insulin sensitivity
Growing rats
topic Low-protein
high-carbohydrate diet
Protein synthesis
Proteolytic pathways
Extensor digitorum longus
Insulin sensitivity
Growing rats
description Compared with the extensor digitorum longus (EDL) muscle of control rats (C), the EDL muscle of rats fed a low-protein, high-carbohydrate diet (LPHC) showed a 36% reduction in mass. Muscle mass is determined by the balance between protein synthesis and proteolysis; thus, the aim of this work was to evaluate the components involved in these processes. Compared with the muscle from C rats, the EDL muscle from LPHC diet-fed rats showed a reduction (34%) in the in vitro basal protein synthesis and a 22% reduction in the in vitro basal proteolysis suggesting that the reduction in the mass can be associated with a change in the rate of the two processes. Soon after euthanasia, in the EDL muscles of the rats fed the LPHC diet for 15 days, the activity of caspase-3 and that of components of the ubiquitin-proteasome system (atrogin-1 content and chymotrypsin-like activity) were decreased. The phosphorylation of p70(S6K) and 4E-BP1, proteins involved in protein synthesis, was also decreased. We observed an increase in the insulin-stimulated protein content of p-Akt. Thus, the higher insulin sensitivity in the EDL muscle of LPHC rats seemed to contribute to the lower proteolysis in LPHC rats. However, even with the higher insulin sensitivity, the reduction in p-E4-BP1 and p70(S6K) indicates a reduction in protein synthesis, showing that factors other than insulin can have a greater effect on the control of protein synthesis. (C) 2016 Elsevier Inc. All rights reserved.
publishDate 2016
dc.date.none.fl_str_mv 2016-08-01
2018-11-26T16:48:31Z
2018-11-26T16:48:31Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/j.jnutbio.2016.04.008
Journal Of Nutritional Biochemistry. New York: Elsevier Science Inc, v. 34, p. 89-98, 2016.
0955-2863
http://hdl.handle.net/11449/161762
10.1016/j.jnutbio.2016.04.008
WOS:000380421700010
WOS000380421700010.pdf
url http://dx.doi.org/10.1016/j.jnutbio.2016.04.008
http://hdl.handle.net/11449/161762
identifier_str_mv Journal Of Nutritional Biochemistry. New York: Elsevier Science Inc, v. 34, p. 89-98, 2016.
0955-2863
10.1016/j.jnutbio.2016.04.008
WOS:000380421700010
WOS000380421700010.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Journal Of Nutritional Biochemistry
1,678
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 89-98
application/pdf
dc.publisher.none.fl_str_mv Elsevier B.V.
publisher.none.fl_str_mv Elsevier B.V.
dc.source.none.fl_str_mv Web of Science
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
_version_ 1808128942528266240