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
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
DOI: | 10.1016/j.jnutbio.2016.04.008 |
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. |
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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 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 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 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 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 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 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_ |
1822182334467670016 |
dc.identifier.doi.none.fl_str_mv |
10.1016/j.jnutbio.2016.04.008 |