Protein Blend and Casein Supplementations before Inactive Phase Similarly Activate Mechanistic Target of Rapamycin Signaling in Rat Skeletal Muscle

Detalhes bibliográficos
Autor(a) principal: Vieira, Tales Sambrano [UNESP]
Data de Publicação: 2020
Outros Autores: Pinto, Ana P., Batitucci, Gabriela [UNESP], Rocha, Alisson L., Filho, Hugo T., Goncalves, Dawit A., Silva, Adelino Sanchez R. da, Freitas, Ellen Cristini de [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.4103/CJP.CJP_31_20
http://hdl.handle.net/11449/209468
Resumo: During overnight sleep, the longest postabsorptive and inactive phase of the day causes protein catabolism and loss. However, the daytime ingestion of dairy proteins has been shown to stimulate muscle protein synthesis and growth. This study compared the effects of pre-sleep supplementation of a protein blend (PB) composed of micellar casein (MCa) and whey protein (1:1) versus isolate MCa on the plasma levels of branched-chain amino acids (BCAAs) and the activation of the mechanistic target of rapamycin (mTOR) signaling, a critical intracellular pathway involved in the regulation of muscle protein synthesis. After 10 h of fasting during the active phase, rats were fed with a single dose of PB or MCa (5.6 g protein/kg of body mass) by gavage, and samples of blood and gastrocnemius muscle were collected at 30, 90, and 450 min. PB and MCa supplementations induced an increase (similar to 3-fold, P < 0.001) of plasma BCAAs at 30 and 90 min. Most importantly, the stimulatory phosphorylation levels of mTOR and its downstream target p70 ribosomal protein S6 kinase (p70S6K) were similarly higher (similar to 2.5-fold, P < 0.001) 30 and 90 min after MCa and PB. Plasma levels of leucine, isoleucine, valine, and overall BCAAs were correlated with the activation of mTOR (P < 0.001) and p70S6K (P < 0.001). MCa and PB supplementations before the inactive phase of rats resulted in an anabolic milieu in the skeletal muscle by inducing a transient increase in plasma BCAAs and a similar activation of the mTOR/p70S6K axis.
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spelling Protein Blend and Casein Supplementations before Inactive Phase Similarly Activate Mechanistic Target of Rapamycin Signaling in Rat Skeletal MuscleMicellar caseinmTOR signaling pathwayprotein supplementationprotein synthesisskeletal musclewhey proteinDuring overnight sleep, the longest postabsorptive and inactive phase of the day causes protein catabolism and loss. However, the daytime ingestion of dairy proteins has been shown to stimulate muscle protein synthesis and growth. This study compared the effects of pre-sleep supplementation of a protein blend (PB) composed of micellar casein (MCa) and whey protein (1:1) versus isolate MCa on the plasma levels of branched-chain amino acids (BCAAs) and the activation of the mechanistic target of rapamycin (mTOR) signaling, a critical intracellular pathway involved in the regulation of muscle protein synthesis. After 10 h of fasting during the active phase, rats were fed with a single dose of PB or MCa (5.6 g protein/kg of body mass) by gavage, and samples of blood and gastrocnemius muscle were collected at 30, 90, and 450 min. PB and MCa supplementations induced an increase (similar to 3-fold, P < 0.001) of plasma BCAAs at 30 and 90 min. Most importantly, the stimulatory phosphorylation levels of mTOR and its downstream target p70 ribosomal protein S6 kinase (p70S6K) were similarly higher (similar to 2.5-fold, P < 0.001) 30 and 90 min after MCa and PB. Plasma levels of leucine, isoleucine, valine, and overall BCAAs were correlated with the activation of mTOR (P < 0.001) and p70S6K (P < 0.001). MCa and PB supplementations before the inactive phase of rats resulted in an anabolic milieu in the skeletal muscle by inducing a transient increase in plasma BCAAs and a similar activation of the mTOR/p70S6K axis.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Pro-Reitoria de Pesquisa da Universidade Federal de Minas GeraisState Univ Sao Paulo, Sch Pharmaceut Sci Araraquara, Dept Food & Nutr, Araraquara, SP, BrazilUniv Sao Paulo, Ribeirao Preto Med Sch, Dept Hlth Sci, Postgrad Program Rehabil & Funct Performance, Ribeirao Preto, SP, BrazilUniv Sao Paulo, Sch Phys Educ & Sport Ribeirao Preto, Ave Bandeirantes 3900, BR-14040907 Ribeirao Preto, SP, BrazilUniv Sao Paulo, Dept Physiol & Biochem & Immunol, Ribeirao Preto Med Sch, Ribeirao Preto, SP, BrazilUniv Fed Minas Gerais, Educ Sch Phys Educ Physiotherapy & Occupat Therap, Dept Phys Educ, Belo Horizonte, MG, BrazilState Univ Sao Paulo, Sch Pharmaceut Sci Araraquara, Dept Food & Nutr, Araraquara, SP, BrazilFAPESP: 12/18861 0FAPESP: 2018/19107 3CAPES: 001Pro-Reitoria de Pesquisa da Universidade Federal de Minas Gerais: 27764*27Wolters Kluwer Medknow PublicationsUniversidade Estadual Paulista (Unesp)Universidade de São Paulo (USP)Universidade Federal de Minas Gerais (UFMG)Vieira, Tales Sambrano [UNESP]Pinto, Ana P.Batitucci, Gabriela [UNESP]Rocha, Alisson L.Filho, Hugo T.Goncalves, Dawit A.Silva, Adelino Sanchez R. daFreitas, Ellen Cristini de [UNESP]2021-06-25T12:19:33Z2021-06-25T12:19:33Z2020-07-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article171-178http://dx.doi.org/10.4103/CJP.CJP_31_20Chinese Journal Of Physiology. Mumbai: Wolters Kluwer Medknow Publications, v. 63, n. 4, p. 171-178, 2020.0304-4920http://hdl.handle.net/11449/20946810.4103/CJP.CJP_31_20WOS:000569856300004Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengChinese Journal Of Physiologyinfo:eu-repo/semantics/openAccess2024-06-21T12:47:11Zoai:repositorio.unesp.br:11449/209468Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T21:46:49.034704Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Protein Blend and Casein Supplementations before Inactive Phase Similarly Activate Mechanistic Target of Rapamycin Signaling in Rat Skeletal Muscle
title Protein Blend and Casein Supplementations before Inactive Phase Similarly Activate Mechanistic Target of Rapamycin Signaling in Rat Skeletal Muscle
spellingShingle Protein Blend and Casein Supplementations before Inactive Phase Similarly Activate Mechanistic Target of Rapamycin Signaling in Rat Skeletal Muscle
Vieira, Tales Sambrano [UNESP]
Micellar casein
mTOR signaling pathway
protein supplementation
protein synthesis
skeletal muscle
whey protein
title_short Protein Blend and Casein Supplementations before Inactive Phase Similarly Activate Mechanistic Target of Rapamycin Signaling in Rat Skeletal Muscle
title_full Protein Blend and Casein Supplementations before Inactive Phase Similarly Activate Mechanistic Target of Rapamycin Signaling in Rat Skeletal Muscle
title_fullStr Protein Blend and Casein Supplementations before Inactive Phase Similarly Activate Mechanistic Target of Rapamycin Signaling in Rat Skeletal Muscle
title_full_unstemmed Protein Blend and Casein Supplementations before Inactive Phase Similarly Activate Mechanistic Target of Rapamycin Signaling in Rat Skeletal Muscle
title_sort Protein Blend and Casein Supplementations before Inactive Phase Similarly Activate Mechanistic Target of Rapamycin Signaling in Rat Skeletal Muscle
author Vieira, Tales Sambrano [UNESP]
author_facet Vieira, Tales Sambrano [UNESP]
Pinto, Ana P.
Batitucci, Gabriela [UNESP]
Rocha, Alisson L.
Filho, Hugo T.
Goncalves, Dawit A.
Silva, Adelino Sanchez R. da
Freitas, Ellen Cristini de [UNESP]
author_role author
author2 Pinto, Ana P.
Batitucci, Gabriela [UNESP]
Rocha, Alisson L.
Filho, Hugo T.
Goncalves, Dawit A.
Silva, Adelino Sanchez R. da
Freitas, Ellen Cristini de [UNESP]
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Universidade de São Paulo (USP)
Universidade Federal de Minas Gerais (UFMG)
dc.contributor.author.fl_str_mv Vieira, Tales Sambrano [UNESP]
Pinto, Ana P.
Batitucci, Gabriela [UNESP]
Rocha, Alisson L.
Filho, Hugo T.
Goncalves, Dawit A.
Silva, Adelino Sanchez R. da
Freitas, Ellen Cristini de [UNESP]
dc.subject.por.fl_str_mv Micellar casein
mTOR signaling pathway
protein supplementation
protein synthesis
skeletal muscle
whey protein
topic Micellar casein
mTOR signaling pathway
protein supplementation
protein synthesis
skeletal muscle
whey protein
description During overnight sleep, the longest postabsorptive and inactive phase of the day causes protein catabolism and loss. However, the daytime ingestion of dairy proteins has been shown to stimulate muscle protein synthesis and growth. This study compared the effects of pre-sleep supplementation of a protein blend (PB) composed of micellar casein (MCa) and whey protein (1:1) versus isolate MCa on the plasma levels of branched-chain amino acids (BCAAs) and the activation of the mechanistic target of rapamycin (mTOR) signaling, a critical intracellular pathway involved in the regulation of muscle protein synthesis. After 10 h of fasting during the active phase, rats were fed with a single dose of PB or MCa (5.6 g protein/kg of body mass) by gavage, and samples of blood and gastrocnemius muscle were collected at 30, 90, and 450 min. PB and MCa supplementations induced an increase (similar to 3-fold, P < 0.001) of plasma BCAAs at 30 and 90 min. Most importantly, the stimulatory phosphorylation levels of mTOR and its downstream target p70 ribosomal protein S6 kinase (p70S6K) were similarly higher (similar to 2.5-fold, P < 0.001) 30 and 90 min after MCa and PB. Plasma levels of leucine, isoleucine, valine, and overall BCAAs were correlated with the activation of mTOR (P < 0.001) and p70S6K (P < 0.001). MCa and PB supplementations before the inactive phase of rats resulted in an anabolic milieu in the skeletal muscle by inducing a transient increase in plasma BCAAs and a similar activation of the mTOR/p70S6K axis.
publishDate 2020
dc.date.none.fl_str_mv 2020-07-01
2021-06-25T12:19:33Z
2021-06-25T12:19:33Z
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/10.4103/CJP.CJP_31_20
Chinese Journal Of Physiology. Mumbai: Wolters Kluwer Medknow Publications, v. 63, n. 4, p. 171-178, 2020.
0304-4920
http://hdl.handle.net/11449/209468
10.4103/CJP.CJP_31_20
WOS:000569856300004
url http://dx.doi.org/10.4103/CJP.CJP_31_20
http://hdl.handle.net/11449/209468
identifier_str_mv Chinese Journal Of Physiology. Mumbai: Wolters Kluwer Medknow Publications, v. 63, n. 4, p. 171-178, 2020.
0304-4920
10.4103/CJP.CJP_31_20
WOS:000569856300004
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Chinese Journal Of Physiology
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 171-178
dc.publisher.none.fl_str_mv Wolters Kluwer Medknow Publications
publisher.none.fl_str_mv Wolters Kluwer Medknow Publications
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
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