dc.contributorUniv Fed Mato Grosso
dc.contributorUniversidade de São Paulo (USP)
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.creatorBatistela, Emanuele
dc.creatorPereira, Mayara Peron
dc.creatorSiqueira, Juliany Torres
dc.creatorPaula-Gomes, Silvia
dc.creatorZanon, Neusa Maria
dc.creatorOliveira, Eduardo Brandt
dc.creatorCarvalho Navegantes, Luiz Carlos
dc.creatorKettelhut, Isis C.
dc.creatorBalbinotti Andrade, Claudia Marlise
dc.creatorKawashita, Nair Honda
dc.creatorBaviera, Amanda Martins [UNESP]
dc.date2014-12-03T13:11:42Z
dc.date2014-12-03T13:11:42Z
dc.date2014-06-01
dc.date.accessioned2023-09-09T10:15:32Z
dc.date.available2023-09-09T10:15:32Z
dc.identifierhttp://dx.doi.org/10.1139/cjpp-2013-0290
dc.identifierCanadian Journal Of Physiology And Pharmacology. Ottawa: Canadian Science Publishing, Nrc Research Press, v. 92, n. 6, p. 445-454, 2014.
dc.identifier0008-4212
dc.identifierhttp://hdl.handle.net/11449/113432
dc.identifier10.1139/cjpp-2013-0290
dc.identifierWOS:000338712700004
dc.identifier3736475025187750
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8763031
dc.descriptionThe aim of this study was to investigate the changes in the rates of both protein synthesis and breakdown, and the activation of intracellular effectors that control these processes in soleus muscles from growing rats fed a low-protein, high-carbohydrate (LPHC) diet for 15 days. The mass and the protein content, as well as the rate of protein synthesis, were decreased in the soleus from LPHC-fed rats. The availability of amino acids was diminished, since the levels of various essential amino acids were decreased in the plasma of LPHC-fed rats. Overall rate of proteolysis was also decreased, explained by reductions in the mRNA levels of atrogin-1 and MuRF-1, ubiquitin conjugates, proteasome activity, and in the activity of caspase-3. Soleus muscles from LPHC-fed rats showed increased insulin sensitivity, with increased levels of insulin receptor and phosphorylation levels of AKT, which probably explains the inhibition of both the caspase-3 activity and the ubiquitin-proteasome system. The fall of muscle proteolysis seems to represent an adaptive response that contributes to spare proteins in a condition of diminished availability of dietary amino acids. Furthermore, the decreased rate of protein synthesis may be the driving factor to the lower muscle mass gain in growing rats fed the LPHC diet.
dc.descriptionFundacao de Amparo a Pesquisa do Estado de Mato Grosso (FAPEMAT)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionUniv Fed Mato Grosso, Dept Chem, Cuiaba, Mato Grosso, Brazil
dc.descriptionUniv Sao Paulo, Sch Med, Dept Biochem & Immunol, Sao Paulo, Brazil
dc.descriptionUniv Sao Paulo, Sch Med, Dept Physiol, Sao Paulo, Brazil
dc.descriptionSao Paulo State Univ, Sch Pharmaceut Sci, Dept Clin Anal, BR-14801360 Sao Paulo, Brazil
dc.descriptionSao Paulo State Univ, Sch Pharmaceut Sci, Dept Clin Anal, BR-14801360 Sao Paulo, Brazil
dc.descriptionFAPEMAT: 286326/2010
dc.format445-454
dc.languageeng
dc.publisherCanadian Science Publishing, Nrc Research Press
dc.relationCanadian Journal of Physiology and Pharmacology
dc.relation2.210
dc.relation0,724
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectlow-protein
dc.subjecthigh-carbohydrate diet
dc.subjectprotein synthesis
dc.subjectoverall proteolysis
dc.subjectcaspase-3 activity
dc.subjectubiquitin-proteasome system
dc.subjectinsulin sensitivity
dc.titleDecreased rate of protein synthesis, caspase-3 activity, and ubiquitin-proteasome proteolysis in soleus muscles from growing rats fed a low-protein, high-carbohydrate diet
dc.typeArtigo


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