Aerobic exercise training rescues protein quality control disruption on white skeletal muscle induced by chronic kidney disease in rats

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dc.contributorSistema FMUSP-HC: Faculdade de Medicina da Universidade de São Paulo (FMUSP) e Hospital das Clínicas da FMUSP
dc.contributor.authorMORAES, Wilson Max Almeida Monteiro De
dc.contributor.authorSOUZA, Pamella Ramona Moraes de
dc.contributor.authorPAIXAO, Nathalie Alves da
dc.contributor.authorSOUSA, Luis Gustavo Oliveira de
dc.contributor.authorRIBEIRO, Daniel Araki
dc.contributor.authorMARSHALL, Andrea G.
dc.contributor.authorPRESTES, Jonato
dc.contributor.authorIRIGOYEN, Maria Claudia
dc.contributor.authorBRUM, Patricia Chakur
dc.contributor.authorMEDEIROS, Alessandra
dc.date.accessioned2018-05-08T14:38:09Z
dc.date.available2018-05-08T14:38:09Z
dc.date.issued2018
dc.description.abstractWe tested whether aerobic exercise training (AET) would modulate the skeletal muscle protein quality control (PQC) in a model of chronic kidney disease (CKD) in rats. Adult Wistar rats were evaluated in four groups: control (CS) or trained (CE), and 5/6 nephrectomy sedentary (5/6NxS) or trained (5/6NxE). Exercised rats were submitted to treadmill exercise (60min., five times/wk for 2months). We evaluated motor performance (tolerance to exercise on the treadmill and rotarod), cross-sectional area (CSA), gene and protein levels related to the unfolded protein response (UPR), protein synthesis/survive and apoptosis signalling, accumulated misfolded proteins, chymotrypsin-like proteasome activity (UPS activity), redox balance and heat-shock protein (HSP) levels in the tibialis anterior. 5/6NxS presented a trend towards to atrophy, with a reduction in motor performance, down-regulation of protein synthesis and up-regulation of apoptosis signalling; increases in UPS activity, misfolded proteins, GRP78, derlin, HSP27 and HSP70 protein levels, ATF4 and GRP78 genes; and increase in oxidative damage compared to CS group. In 5/6NxE, we observed a restoration in exercise tolerance, accumulated misfolded proteins, UPS activity, protein synthesis/apoptosis signalling, derlin, HSPs protein levels as well as increase in ATF4, GRP78 genes and ATF6 protein levels accompanied by a decrease in oxidative damage and increased catalase and glutathione peroxidase activities. The results suggest a disruption of PQC in white muscle fibres of CKD rats previous to the atrophy. AET can rescue this disruption for the UPR, prevent accumulated misfolded proteins and reduce oxidative damage, HSPs protein levels and exercise tolerance.
dc.description.indexMEDLINE
dc.description.sponsorshipCoordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES) [12/51090-1]
dc.description.sponsorshipFundacao de Amparoa Pesquisa do Estado de Sao Paulo (FAPESP) [15/198936-0]
dc.identifier.citationJOURNAL OF CELLULAR AND MOLECULAR MEDICINE, v.22, n.3, p.1452-1463, 2018
dc.identifier.doi10.1111/jcmm.13374
dc.identifier.issn1582-4934
dc.identifier.urihttps://observatorio.fm.usp.br/handle/OPI/26526
dc.language.isoeng
dc.publisherWILEY
dc.relation.ispartofJournal of Cellular and Molecular Medicine
dc.rightsopenAccess
dc.rights.holderCopyright WILEY
dc.subjectchronic kidney disease
dc.subjectaerobic exercise training
dc.subjectskeletal muscle
dc.subjectprotein quality control
dc.subjectunfolded protein response
dc.subject.otherchronic-renal-failure
dc.subject.otherubiquitin-proteasome pathway
dc.subject.otherendoplasmic-reticulum stress
dc.subject.otheroxidative stress
dc.subject.othercatabolic conditions
dc.subject.otherendurance
dc.subject.othersurvival
dc.subject.otherdegradation
dc.subject.otherproteolysis
dc.subject.otheractivation
dc.subject.wosCell Biology
dc.subject.wosMedicine, Research & Experimental
dc.titleAerobic exercise training rescues protein quality control disruption on white skeletal muscle induced by chronic kidney disease in rats
dc.typearticle
dc.type.categoryoriginal article
dc.type.versionpublishedVersion
dspace.entity.typePublication
hcfmusp.affiliation.countryEstados Unidos
hcfmusp.affiliation.countryisous
hcfmusp.author.externalMORAES, Wilson Max Almeida Monteiro De:Univ Fed Sao Paulo, Biosci Dept, Santos, Brazil; Catholic Univ Brasilia UCB, Postgrad Program Phys Educ, Brasilia, DF, Brazil
hcfmusp.author.externalSOUZA, Pamella Ramona Moraes de:Nove de Julho Univ UNINOVE, Dept Postgrad Med, Sao Paulo, Brazil
hcfmusp.author.externalPAIXAO, Nathalie Alves da:Univ Sao Paulo, Sch Phys Educ & Sport, Sao Paulo, Brazil
hcfmusp.author.externalSOUSA, Luis Gustavo Oliveira de:Univ Sao Paulo, Dept Physiol & Biophys, Inst Biomed Sci, Sao Paulo, Brazil
hcfmusp.author.externalRIBEIRO, Daniel Araki:Univ Fed Sao Paulo, Biosci Dept, Santos, Brazil
hcfmusp.author.externalMARSHALL, Andrea G.:Univ Calif Davis, Dept Neurobiol Physiol & Behav, Davis, CA 95616 USA
hcfmusp.author.externalPRESTES, Jonato:Catholic Univ Brasilia UCB, Postgrad Program Phys Educ, Brasilia, DF, Brazil
hcfmusp.author.externalBRUM, Patricia Chakur:Nove de Julho Univ UNINOVE, Dept Postgrad Med, Sao Paulo, Brazil
hcfmusp.author.externalMEDEIROS, Alessandra:Univ Fed Sao Paulo, Biosci Dept, Santos, Brazil
hcfmusp.citation.scopus10
hcfmusp.contributor.author-fmusphcMARIA CLAUDIA COSTA IRIGOYEN
hcfmusp.description.beginpage1452
hcfmusp.description.endpage1463
hcfmusp.description.issue3
hcfmusp.description.volume22
hcfmusp.origemWOS
hcfmusp.origem.pubmed29265674
hcfmusp.origem.scopus2-s2.0-85042354136
hcfmusp.origem.wosWOS:000426069300007
hcfmusp.publisher.cityHOBOKEN
hcfmusp.publisher.countryUSA
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