Aerobic exercise training rescues protein quality control disruption on white skeletal muscle induced by chronic kidney disease in rats
Carregando...
Citações na Scopus
10
Tipo de produção
article
Data de publicação
2018
Título da Revista
ISSN da Revista
Título do Volume
Editora
WILEY
Autores
MORAES, Wilson Max Almeida Monteiro De
SOUZA, Pamella Ramona Moraes de
PAIXAO, Nathalie Alves da
SOUSA, Luis Gustavo Oliveira de
RIBEIRO, Daniel Araki
MARSHALL, Andrea G.
PRESTES, Jonato
BRUM, Patricia Chakur
MEDEIROS, Alessandra
Citação
JOURNAL OF CELLULAR AND MOLECULAR MEDICINE, v.22, n.3, p.1452-1463, 2018
Resumo
We 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.
Palavras-chave
chronic kidney disease, aerobic exercise training, skeletal muscle, protein quality control, unfolded protein response
Referências
- Adams GR, 2006, AM J PHYSIOL-RENAL, V290, pF753, DOI 10.1152/ajprenal.00296.2005
- AEBI H, 1984, METHOD ENZYMOL, V105, P121
- de Moraes WMAM, 2015, NUTRIENTS, V7, P3751, DOI 10.3390/nu7053751
- Antony JM, 2004, NAT NEUROSCI, V7, P1088, DOI 10.1038/nn1319
- Bailey JL, 1996, J CLIN INVEST, V97, P1447, DOI 10.1172/JCI118566
- Bergamaschi CT, 1997, MED SCI SPORT EXER, V29, P169, DOI 10.1097/00005768-199702000-00001
- Bozi LHM, 2016, J CELL MOL MED, V20, P2208, DOI 10.1111/jcmm.12894
- Calegari VC, 2012, J APPL PHYSIOL, V112, P711, DOI 10.1152/japplphysiol.00318.2011
- Chakrabarti A, 2011, BIOTECHNOL BIOENG, V108, P2777, DOI 10.1002/bit.23282
- Collins AJ, 2015, KIDNEY INT SUPPL, V5, P2, DOI 10.1038/kisup.2015.2
- Cunha TF, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0041701
- Deldicque L, 2013, FRONT PHYSIOL, V4, DOI 10.3389/fphys.2013.00236
- Deldicque L, 2013, J PHYSIOL BIOCHEM, V69, P215, DOI 10.1007/s13105-012-0204-9
- Deldicque L, 2012, EXERC SPORT SCI REV, V40, P43, DOI 10.1097/JES.0b013e3182355e8c
- Deldicque L, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0020993
- Dhanasekaran DN, 2008, ONCOGENE, V27, P6245, DOI 10.1038/onc.2008.301
- DIESEL W, 1993, AM J KIDNEY DIS, V22, P677, DOI 10.1016/S0272-6386(12)80430-6
- Drescher C, 2015, J CACHEXIA SARCOPENI, V6, P303, DOI 10.1002/jcsm.12082
- Du J, 2004, J CLIN INVEST, V113, P115, DOI 10.1172/JCI200418330
- Essig DA, 1997, CAN J APPL PHYSIOL, V22, P409, DOI 10.1139/h97-026
- Fahal IH, 1997, NEPHROL DIAL TRANSPL, V12, P119, DOI 10.1093/ndt/12.1.119
- Flisinski M, 2014, J PHYSIOL PHARMACOL, V65, P567
- Flisinski M, 2008, RENAL FAILURE, V30, P443, DOI 10.1080/08860220801985694
- FLOHE L, 1984, METHOD ENZYMOL, V105, P114
- Heiwe S, 2014, AM J KIDNEY DIS, V64, P383, DOI 10.1053/j.ajkd.2014.03.020
- Howden EJ, 2012, SPORTS MED, V42, P473, DOI 10.2165/11630800-000000000-00000
- Kanazawa M, 2006, AM J HYPERTENS, V19, P80, DOI 10.1016/j.amhyper.2005.07.009
- Konstantinidou E, 2002, J REHABIL MED, V34, P40, DOI 10.1080/165019702317242695
- Lecker SH, 2006, J AM SOC NEPHROL, V17, P1807, DOI 10.1681/ASN.2006010083
- LOTT JA, 1983, CLIN CHEM, V29, P1946
- Maloyan A, 2007, P NATL ACAD SCI USA, V104, P5995, DOI 10.1073/pnas.0609202104
- Manning BD, 2007, CELL, V129, P1261, DOI 10.1016/j.cell.2007.06.009
- Memme JM, 2016, AM J PHYSIOL-CELL PH, V310, pC1024, DOI 10.1152/ajpcell.00009.2016
- Moreira JBN, 2013, J APPL PHYSIOL, V114, P1029, DOI 10.1152/japplphysiol.00760.2012
- NOUROOZZADEH J, 1994, ANAL BIOCHEM, V220, P403, DOI 10.1006/abio.1994.1357
- Raj DSC, 2005, KIDNEY INT, V68, P2338, DOI 10.1111/j.1523-1755.2005.00695.x
- Sietsema KE, 2004, KIDNEY INT, V65, P719, DOI 10.1111/j.1523-1755.2004.00411.x
- Smolka MB, 2000, AM J PHYSIOL-REG I, V279, pR1539
- Tamaki M, 2014, KIDNEY INT, V85, P1330, DOI 10.1038/ki.2013.473
- Tice RR, 2000, ENVIRON MOL MUTAGEN, V35, P206, DOI 10.1002/(SICI)1098-2280(2000)35:3<206::AID-EM8>3.0.CO;2-J
- Turgeman T, 2008, NEUROMUSCULAR DISORD, V18, P857, DOI 10.1016/j.nmd.2008.06.386
- Venditti P, 1996, ARCH BIOCHEM BIOPHYS, V331, P63, DOI 10.1006/abbi.1996.0283
- Wang XNH, 2009, KIDNEY INT, V76, P751, DOI 10.1038/ki.2009.260
- Workeneh BT, 2006, J AM SOC NEPHROL, V17, P3233, DOI 10.1681/ASN.2006020131
- Wu J, 2011, CELL METAB, V13, P160, DOI 10.1016/j.cmet.2011.01.003
- Zoppi CC, 2008, SCAND J MED SCI SPOR, V18, P67, DOI 10.1111/j.1600-0838.2006.00630.x