Ubiquitin Proteasome System Activity is Suppressed by Curcumin following Exercise-Induced Muscle Damage in Human Skeletal Muscle

References

• Bilodeau PA, Coyne ES, Wing SS. The ubiquitin proteasome system in atrophying skeletal muscle: Roles and regulation. Am J Physiol Cell Physiol. 2016;311(3):C392–C403. doi:10.1152/ajpcell.00125.2016.
   PubMed Web of Science ®Google Scholar
• Jagoe RT, Goldberg AL. What do we really know about the ubiquitin-proteasome pathway in muscle atrophy? Current Opinion in. Clin Nutr Metab Care. 2001;4(3):183–90.
   PubMed Web of Science ®Google Scholar
• Schiaffino S, Dyar KA, Ciciliot S, Blaauw B, Sandri M. Mechanisms regulating skeletal muscle growth and atrophy. Febs J. 2013;280(17):4294–314. doi:10.1111/febs.12253.
   PubMed Web of Science ®Google Scholar
• Wing S, Lecker S, Jagoe R. Proteolysis in illness-associated skeletal muscle atrophy: from pathways to networks. Crit Rev Clin Lab Sci. 2011;48(2):49–70. doi:10.3109/10408363.2011.586171.
   PubMed Web of Science ®Google Scholar
• Murton AJ, Constantin D, Greenhaff PL. The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy. Biochim Biophys Acta. 2008;1782(12):730–43. doi:10.1016/j.bbadis.2008.10.011.
   PubMed Web of Science ®Google Scholar
• Passmore LA, Barford D. Getting into position: the catalytic mechanisms of protein ubiquitylation. Biochem J. 2004;379(Pt 3):513–25. doi:10.1042/BJ20040198.
   PubMedGoogle Scholar
• Thrower JS, Hoffman L, Rechsteiner M, Pickart CM. Recognition of the polyubiquitin proteolytic signal. Embo J. 2000;19(1):94–102. doi:10.1093/emboj/19.1.94.
   PubMed Web of Science ®Google Scholar
• Tanaka K. The proteasome: overview of structure and functions. Proc Jpn Acad, Ser B, Phys Biol Sci. 2009;85(1):12–36. doi:10.2183/pjab.85.12.
   PubMed Web of Science ®Google Scholar
• Kish-Trier E, Hill CP. Structural biology of the proteasome. Annu Rev Biophys. 2013;42:29–49. doi:10.1146/annurev-biophys-083012-130417.
   PubMed Web of Science ®Google Scholar
• Liu J, Shaik S, Dai X, Wu Q, Zhou X, Wang Z, Wei W. Targeting the ubiquitin pathway for cancer treatment. Biochim Biophys Acta. 2015;1855(1):50–60. doi:10.1016/j.bbcan.2014.11.005.
   PubMed Web of Science ®Google Scholar
• Reyes-Turcu FE, Ventii KH, Wilkinson KD. Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu Rev Biochem. 2009;78:363–97. doi:10.1146/annurev.biochem.78.082307.091526.
   PubMed Web of Science ®Google Scholar
• Buford TW, Cooke MB, Redd LZ, Hudson GM, Shelmadine BD, Willoughby DS. Protease supplementation improves muscle function after eccentric exercise. Med Sci Sports Exercise. 2009;41(10):1908–14.
   PubMed Web of Science ®Google Scholar
• Fielding RA, Manfredi TJ, Ding W, Fiatarone MA, Evans WJ, Cannon JG. Acute phase response in exercise. III. neutrophil and IL-1 beta accumulation in skeletal muscle. Am J Physiol. 1993;265(1):R166–R172. doi:10.1152/ajpregu.1993.265.1.R166.
   PubMed Web of Science ®Google Scholar
• Fridén J, Sjöström J, Ekblom B. A morphological study of delayed muscle soreness. Experientia. 1981;37(5):506–7. doi:10.1007/BF01986165.
   PubMedGoogle Scholar
• Fridén J, Sjöström J, Ekblom B. Myofibrillar damage following intense eccentric exercise in man. Int J Sports Med. 1983;4(3):170–6. doi:10.1055/s-2008-1026030.
   PubMed Web of Science ®Google Scholar
• Nosaka K, Clarkson P. Relationship between post-exercise plasma CK elevation and muscle mass involved in the exercise. Int J Sports Med. 1992;13(06):471–5. doi:10.1055/s-2007-1021300.
   PubMedGoogle Scholar
• Willoughby DS, Taylor M, Taylor L. Glucocorticoid receptor and ubiquitin expression after repeated eccentric exercise. Med Sci Sports Exercise. 2003;35(12):2023–31.
   PubMed Web of Science ®Google Scholar
• Thompson HS, Scordilis SP. Ubiquitin changes in human biceps muscle following exercise-induced damage. Biochem Biophys Res Commun. 1994;204(3):1193–8. doi:10.1006/bbrc.1994.2589.
   PubMed Web of Science ®Google Scholar
• Willoughby DS, Rosene J, Myers J. HSP-72 and ubiquitin expression and caspase-3 activity after a single bout of eccentric exercise. J Exercise Physiol Online. 2003;6(2):96–104.
   Google Scholar
• Clarke BA, Drujan D, Willis MS, Murphy LO, Corpina RA, Burova E, Rakhilin SV, Stitt TN, Patterson C, Latres E, et al. The E3 ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle. Cell Metab. 2007;6(5):376–85. doi:10.1016/j.cmet.2007.09.009.
   PubMed Web of Science ®Google Scholar
• Cohen S, Brault JJ, Gygi SP, Glass DJ, Valenzuela DM, Gartner C, Latres E, Goldberg AL. During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation. J Cell Biol. 2009;185(6):1083–95. doi:10.1083/jcb.200901052.
   PubMed Web of Science ®Google Scholar
• Csibi A, Cornille K, Leibovitch MP, Poupon A, Tintignac LA, Sanchez AMJ, Leibovitch SA. The translation regulatory subunit eIF3f controls the kinase-dependent mTOR signaling required for muscle differentiation and hypertrophy in mouse. PloS One. 2010;5(2):e8994doi:10.1371/journal.pone.0008994.
   PubMed Web of Science ®Google Scholar
• Fielitz J, Kim M-S, Shelton JM, Latif S, Spencer JA, Glass DJ, Richardson JA, Bassel-Duby R, Olson EN. Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3. J Clin Invest. 2007;117(9):2486–95. doi:10.1172/JCI32827.
   PubMed Web of Science ®Google Scholar
• Kedar V, McDonough H, Arya R, Li HH, Rockman HA, Patterson C. Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I. Proc Natl Acad Sci USA. 2004;101(52):18135–40. doi:10.1073/pnas.0404341102.
   PubMed Web of Science ®Google Scholar
• Polge C, Heng A-E, Jarzaguet M, Ventadour S, Claustre A, Combaret L, Béchet D, Matondo M, Uttenweiler-Joseph S, Monsarrat B, et al. Muscle actin is polyubiquitinylated in vitro and in vivo and targeted for breakdown by the E3 ligase MuRF1. Faseb J. 2011;25(11):3790–802. doi:10.1096/fj.11-180968.
   PubMed Web of Science ®Google Scholar
• Sandri M. Protein breakdown in muscle wasting: role of autophagy-lysosome and ubiquitin-proteasome. Int J Biochem Cell Biol. 2013;45(10):2121–9. doi:10.1016/j.biocel.2013.04.023.
   PubMed Web of Science ®Google Scholar
• Tintignac LA, Lagirand J, Batonnet S, Sirri V, Leibovitch MP, Leibovitch SA. Degradation of MyoD mediated by the SCF (MAFbx) ubiquitin ligase. J Biol Chem. 2005;280(4):2847–56. [Database] doi:10.1074/jbc.M411346200.
   PubMed Web of Science ®Google Scholar
• Jamart C, Raymackers JM, Li An G, Deldicque L, Francaux M. Prevention of muscle disuse atrophy by MG132 proteasome inhibitor. Muscle Nerve. 2011;43(5):708–15. doi:10.1002/mus.21949.
   PubMed Web of Science ®Google Scholar
• Yin L, Krantz B, Russell NS, Deshpande S, Wilkinson KD. Nonhydrolyzable diubiquitin analogues are inhibitors of ubiquitin conjugation and deconjugation. Biochemistry. 2000;39(32):10001–10. doi:10.1021/bi0007019.
   PubMed Web of Science ®Google Scholar
• Merin NM, Kelly KR. Clinical use of proteasome inhibitors in the treatment of multiple myeloma. Pharmaceuticals (Basel). 2014;8(1):1–‐20. doi:10.3390/ph8010001.
   PubMedGoogle Scholar
• Dikshit P, Goswami A, Mishra A, Chatterjee M, Jana NR. Curcumin induces stress response, neurite outgrowth and prevent NF-kappaB activation by inhibiting the proteasome function . Neurotox Res. 2006;9(1):29–37. doi:10.1007/BF03033305.
   PubMed Web of Science ®Google Scholar
• Jana NR, Dikshit P, Goswami A, Nukina N. Inhibition of proteasomal function by curcumin induces apoptosis through mitochondrial pathway. J Biol Chem. 2004;279(12):11680–5. doi:10.1074/jbc.M310369200.
   PubMed Web of Science ®Google Scholar
• Milacic V, Banerjee S, Landis-Piwowar KR, Sarkar FH, Majumdar APN, Dou QP. Curcumin inhibits the proteasome activity in human colon cancer cells in vitro and in vivo. Cancer Res. 2008;68(18):7283–92. doi:10.1158/0008-5472.CAN-07-6246.
   PubMed Web of Science ®Google Scholar
• Mullally JE, Fitzpatrick FA. Pharmacophore model for novel inhibitors of ubiquitin isopeptidases that induce p53-independent cell death. Mol Pharmacol. 2002;62(2):351–8. doi:10.1124/mol.62.2.351.
   PubMed Web of Science ®Google Scholar
• Si X, Wang Y, Wong J, Zhang J, McManus BM, Luo H. Dysregulation of the ubiquitin-proteasome system by curcumin suppresses coxsackievirus B3 replication. J Virol. 2007;81(7):3142–50. doi:10.1128/JVI.02028-06.
   PubMed Web of Science ®Google Scholar
• Fernández-Lázaro D, Mielgo-Ayuso J, Seco Calvo J, Córdova Martínez A, Caballero García A, Fernandez-Lazaro CI. Modulation of exercise-induced muscle damage, inflammation, and oxidative markers by curcumin supplementation in a physically active population: a systematic review. Nutrients. 2020;12(2):501. doi:10.3390/nu12020501.
   PubMed Web of Science ®Google Scholar
• Shelmadine B, Cooke M, Buford T, Hudson G, Redd L, Leutholtz B, Willoughby DS. Effects of 28 days of resistance exercise and consuming a commercially available pre-workout supplement, NO-Shotgun, on body composition, muscle strength and mass, markers of satellite cell activation, and clinical safety markers in males. J Int Soc Sports Nutr. 2009;6(1):16. doi:10.1186/1550-2783-6-16.
   PubMedGoogle Scholar
• Spillane M, Schwarz N, Leddy S, Correa T, Minter M, Longoria V, Willoughby DS. Effects of 28 days of resistance exercise while consuming commercially available pre- and post-workout supplements, NO-Shotgun and NO-Synthesize® on body composition, muscle strength and mass, markers of protein synthesis, and clinical safety markers in males. Nutr Metab (Lond). 2011;8(1):78. doi:10.1186/1743-7075-8-78.
   PubMedGoogle Scholar
• Willoughby DS, Leutholtz BD. Aspartic acid supplementation combined with 28 days of heavy resistance training has no effect on body composition, muscle strength, and serum hormones associated with the hypothalamo-pituitary-gonadal axis in resistance-trained men. Nutr Res. 2013;33(10):803–10. doi:10.1016/j.nutres.2013.07.010.
   PubMed Web of Science ®Google Scholar
• Fielding RA, Frontera WR, Hughes VA, Fisher EC, Evans WJ. The reproducibility of the Bruce protocol exercise test for the determination of aerobic capacity in older women. Med Sci Sports Exercise. 1997;29(8):1109–13.
   PubMed Web of Science ®Google Scholar
• Buford TW, Cooke MB, Shelmadine BD, Hudson GM, Redd L, Willoughby DS. Effects of eccentric treadmill exercise on inflammatory gene expression in human skeletal muscle. Appl Physiol Nutr Metab. 2009;34(4):745–53. doi:10.1139/H09-067.
   PubMed Web of Science ®Google Scholar
• Kim J, Lee J. The relationship of creatine kinase variability with body composition and muscle damage markers following eccentric muscle contractions. Journal of Exercise Nutrition & Biochemistry. 2015;19(2):123–9. doi:10.5717/jenb.2015.15061910.
   PubMedGoogle Scholar
• Shoba G, Joy D, Joseph T, Majeed M, Rajendran R, Srinivas PS. Influence of piperine on the pharmacokinetics of curcumin in animals and human volunteers. Planta Med. 1998;64(04):353–6. doi:10.1055/s-2006-957450.
   PubMed Web of Science ®Google Scholar
• Bakeman R. Recommended effect size statistics for repeated measures designs. Behav Res Methods. 2005;37(3):379–84. doi:10.3758/bf03192707.
   PubMed Web of Science ®Google Scholar
• Fernandes JFT, Lamb KL, Twist C. Exercise-induced muscle damage and recovery in young and middle-aged males with different resistance training experience. Sports (Basel). 2019;7(6):132. doi:10.3390/sports7060132.
   Google Scholar
• Nicol LM, Rowlands DS, Fazakerly R, Kellett J. Curcumin supplementation likely attenuates delayed onset muscle soreness (DOMS). Eur J Appl Physiol. 2015;115(8):1769–77. doi:10.1007/s00421-015-3152-6.
   PubMed Web of Science ®Google Scholar
• Bhaumik S, Anjum R, Rangaraj N, Pardhasaradhi BV, Khar A. Curcumin mediated apoptosis in AK-5 tumor cells involves the production of reactive oxygen intermediates. FEBS Lett. 1999;456(2):311–4. doi:10.1016/s0014-5793(99)00969-2.
   PubMed Web of Science ®Google Scholar
• Woo J-H, Kim Y-H, Choi Y-J, Kim D-G, Lee K-S, Bae JH, Min DS, Chang J-S, Jeong Y-J, Lee YH, et al. Molecular mechanisms of curcumin-induced cytotoxicity: induction of apoptosis through generation of reactive oxygen species, down-regulation of Bcl-XL and IAP, the release of cytochrome c and inhibition of Akt. Carcinogenesis. 2003;24(7):1199–208. doi:10.1093/carcin/bgg082.
   PubMed Web of Science ®Google Scholar