The Role of Mitochondrial Stress in Muscle Wasting Following Severe Burn Trauma
Open accessAbstract
Increased resting metabolic rate and skeletal muscle wasting are hallmarks of the pathophysiological stress response to severe burn trauma. However, whether these two responses occur independently in burn patients or are in fact related remains unclear. In light of recent evidence demonstrating that increased proteolysis in skeletal muscle of burned patients is accompanied by mitochondrial hypermetabolism, oxidative stress, and protein damage; in this article, we discuss the evidence for a role for the mitochondrion in skeletal muscle wasting following severe burn trauma. In particular, we focus on the role of mitochondrial superoxide production in oxidative stress and subsequent proteolysis, and discuss the role of the mitochondrion as a signaling organelle resulting in protein catabolism in other cellular compartments following severe burn trauma.
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Alterations in mitochondrial distribution, morphology, and function are present in atrophic muscles in aging, muscle disuse, burn injury, intensive care unit-acquired weakness, insulin resistance, chronic obstructive pulmonary disease, cancer cachexia, and different neuromuscular disorders.
“Alterations in mitochondrial distribution, morphology, and function are present in atrophic muscles in aging [148–150], muscle disuse [151, 152], burn injury [153], intensive care unit-acquired weakness [154], insulin resistance [155] chronic obstructive pulmonary disease (COPD) [156], cancer cachexia [157–159], and different neuromuscular disorders [160].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [153]
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How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
Cellular energy utilization and molecular origin of standard metabolic rate in mammals
Rolfe, D. F., & Brown, G. C. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.3.731 · Cited by 2,021 · see citing works
Mitochondrial Membrane Potential Probes and the Proton Gradient: A Practical Usage Guide
Perry, S. W., Norman, J. P., Barbieri, J., Brown, E. B., & Gelbard, H. A. (2011) · BioTechniques · doi:10.2144/000113610 · Cited by 1,196 · see citing works
Oxidative stress in health and disease: The therapeutic potential of Nrf2 activation
Hybertson, B. M., Gao, B., Bose, S. K., & McCord, J. M. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.10.006 · Cited by 1,030 · see citing works
A mitochondrial specific stress response in mammalian cells
Zhao, Q., Wang, J., Levichkin, I. V., Stasinopoulos, S., Ryan, M. T., & Hoogenraad, N. J. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf445 · Cited by 1,026 · see citing works
Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
Hamanaka, R. B., & Chandel, N. S. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.002 · Cited by 1,011 · see citing works
The emerging role of Nrf2 in mitochondrial function
Dinkova-Kostova, A. T., & Abramov, A. Y. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.04.036 · Cited by 983 · see citing works
Reversal of Catabolism by Beta-Blockade after Severe Burns
Herndon, D. N., Hart, D. W., Wolf, S. E., Chinkes, D. L., & Wolfe, R. R. (2001) · New England Journal of Medicine · doi:10.1056/nejmoa010342 · Cited by 638 · see citing works
Self-citationEffect of age on <i>in vivo</i> rates of mitochondrial protein synthesis in human skeletal muscle
Rooyackers, O. E., Adey, D. B., Ades, P. A., & Nair, K. S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15364 · Cited by 564 · see citing works
Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
Bota, D. A., & Davies, K. J. A. (2002) · Nature Cell Biology · doi:10.1038/ncb836 · Cited by 557 · see citing works
Persistence of muscle catabolism after severe burn
Hart, D. W., Wolf, S. E., Mlcak, R. P., Chinkes, D. L., Ramzy, P. I., Obeng, M. K., Ferrando, A. A., Wolfe, R. R., & Herndon, D. N. (2000) · Surgery · doi:10.1067/msy.2000.108059 · Cited by 546 · see citing works
Self-citationCROSSTALK BETWEEN NUCLEAR AND MITOCHONDRIAL GENOMES
Poyton, R. Ο., & McEwen, J. E. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.003023 · Cited by 499 · see citing works
The mitochondrial UPR – protecting organelle protein homeostasis
Haynes, C. M., & Ron, D. (2010) · Journal of Cell Science · doi:10.1242/jcs.075119 · Cited by 490 · see citing works
Prevention of mitochondrial oxidative damage as a therapeutic strategy in diabetes
Green, K., Brand, M. D., & Murphy, M. P. (2004) · Diabetes · doi:10.2337/diabetes.53.2007.s110 · Cited by 490 · see citing works
ClpXP, an ATP-powered unfolding and protein-degradation machine
Baker, T. A., & Sauer, R. T. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.06.007 · Cited by 468 · see citing works
Browning of Subcutaneous White Adipose Tissue in Humans after Severe Adrenergic Stress
Sidossis, L. S., Porter, C. C., Saraf, M. K., Børsheim, E., Radhakrishnan, R. S., Chao, T., Ali, A., Chondronikola, M., Mlcak, R. P., Finnerty, C. C., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.06.022 · Cited by 394 · see citing works
Self-citationSignaling the mitochondrial unfolded protein response
Pellegrino, M. W., Nargund, A. M., & Haynes, C. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.02.019 · Cited by 359 · see citing works
The metabolic stress response to burn trauma: current understanding and therapies
Porter, C. C., Tompkins, R. G., Finnerty, C. C., Sidossis, L. S., Suman-Vejas, O. E., & Herndon, D. N. (2016) · The Lancet · doi:10.1016/s0140-6736(16)31469-6 · Cited by 350 · see citing works
Self-citationDeterminants of Skeletal Muscle Catabolism After Severe Burn
Hart, D. W., Wolf, S. E., Chinkes, D. L., Gore, D. C., Mlcak, R. P., Beauford, R. B., Obeng, M. K., Lal, S., Gold, W. F., Wolfe, R. R., et al. (2000) · Annals of Surgery · doi:10.1097/00000658-200010000-00001 · Cited by 340 · see citing works
Self-citationJovaisaite, V., Mouchiroud, L., & Auwerx, J. (2014) · Journal of Experimental Biology · doi:10.1242/jeb.090738 · Cited by 335 · see citing works
Mitochondrial Aconitase Is a Source of Hydroxyl Radical
Vasquez-Vivar, J. M., Kalyanaraman, B., & Kennedy, M. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14064 · Cited by 317 · see citing works
Li, Y.-P., Chen, Y., Li, A. S., & Reid, M. B. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00129.2003 · Cited by 313 · see citing works
Anabolic Effects of Oxandrolone After Severe Burn
Hart, D. W., Wolf, S. E., Ramzy, P. I., Chinkes, D. L., Beauford, R. B., Ferrando, A. A., Wolfe, R. R., & Herndon, D. N. (2001) · Annals of Surgery · doi:10.1097/00000658-200104000-00012 · Cited by 283 · see citing works
Self-citationProtein Degradation within Mitochondria: Versatile Activities of AAA Proteases and Other Peptidases
Koppen, M., & Langer, T. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701380452 · Cited by 252 · see citing works
Stimulation of Muscle Protein Synthesis by Long-Term Insulin Infusion in Severely Burned Patients
Sakurai, Y., Aarsland, A. A., Herndon, D. N., Chinkes, D. L., Pierre, E. J., Nguyen, T. T., Patterson, B. W., & Wolfe, R. R. (1995) · Annals of Surgery · doi:10.1097/00000658-199509000-00007 · Cited by 238 · see citing works
Self-citationNuclear erythroid factor 2-mediated proteasome activation delays senescence in human fibroblasts
Kapeta, S., Chondrogianni, N., & Gonos, E. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.031575 · Cited by 234 · see citing works
Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress
Bota, D. A., Van Remmen, H., & Davies, K. J. A. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03638-4 · Cited by 233 · see citing works
Nelson, S. K., Bose, S. K., Grunwald, G. K., Myhill, P., & McCord, J. M. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.043 · Cited by 215 · see citing works
Mitochondrial protein-import machinery: correlating structure with function
Baker, M. J., Frazier, A. E., Gulbis, J. M., & Ryan, M. T. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.07.010 · Cited by 213 · see citing works
Kotiadis, V. N., Duchen, M. R., & Osellame, L. D. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.041 · Cited by 212 · see citing works
Maharjan, S., Oku, M., Tsuda, M., Hoseki, J., & Sakai, Y. (2014) · Scientific Reports · doi:10.1038/srep05896 · Cited by 212 · see citing works
Post burn muscle wasting and the effects of treatments
Pereira, C. T., Murphy, K. D., Jeschke, M. G., & Herndon, D. N. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.05.009 · Cited by 202 · see citing works
Self-citationJang, J., Wang, Y., Kim, H.-S., Lalli, M. A., & Kosik, K. S. (2014) · Stem Cells · doi:10.1002/stem.1764 · Cited by 198 · see citing works
Hart, D. W., Wolf, S. E., Chinkes, D. L., Beauford, R. B., Mlcak, R. P., Heggers, J. P., Wolfe, R. R., & Herndon, D. N. (2003) · The Journal of Trauma: Injury, Infection, and Critical Care · doi:10.1097/01.ta.0000060260.61478.a7 · Cited by 192 · see citing works
Self-citationMitochondrial protein quality control during biogenesis and aging
Baker, B. M., & Haynes, C. M. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.01.004 · Cited by 192 · see citing works
Burn Induces Browning of the Subcutaneous White Adipose Tissue in Mice and Humans
Patsouris, D., Qi, P., Abdullahi, A., Stanojcic, M., Chen, P., Parousis, A., Amini‐Nik, S., & Jeschke, M. G. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.10.028 · Cited by 186 · see citing works
Biolo, G., Fleming, R., Maggi, S. P., Nguyen, T. T., Herndon, D. N., & Wolfe, R. R. (2002) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.87.7.8699 · Cited by 162 · see citing works
Self-citationLong-Term Propranolol Use in Severely Burned Pediatric Patients
Herndon, D. N., Rodriguez, N. A., Diaz, E. C., Hegde, S. D., Jennings, K., Mlcak, R. P., Suri, J. S., Lee, J. O., Williams, F. N., Meyer, W. J., et al. (2012) · Annals of Surgery · doi:10.1097/sla.0b013e318265427e · Cited by 154 · see citing works
Self-citationProtein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP
Hoskins, J. R., Singh, S. K., Maurizi, M. R., & Wickner, S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.16.8892 · Cited by 149 · see citing works
Cantu, D., Schaack, J. B., & Patel, M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007095 · Cited by 142 · see citing works
Mitochondrial biogenesis: The Tom and Tim machine
Pfanner, N., & Meijer, M. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00048-0 · Cited by 136 · see citing works
Mitochondrial quality control pathways as determinants of metabolic health
Held, N. M., & Houtkooper, R. H. (2015) · BioEssays · doi:10.1002/bies.201500013 · Cited by 128 · see citing works
Attenuation of Posttraumatic Muscle Catabolism and Osteopenia by Long-Term Growth Hormone Therapy
Hart, D. W., Herndon, D. N., Klein, G. L., Lee, S. B., Celis, M. M., Mohan, S., Chinkes, D. L., & Wolf, S. E. (2001) · Annals of Surgery · doi:10.1097/00000658-200106000-00013 · Cited by 126 · see citing works
Self-citationNrf2 in health and disease: current and future clinical implications
Al‐Sawaf, O., Clarner, T., Fragoulis, A., Kan, Y. W., Pufe, T., Streetz, K. L., & Wruck, C. J. (2015) · Clinical Science · doi:10.1042/cs20150436 · Cited by 125 · see citing works
Efficacy of a high-carbohydrate diet in catabolic illness
Hart, D. W., Wolf, S. E., Zhang, X., Chinkes, D. L., Buffalo, M. C., Matin, S. I., DebRoy, M. A., Wolfe, R. R., & Herndon, D. N. (2001) · Critical Care Medicine · doi:10.1097/00003246-200107000-00004 · Cited by 123 · see citing works
Self-citationInfluence of Metformin on Glucose Intolerance and Muscle Catabolism Following Severe Burn Injury
Gore, D. C., Wolf, S. E., Sanford, A. P., Herndon, D. N., & Wolfe, R. R. (2005) · Annals of Surgery · doi:10.1097/01.sla.0000152013.23032.d1 · Cited by 115 · see citing works
Self-citationWolf, S. E., Thomas, S. J., Dasu, M. R. K., Ferrando, A. A., Chinkes, D. L., Wolfe, R. R., & Herndon, D. N. (2003) · Annals of Surgery · doi:10.1097/01.sla.0000071562.12637.3e · Cited by 115 · see citing works
Self-citationAlternative function for the mitochondrial SAM complex in biogenesis of α-helical TOM proteins
Stojanovski, D., Guiard, B., Kozjak‐Pavlovic, V., Pfanner, N., & Meisinger, C. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200706043 · Cited by 113 · see citing works
Bezawork-Geleta, A., Brodie, E. J., Dougan, D. A., & Truscott, K. N. (2015) · Scientific Reports · doi:10.1038/srep17397 · Cited by 113 · see citing works
ClpXP, an ATP-powered unfolding and protein-degradation machine
Sauer, R. T., & Baker, T. A. (2011) · Cited by 113 · see citing works
Major, T., von Janowsky, B., Ruppert, T., Mogk, A., & Voos, W. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.3.762-776.2006 · Cited by 105 · see citing works
Mitochondrial Proteins Moonlighting in the Nucleus
Monaghan, R. M., & Whitmarsh, A. J. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.10.003 · Cited by 104 · see citing works
Protein degradation in mitochondria
Käser, M., & Langer, T. (2000) · Seminars in Cell and Developmental Biology · doi:10.1006/scdb.2000.0166 · Cited by 100 · see citing works
YME1L degradation reduces mitochondrial proteolytic capacity during oxidative stress
Rainbolt, T. K., Saunders, J. M., & Wiseman, R. L. (2014) · EMBO Reports · doi:10.15252/embr.201438976 · Cited by 91 · see citing works
Proteotoxic stress and ageing triggers the loss of redox homeostasis across cellular compartments
Kirstein, J., Morito, D., Kakihana, T., Sugihara, M., Minnen, A., Hipp, M. S., Nussbaum-Krammer, C. I., Kasturi, P., Hartl, F. U., Nagata, K., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201591711 · Cited by 89 · see citing works
Cooperation of translocase complexes in mitochondrial protein import
Kutik, S., Guiard, B., Meyer, H. E., Wiedemann, N., & Pfanner, N. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200708199 · Cited by 88 · see citing works
β-Blockade and Growth Hormone After Burn
Hart, D. W., Wolf, S. E., Chinkes, D. L., Lal, S. O., Ramzy, P. I., & Herndon, D. N. (2002) · Annals of Surgery · doi:10.1097/00000658-200210000-00007 · Cited by 83 · see citing works
Self-citationHorton, J. W., White, D. J., Maass, D. L., Hybki, D. P., Haudek, S. B., & Giroir, B. P. (2001) · doi:10.1097/00005373-200103000-00002 · Cited by 81 · see citing works
Extremity hyperinsulinemia stimulates muscle protein synthesis in severely injured patients
Gore, D. C., Wolf, S. E., Sanford, A. P., Herndon, D. N., & Wolfe, R. R. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00258.2003 · Cited by 77 · see citing works
Self-citationThe impact of severe burns on skeletal muscle mitochondrial function
Porter, C. C., Herndon, D. N., Sidossis, L. S., & Børsheim, E. (2013) · Burns · doi:10.1016/j.burns.2013.03.018 · Cited by 76 · see citing works
Self-citationThe mitochondrial unfolded protein response in mammalian physiology
Mottis, A., Jovaisaite, V., & Auwerx, J. H. (2014) · Mammalian Genome · doi:10.1007/s00335-014-9525-z · Cited by 68 · see citing works
Diaz, E. C., Herndon, D. N., Porter, C. C., Sidossis, L. S., Suman-Vejas, O. E., & Børsheim, E. (2014) · Burns · doi:10.1016/j.burns.2014.10.010 · Cited by 67 · see citing works
Self-citationUncoupled skeletal muscle mitochondria contribute to hypermetabolism in severely burned adults
Porter, C. C., Herndon, D. N., Børsheim, E., Chao, T., Reidy, P. T., Borack, M. S., Rasmussen, B. B., Chondronikola, M., Saraf, M. K., & Sidossis, L. S. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00206.2014 · Cited by 67 · see citing works
Self-citationChao, T., Herndon, D. N., Porter, C. C., Chondronikola, M., Chaidemenou, A., Abdelrahman, D. R., Bohanon, F. J., Andersen, C. R., & Sidossis, L. S. (2015) · Shock · doi:10.1097/shk.0000000000000454 · Cited by 60 · see citing works
Self-citationPorter, C. C., Herndon, D. N., Børsheim, E., Bhattarai, N., Chao, T., Reidy, P. T., Rasmussen, B. B., Andersen, C. R., Suman-Vejas, O. E., & Sidossis, L. S. (2015) · Journal of Burn Care & Research · doi:10.1097/bcr.0000000000000308 · Cited by 59 · see citing works
Self-citationLoss of Yme1L perturbates mitochondrial dynamics
Ruan, Y., Li, H., Zhang, K., Jian, F., Tang, J., & Song, Z. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.414 · Cited by 56 · see citing works
Ogunbileje, J. O., Porter, C. C., Herndon, D. N., Chao, T., Abdelrahman, D. R., Papadimitriou, A., Chondronikola, M., Zimmers, T. A., Reidy, P. T., Rasmussen, B. B., et al. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00535.2015 · Cited by 55 · see citing works
Self-citationThe Therapeutic Potential of Brown Adipocytes in Humans
Porter, C. C., Chondronikola, M., & Sidossis, L. S. (2015) · Frontiers in Endocrinology · doi:10.3389/fendo.2015.00156 · Cited by 50 · see citing works
Self-citationRole of antioxidants in the treatment of burn lesions.
Al‐Jawad, F. H., Sahib, A. S., & Al-Kaisy, A. A. (2008) · PubMed Central · Cited by 49 · see citing works
Severe Burn Injury Induces Thermogenically Functional Mitochondria in Murine White Adipose Tissue
Porter, C. C., Herndon, D. N., Bhattarai, N., Ogunbileje, J. O., Szczęsny, B., Szabó, C., Toliver-Kinsky, T. E., & Sidossis, L. S. (2015) · Shock · doi:10.1097/shk.0000000000000410 · Cited by 49 · see citing works
Self-citationMitochondrial uncoupling proteins in human physiology and disease.
Hagen, T., & Vidal‐Puig, A. (2002) · PubMed · Cited by 47 · see citing works
Systemic Responses to Injury and the Healing Wound
Wilmore, D. W., & AULICK, L. H. (1980) · Journal of Parenteral and Enteral Nutrition · doi:10.1177/014860718000400215 · Cited by 42 · see citing works
Mlcak, R. P., Suman-Vejas, O. E., Murphy, K. D., & Herndon, D. N. (2004) · Burns · doi:10.1016/j.burns.2004.08.006 · Cited by 32 · see citing works
Self-citationMitochondrial protein turnover: Methods to measure turnover rates on a large scale
Chan, X., Black, C. M., Lin, A. J., Ping, P., & Lau, E. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.10.012 · Cited by 31 · see citing works
Righi, V., Constantinou, C., Mintzopoulos, D., Khan, N. I., Mupparaju, S. P., Rahme, L. G., Swartz, H. M., Szeto, H. H., Tompkins, R. G., & Tzika, A. A. (2013) · The FASEB Journal · doi:10.1096/fj.12-220764 · Cited by 26 · see citing works
Tzika (2009) · International Journal of Molecular Medicine · doi:10.3892/ijmm_00000244 · Cited by 26 · see citing works
Circulating Proteasomes After Burn Injury
Majetschak, M., Zedler, S., Romero, J. A., Albright, J. M., Kraft, R., Kovacs, E. J., Faist, E., & Gamelli, R. L. (2010) · Journal of Burn Care & Research · doi:10.1097/bcr.0b013e3181d0f55d · Cited by 23 · see citing works
Differential acute and chronic effects of burn trauma on murine skeletal muscle bioenergetics
Porter, C. C., Herndon, D. N., Bhattarai, N., Ogunbileje, J. O., Szczęsny, B., Szabó, C., Toliver-Kinsky, T. E., & Sidossis, L. S. (2015) · Burns · doi:10.1016/j.burns.2015.10.026 · Cited by 22 · see citing works
Self-citationEvaluation of the antioxidant peptide SS31 for treatment of burn-induced insulin resistance
Fischman, A. J. (2011) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2011.752 · Cited by 20 · see citing works
Porter, C. C., Cotter, M., Diaz, E. C., Jennings, K., Herndon, D. N., & Børsheim, E. (2013) · The Journal of Trauma: Injury, Infection, and Critical Care · doi:10.1097/ta.0b013e3182921651 · Cited by 20 · see citing works
Self-citationSensing Mitochondrial Homeostasis: the Protein Import Machinery Takes Control
Vögtle, F. ‐., & Meisinger, C. (2012) · Developmental Cell · doi:10.1016/j.devcel.2012.07.018 · Cited by 18 · see citing works
Hoppeler, H., Lüthi, P., Claassen, H., Weibel, E. R., & HOWALD, H. (1973) · PubMed · Cited by 12 · see citing works
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- [54]Ogunbileje JO Porter C Herndon DN Chao T Abdelrahman DR Papadimitriou A Chondronikola M Zimmers TA Reidy PT Rasmussen BB Sidossis LS Hypermetabolism and hypercatabolism of skeletal muscle accompany mitochondrial stress following severe burn trauma American journal of physiology Endocrinology and metabolism 311 E436 448 2016 27382037 PMC5005969
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Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
Mitochondrial dysfunction and mitophagy: crucial players in burn trauma and wound healing
Prabhakaran, H. S., Hu, D., He, W., Luo, G., & Liou, Y. (2023) · Burns & Trauma · doi:10.1093/burnst/tkad029 · Cited by 42 · see citing works
Oxidative pathophysiology following volumetric muscle loss injury in a porcine model
Chao, T., Burmeister, D. M., Corona, B. T., & Greising, S. M. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00026.2019 · Cited by 26 · see citing works
Burn injury insulin resistance and central nervous system complications: A review
Berlanga‐Acosta, J., Mendoza‐Marí, Y., Rodríguez-Rodríguez, N., Herrera, D. G. D. B., Ojalvo, A. G., Fernández‐Mayola, M., Guillén, G. E., & Valdes-Sosa, P. A. (2020) · Burns Open · doi:10.1016/j.burnso.2020.02.001 · Cited by 22 · see citing works
Fatigue Following Burn Injury: A Burn Model System National Database Study
Simko, L. C., Espinoza, L. F., McMullen, K. A., Herndon, D. N., Suman-Vejas, O. E., Fauerbach, J. A., Kowalske, K. J., WIECHMAN, S. A., Kazis, L. E., Ryan, C. M., et al. (2017) · Journal of Burn Care & Research · doi:10.1097/bcr.0000000000000625 · Cited by 20 · see citing works
Self-citationErythropoietin Alleviates Burn-induced Muscle Wasting
Wu, S., Lu, I., Tai, M., Chai, C., Kwan, A., & Huang, S. (2020) · International Journal of Medical Sciences · doi:10.7150/ijms.38590 · Cited by 12 · see citing works
Crandall, C. G., Cramer, M. N., & Kowalske, K. J. (2021) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00620.2021 · Cited by 10 · see citing works
Application of nanomedicine and mesenchymal stem cells in burn injuries for the elderly patients
Xiong, W., Zhang, R., Zhou, H., Liu, Y., Liang, M., Li, K., Duan, X., Chen, D. P., Luo, Y., Xu, J., et al. (2022) · Smart Materials in Medicine · doi:10.1016/j.smaim.2022.08.001 · Cited by 11 · see citing works
Metabolic and Hormonal Changes in Pediatric Burn Patients: Mechanisms, Evidence, and Care Strategies
Pelizzo, G., Calcaterra, V., Marinaro, M., Baldassarre, P., Canonica, C. P. M., & Zuccotti, G. (2025) · European Burn Journal · doi:10.3390/ebj6020017 · Cited by 8 · see citing works
Wallace, R. G., Kenealy, M.-R., Brady, A. J., Twomey, L. C., Duffy, E., Degryse, B., Caballero‐Lima, D., Moyna, N. M., Custaud, M., Meade‐Murphy, G., et al. (2020) · Burns · doi:10.1016/j.burns.2020.04.036 · Cited by 7 · see citing works
Farnesysltransferase Inhibitor Prevents Burn Injury-Induced Metabolome Changes in Muscle
Nakazawa, H., Wong, L. P., Shelton, L. M., Sadreyev, R. I., & Kaneki, M. (2022) · Metabolites · doi:10.3390/metabo12090800 · Cited by 6 · see citing works
Rikihisa, N., Shimanouchi, K., Saito, Y., Sakai, H., & Mitsukawa, N. (2022) · Burns · doi:10.1016/j.burns.2022.03.009 · Cited by 5 · see citing works
Buckwheat trypsin inhibitors: novel nutraceuticals for mitochondrial homeostasis
Li, S. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90256-4.00009-6 · Cited by 4 · see citing works
Kingren, M. S., Barre, M., Barlow, A., Hall, J., Varisco, A., & Porter, C. C. (2025) · Journal of Burn Care & Research · doi:10.1093/jbcr/iraf026 · Cited by 2 · see citing works
Self-citationShielding Burn Patients from Oxidative Stress: The Therapeutic Potential of Antioxidant MembranesPreprint
Haller, H. L., Sander, F., Nischwitz, S. P., Luze, H., Bandke, D., Rapp, M., Rapp, S., Hartmann, B. R., Demircan, M., & Kamolz, L. (2023) · Preprints.org · doi:10.20944/preprints202306.1065.v1 · Cited by 1 · see citing works
An Investigation of Muscle Mechanical Properties in Acute Burns and Burn Types
Ramazanoğlu, E., Usgu, S., Yakut, Y., Çınar, M. A., Bayramlar, K., Güneş, A., & Erkılıç, A. (2025) · Journal of Clinical Medicine · doi:10.3390/jcm14072344 · Cited by 1 · see citing works
Sivayoganathan, T. (2018) · TSpace (University of Toronto) · Cited by 1 · see citing works
HOUSING TEMPERATURE ALTERS BURN-INDUCED HYPERMETABOLISM IN MICE
Kingren, M. S., Hall, J. S., Taylor Joseph Ross, T., Barre, M., Barlow, A., Morales, M. A. L., Treas, L. D., Maxson, R. T., Teo, E. H., & Porter, C. C. (2024) · Shock · doi:10.1097/shk.0000000000002476
Self-citation
- Authors
- Ogunbileje, J. O., Herndon, D. N., Murton, A. J., & Porter, C.
- Affiliations
- Shriners Hospitals for Children - Galveston (US)
- Corresponding author
- Porter, Craig
- Venue
- Journal of Burn Care & Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2017-12-27
- Volume
- 39
- Issue
- 1
- Pages
- 100-108
- ISSN
- 1559-047X (ISSN-L)
- 1559-0488
- PMC
- PMC5650955
- OpenAlex
- W2608634715
- Cited by
- 18
- References
- 82
- Citations by year
- 2025: 3 · 2024: 1 · 2023: 2 · 2022: 4 · 2021: 1 · 2020: 4 · 2019: 1 · 2018: 1 · 2017: 1
- FWCI
- 0.25
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Burn Care & Research (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (P50GM060338, R01GM056687, T32GM008256)
- Topics
- Health Sciences › Medicine › Epidemiology › Burn Injury Management and Outcomes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- mitochondrial stress, skeletal muscle atrophy, mitochondrial superoxide, oxidative stress, muscle protein degradation, resting metabolic rate, mitochondrial signaling, protein degradation
- MeSH terms
- Basal Metabolism, Burns, Humans, Mitochondria, Muscular Atrophy, Superoxides, Oxidative Stress, Muscle, Skeletal
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