Intensive Care Unit-Acquired Weakness: Not Just Another Muscle Atrophying Condition
Abstract
:1. Introduction
2. Hallmarks of Muscle Atrophy in the ICU
3. Models of ICUAW
3.1. Porcine Ventilation Models of ICUAW
3.2. Rat Ventilation Models of ICUAW
4. Mechanisms and the Potential for Intervention during and after ICU Stay
4.1. Mechanisms of Muscle Catabolism during ICU Stay
4.1.1. The Ubiquitin Proteasome System in Critical Illness
4.1.2. Dysregulated Autophagy in Critical Illness
4.1.3. Mitochondrial Dysfunction in the ICU
4.1.4. Cytokine Elevation in Critical Illness
4.1.5. Other Mechanisms Contributing to Muscle Loss and Weakness: Calpains, Caspases, and Chaperones
4.1.6. Potential Treatments
4.2. Decrease in Muscle Synthesis during ICU Stay and Strategies to Counteract It
4.2.1. Minimizing Sedation and Implementing Mobilization Strategies in the ICU
4.2.2. Nutritional Strategies
4.2.3. Hormone Stimulation
4.3. Muscle Repair and Regeneration after ICU Discharge
5. Knowledge Gaps and Avenues to New Insights
5.1. Knowledge Gaps
5.2. Circulating Factors as Biomarkers and Drivers of ICUAW
5.3. 3D Human Skeletal Muscle Models
6. Conclusions
Author Contributions
Funding
Conflicts of Interest
Abbreviations
2D | 2- Dimensional |
3D | 3- Dimensional |
AKT | Protein kinase B |
AMPK | 5′ Adenosine monophosphate - activated protein kinase |
ATP | Adenosine triphosphate |
BGP-15 | Poly (adenosine 5′-diphosphate)–ribose] polymerase 1 (PARP-1) Inhibitor |
CIM | Critical illness myopathy |
CIP | Critical illness polyneuropathy |
CK | Creatine kinase |
CMAP | Compound muscle action potential |
COVID-19 | Coronavirus disease 2019 |
CSA | Cross sectional area |
FBOX31, | F-box only protein 31 |
FDA | Food and drug administration |
GCaMP6 | Genetically encoded calcium indicator |
GDF-15 | Growth and differentiation factor 15 |
HSP | Heat shock protein |
ICU | Intensive care unit |
ICUAW | ICU - acquired weakness |
IF4E- binding protein 1 | Eukaryotic translation initiation factor 4E binding protein 1 |
IGF1 | Insulin-like growth factor -1 |
IL-1 | Interleukin-1 |
IL-6 | Interleukin-6 |
LC3 -I/II | Microtubule-associated protein light chain 3 (I/II) |
MAFbx | Muscle-atrophy F box protein |
MAPK | Mitogen-activated protein kinase |
MRC | Medical research council |
mRNA | Messenger RNA |
mTOR | Mammalian target of rapamycin |
mTORC1 | Mammalian target of rapamycin complex 1 |
mTORC2 | Mammalian target of rapamycin complex 2 |
MuRF1 | Muscle ring finger protein 1 |
MuRF2 | Muscle ring finger protein 2 |
MV | Mechanical ventilation |
MyHC | Myosin heavy chain |
NF-kB | Nuclear factor-κB |
NMBA | Neuromuscular blocking agent |
PGC-1 | Peroxisome proliferator-activated receptor gamma coactivator 1-alpha |
PI3K | Phosphoinositide 3-kinase |
RNA | Ribonucleic acid |
RyR | Ryanodine receptors |
SARS-CoV-2 | Severe acute respiratory syndrome coronavirus 2 |
SERCA | Sarco/endoplasmic reticulum Ca2+ -ATPase |
TEAD1 | TEA domain transcription factor 1 |
TFAM | Mitochondrial transcription factor A |
TGFβ | Transforming growth factor β |
TNFα | Tumor necrosis factor α |
TRIM32 | Tripartite motif-containing protein 32 |
UNC-45B | Unc-45 myosin chaperone B |
UPS | Ubiquitin proteasome system |
UTR | Untranslated region |
References
- Stevens, R.D.; Marshall, S.A.; Cornblath, D.R.; Hoke, A.; Needham, D.M.; De Jonghe, B.; Ali, N.A.; Sharshar, T. A framework for diagnosing and classifying intensive care unit-acquired weakness. Crit. Care Med. 2009, 37, S299–S308. [Google Scholar] [CrossRef] [PubMed]
- Fan, E.; Cheek, F.; Chlan, L.; Gosselink, R.; Hart, N.; Herridge, M.S.; Hopkins, R.O.; Hough, C.L.; Kress, J.P.; Latronico, N.; et al. An Official American Thoracic Society Clinical Practice Guideline: The Diagnosis of Intensive Care Unit–acquired Weakness in Adults. Am. J. Respir. Crit. Care Med. 2014, 190, 1437–1446. [Google Scholar] [CrossRef] [PubMed]
- Traon, A.P.-L.; Heer, M.; Narici, M.V.; Rittweger, J.; Vernikos, J. From space to Earth: Advances in human physiology from 20 years of bed rest studies (1986–2006). Graefe’s Arch. Clin. Exp. Ophthalmol. 2007, 101, 143–194. [Google Scholar] [CrossRef]
- Appleton, R.T.; Kinsella, J.; Quasim, T. The incidence of intensive care unit-acquired weakness syndromes: A systematic review. J. Intensive Care Soc. 2014, 16, 126–136. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Ali, N.A.; O’Brien, J.M.; Hoffmann, S.P.; Phillips, G.; Garland, A.; Finley, J.C.W.; Almoosa, K.; Hejal, R.; Wolf, K.M.; Lemeshow, S.; et al. Acquired Weakness, Handgrip Strength, and Mortality in Critically Ill Patients. Am. J. Respir. Crit. Care Med. 2008, 178, 261–268. [Google Scholar] [CrossRef]
- Sharshar, T.; Bastuji-Garin, S.; Stevens, R.D.; Durand, M.-C.; Malissin, I.; Rodriguez, P.; Cerf, C.; Outin, H.; De Jonghe, B. Presence and severity of intensive care unit-acquired paresis at time of awakening are associated with increased intensive care unit and hospital mortality*. Crit. Care Med. 2009, 37, 3047–3053. [Google Scholar] [CrossRef]
- De Jonghe, B.; Bastuji-Garin, S.; Sharshar, T.; Outin, H.; Brochard, L. Does ICU-acquired paresis lengthen weaning from mechanical ventilation? Intensive Care Med. 2004, 30, 1117–1121. [Google Scholar] [CrossRef]
- De Jonghe, B.; Bastuji-Garin, S.; Durand, M.-C.; Malissin, I.; Rodrigues, P.; Cerf, C.; Outin, H.; Sharshar, T. Respiratory weakness is associated with limb weakness and delayed weaning in critical illness*. Crit. Care Med. 2007, 35, 2007–2015. [Google Scholar] [CrossRef]
- Nanas, S.; Kritikos, K.; Angelopoulos, E.; Siafaka, A.; Tsikriki, S.; Poriazi, M.; Kanaloupiti, D.; Kontogeorgi, M.; Pratikaki, M.; Zervakis, D.; et al. Predisposing factors for critical illness polyneuromyopathy in a multidisciplinary intensive care unit. Acta Neurol. Scand. 2008, 118, 175–181. [Google Scholar] [CrossRef]
- De Jonghe, B.; Sharshar, T.; Lefaucheur, J.-P.; Authier, F.-J.; Durand-Zaleski, I.; Boussarsar, M.; Cerf, C.; Renaud, E.; Mesrati, F.; Carlet, J.; et al. Paresis Acquired in the Intensive Care UnitA Prospective Multicenter Study. J. Am. Med. Assoc 2002, 288, 2859–2867. [Google Scholar] [CrossRef] [Green Version]
- Van Aerde, N.; Meersseman, P.; Debaveye, Y.; Wilmer, A.; Gunst, J.; Casaer, M.P.; Bruyninckx, F.; Wouters, P.J.; Gosselink, R.; Berghe, G.V.D.; et al. Five-year impact of ICU-acquired neuromuscular complications: A prospective, observational study. Intensive Care Med. 2020, 46, 1184–1193. [Google Scholar] [CrossRef] [PubMed]
- Koch, S.; Wollersheim, T.; Bierbrauer, J.; Haas, K.; Mörgeli, R.; Deja, M.; Spies, C.D.; Spuler, S.; Krebs, M.; Weber-Carstens, S. Long-term recovery In critical illness myopathy is complete, contrary to polyneuropathy. Muscle Nerve 2014, 50, 431–436. [Google Scholar] [CrossRef]
- Herridge, M.S.; Tansey, C.M.; Matté, A.; Tomlinson, G.; Diaz-Granados, N.; Cooper, A.; Guest, C.B.; Mazer, C.D.; Mehta, S.; Stewart, T.E.; et al. Functional Disability 5 Years after Acute Respiratory Distress Syndrome. N. Engl. J. Med. 2011, 364, 1293–1304. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Yang, T.; Li, Z.; Jiang, L.; Wang, Y.; Xi, X. Risk factors for intensive care unit-acquired weakness: A systematic review and meta-analysis. Acta Neurol. Scand. 2018, 138, 104–114. [Google Scholar] [CrossRef]
- Barreiro, E. Models of disuse muscle atrophy: Therapeutic implications in critically ill patients. Ann. Transl. Med. 2018, 6, 29. [Google Scholar] [CrossRef] [PubMed]
- Batt, J.; Herridge, M.; Dos Santos, C. Mechanism of ICU-acquired weakness: Skeletal muscle loss in critical illness. Intensive Care Med. 2017, 43, 1844–1846. [Google Scholar] [CrossRef] [PubMed]
- Parotto, M.; Batt, J.; Herridge, M. The Pathophysiology of Neuromuscular Dysfunction in Critical Illness. Crit. Care Clin. 2018, 34, 549–556. [Google Scholar] [CrossRef]
- Guarneri, B.; Bertolini, G.; Latronico, N. Long-term outcome in patients with critical illness myopathy or neuropathy: The Italian multicentre CRIMYNE study. J. Neurol. Neurosurg. Psychiatry 2008, 79, 838–841. [Google Scholar] [CrossRef]
- Leijten, F.S.S.; Harinck-de Weerd, J.E.; Poortvliet, D.C.J.; De Weerd, A.W. The role of polyneuropathy in motor convalescence after prolonged mechanical ventilation. J. Am. Med. Assoc. 1995, 274, 1221–1225. [Google Scholar] [CrossRef]
- Zifko, U.A. Long-term outcome of critical illness polyneuropathy. Muscle Nerve 2000, 23, S49–S52. [Google Scholar] [CrossRef]
- Fletcher, S.N.; Kennedy, D.D.; Ghosh, I.R.; Misra, V.P.; Kiff, K.; Coakley, J.H.; Hinds, C.J. Persistent neuromuscular and neurophysiologic abnormalities in long-term survivors of prolonged critical illness*. Crit. Care Med. 2003, 31, 1012–1016. [Google Scholar] [CrossRef] [PubMed]
- Crisafulli, S.; Isgrò, V.; La Corte, L.; Atzeni, F.; Trifirò, G. Potential Role of Anti-interleukin (IL)-6 Drugs in the Treatment of COVID-19: Rationale, Clinical Evidence and Risks. BioDrugs 2020, 34, 415–422. [Google Scholar] [CrossRef]
- Mehta, P.; McAuley, D.F.; Brown, M.; Sanchez, E.; Tattersall, R.S.; Manson, J.J. COVID-19: Consider cytokine storm syndromes and immunosuppression. Lancet 2020, 395, 1033–1034. [Google Scholar] [CrossRef]
- Van Aerde, N.; COVID-19 Consortium; Berghe, G.V.D.; Wilmer, A.; Gosselink, R.; Hermans, G. Intensive care unit acquired muscle weakness in COVID-19 patients. Intensive Care Med. 2020, 1–3. [Google Scholar] [CrossRef]
- Ochala, J.; Larsson, L. Effects of a preferential myosin loss on Ca2+activation of force generation in single human skeletal muscle fibres. Exp. Physiol. 2008, 93, 486–495. [Google Scholar] [CrossRef] [PubMed]
- Larsson, L.; Li, X.; E Berg, H.; Frontera, W.R. Effects of removal of weight-bearing function on contractility and myosin isoform composition in single human skeletal muscle cells. Pflügers Arch. 1996, 432, 320–328. [Google Scholar] [CrossRef] [PubMed]
- Larsson, L.; Li, X.; Edström, L.; Eriksson, L.I.; Zackrisson, H.; Argentini, C.; Schiaffino, S. Acute quadriplegia and loss of muscle myosin in patients treated with nondepolarizing neuromuscular blocking agents and corticosteroids: Mechanisms at the cellular and molecular levels. Crit. Care Med. 2000, 28, 34–45. [Google Scholar] [CrossRef]
- Llano-Diez, M.; Renaud, G.; Andersson, M.; Marrero, H.G.; Cacciani, N.; Engquist, H.; Corpeño, R.; Artemenko, K.; Bergquist, J.; Larsson, L. Mechanisms underlying ICU muscle wasting and effects of passive mechanical loading. Crit. Care 2012, 16, R209. [Google Scholar] [CrossRef] [Green Version]
- Derde, S.; Hermans, G.; Derese, I.; Güiza, F.; Hedström, Y.; Wouters, P.J.; Bruyninckx, F.; D’hoore, A.; Larsson, L.; Berghe, G.V.D.; et al. Muscle atrophy and preferential loss of myosin in prolonged critically ill patients*. Crit. Care Med. 2012, 40, 79–89. [Google Scholar] [CrossRef]
- Borina, E.; Pellegrino, M.A.; D’Antona, G.; Bottinelli, R. Myosin and actin content of human skeletal muscle fibers following 35 days bed rest. Scand. J. Med. Sci. Sports 2010, 20, 65–73. [Google Scholar] [CrossRef]
- Haus, J.M.; Carrithers, J.A.; Carroll, C.C.; Tesch, P.A.; Trappe, T.A. Contractile and connective tissue protein content of human skeletal muscle: Effects of 35 and 90 days of simulated microgravity and exercise countermeasures. Am. J. Physiol. Integr. Comp. Physiol. 2007, 293, R1722–R1727. [Google Scholar] [CrossRef] [Green Version]
- Dos Santos, C.; Hussain, S.N.A.; Mathur, S.; Picard, M.; Herridge, M.; Correa, J.; Bain, A.; Guo, Y.; Advani, A.; Advani, S.L.; et al. Mechanisms of Chronic Muscle Wasting and Dysfunction after an Intensive Care Unit Stay. A Pilot Study. Am. J. Respir. Crit. Care Med. 2016, 194, 821–830. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Bierbrauer, J.; Koch, S.; Olbricht, C.; Hamati, J.; Lodka, D.; Schneider, J.; Luther-Schröder, A.; Kleber, C.; Faust, K.; Wiesener, S.; et al. Early type II fiber atrophy in intensive care unit patients with nonexcitable muscle membrane. Crit. Care Med. 2012, 40, 647–650. [Google Scholar] [CrossRef] [PubMed]
- Wollersheim, T.; Woehlecke, J.; Krebs, M.; Hamati, J.; Lodka, D.; Luther-Schroeder, A.; Langhans, C.; Haas, K.; Radtke, T.; Kleber, C.; et al. Dynamics of myosin degradation in intensive care unit-acquired weakness during severe critical illness. Intensive Care Med. 2014, 40, 528–538. [Google Scholar] [CrossRef] [PubMed]
- Helliwell, T.R.; Wilkinson, G.; Clelland, M.; Palmer, T. Bone Muscle fibre atrophy in critically ill patients is associated with the loss of myosin filaments and the presence of lysosomal enzymes and ubiquitin. Neuropathol. Appl. Neurobiol. 1998, 24, 507–517. [Google Scholar] [CrossRef] [PubMed]
- Riley, D.A.; Ba, J.L.B.; Thompson, J.L.; Fitts, R.H.; Widrick, J.J.; Trappe, S.W.; Trappe, T.A.; Costill, D.L. Disproportionate loss of thin filaments in human soleus muscle after 17-day bed rest. Muscle Nerve 1998, 21, 1280–1289. [Google Scholar] [CrossRef]
- Widrick, J.J.; Romatowski, J.G.; Bain, J.L.W.; Trappe, S.W.; Trappe, T.A.; Thompson, J.L.; Costill, D.L.; Riley, D.A.; Fitts, R.H. Effect of 17 days of bed rest on peak isometric force and unloaded shortening velocity of human soleus fibers. Am. J. Physiol. Content 1997, 273, C1690–C1699. [Google Scholar] [CrossRef]
- Trappe, S.; Trappe, T.; Gallagher, P.; Harber, M.; Alkner, B.; Tesch, P. Human single muscle fibre function with 84 day bed-rest and resistance exercise. J. Physiol. 2004, 557, 501–513. [Google Scholar] [CrossRef]
- Mounier, Y.; Tiffreau, V.; Montel, V.; Bastide, B.; Stevens, L. Phenotypical transitions and Ca2+ activation properties in human muscle fibers: Effects of a 60-day bed rest and countermeasures. J. Appl. Physiol. 2009, 106, 1086–1099. [Google Scholar] [CrossRef] [Green Version]
- Batt, J.; Dos Santos, C.C.; Cameron, J.I.; Herridge, M.S. Intensive care unit-acquired weakness clinical phenotypes and molecular mechanismsIntensive care unit-acquired weakness clinical phenotypes and molecular mechanisms. Am. J. Respir. Crit. Care Med. 2013, 187, 238–246. [Google Scholar] [CrossRef]
- Friedrich, O.; Reid, M.B.; Berghe, G.V.D.; Vanhorebeek, I.; Hermans, G.; Rich, M.M.; Larsson, L. The Sick and the Weak: Neuropathies/Myopathies in the Critically ILL. Physiol. Rev. 2015, 95, 1025–1109. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Romanick, M.; Thompson, L.V.; Brown-Borg, H.M. Murine models of atrophy, cachexia, and sarcopenia in skeletal muscle. Biochim. Biophys. Acta (BBA)-Mol. Basis Dis. 2013, 1832, 1410–1420. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Gao, Y.; Arfat, Y.; Wang, H.; Goswami, N. Muscle Atrophy Induced by Mechanical Unloading: Mechanisms and Potential Countermeasures. Front. Physiol. 2018, 9, 235. [Google Scholar] [CrossRef] [PubMed]
- Bonaldo, P.; Sandri, M. Cellular and molecular mechanisms of muscle atrophy. Dis. Model. Mech. 2012, 6, 25–39. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Jackman, R.W.; Kandarian, S.C. The molecular basis of skeletal muscle atrophy. Am. J. Physiol. Physiol. 2004, 287, C834–C843. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Banduseela, V.C.; Ochala, J.; Chen, Y.-W.; Göransson, H.; Norman, H.; Radell, P.; Eriksson, L.I.; Hoffman, E.P.; Larsson, L. Gene expression and muscle fiber function in a porcine ICU model. Physiol. Genom. 2009, 39, 141–159. [Google Scholar] [CrossRef] [Green Version]
- Ochala, J.; Ahlbeck, K.; Radell, P.J.; Eriksson, L.I.; Larsson, L. Factors Underlying the Early Limb Muscle Weakness in Acute Quadriplegic Myopathy Using an Experimental ICU Porcine Model. PLoS ONE 2011, 6, e20876. [Google Scholar] [CrossRef]
- Norman, H.; Kandala, K.; Kolluri, R.; Zackrisson, H.; Nordquist, J.; Walther, S.; Eriksson, L.I.; Larsson, L. A porcine model of acute quadriplegic myopathy: A feasibility study. Acta Anaesthesiol. Scand. 2006, 50, 1058–1067. [Google Scholar] [CrossRef]
- Aare, S.; Ochala, J.; Norman, H.S.; Radell, P.; Eriksson, L.I.; Göransson, H.; Chen, Y.-W.; Hoffman, E.P.; Larsson, L. Mechanisms underlying the sparing of masticatory versus limb muscle function in an experimental critical illness model. Physiol. Genom. 2011, 43, 1334–1350. [Google Scholar] [CrossRef]
- Aare, S.; Radell, P.; Eriksson, L.I.; Chen, Y.-W.; Hoffman, E.P.; Larsson, L. Role of sepsis in the development of limb muscle weakness in a porcine intensive care unit model. Physiol. Genom. 2012, 44, 865–877. [Google Scholar] [CrossRef] [Green Version]
- A Ackermann, K.; Bostock, H.; Brander, L.; Schröder, R.; Djafarzadeh, S.; Tuchscherer, D.; Jakob, S.M.; Takala, J.; Z’Graggen, W.J. Early changes of muscle membrane properties in porcine faecal peritonitis. Crit. Care 2014, 18, 484. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Matecki, S.; Jung, B.; Saint, N.; Scheuermann, V.; Jaber, S.; Lacampagne, A. Respiratory muscle contractile inactivity induced by mechanical ventilation in piglets leads to leaky ryanodine receptors and diaphragm weakness. J. Muscle Res. Cell Motil. 2017, 38, 17–24. [Google Scholar] [CrossRef] [PubMed]
- Boërio, D.; Corrêa, T.D.; Jakob, S.M.; Ackermann, K.A.; Bostock, H.; Z’Graggen, W.J. Muscle membrane properties in A pig sepsis model: Effect of norepinephrine. Muscle Nerve 2017, 57, 808–813. [Google Scholar] [CrossRef] [PubMed]
- Corpeno, R.; Dworkin, B.; Cacciani, N.; Salah, H.; Bergman, H.-M.; Ravara, B.; Vitadello, M.; Gorza, L.; Gustafson, A.-M.; Hedström, Y.; et al. Time course analysis of mechanical ventilation-induced diaphragm contractile muscle dysfunction in the rat. J. Physiol. 2014, 592, 3859–3880. [Google Scholar] [CrossRef] [PubMed]
- Kalamgi, R.C.; Larsson, L. Mechanical Signaling in the Pathophysiology of Critical Illness Myopathy. Front. Physiol. 2016, 7, 7. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Ochala, J.; Gustafson, A.-M.; Diez, M.L.; Renaud, G.; Li, M.; Aare, S.; Qaisar, R.; Banduseela, V.C.; Hedström, Y.; Tang, X.; et al. Preferential skeletal muscle myosin loss in response to mechanical silencing in a novel rat intensive care unit model: Underlying mechanisms. J. Physiol. 2011, 589, 2007–2026. [Google Scholar] [CrossRef] [PubMed]
- Norman, H.; Nordquist, J.; Andersson, P.; Ansved, T.; Tang, X.; Dworkin, B.; Larsson, L. Impact of post-synaptic block of neuromuscular transmission, muscle unloading and mechanical ventilation on skeletal muscle protein and mRNA expression. Pflugers Arch. 2006, 453, 53–66. [Google Scholar] [CrossRef]
- Renaud, G.; Llano-Diez, M.; Ravara, B.; Gorza, L.; Feng, H.-Z.; Jin, J.-P.; Cacciani, N.; Gustafson, A.-M.; Ochala, J.; Corpeño, R.; et al. Sparing of muscle mass and function by passive loading in an experimental intensive care unit model. J. Physiol. 2012, 591, 1385–1402. [Google Scholar] [CrossRef]
- Perleberg, C.; Kind, A.; Schnieke, A. Genetically engineered pigs as models for human disease. Dis. Model. Mech. 2018, 11, dmm030783. [Google Scholar] [CrossRef] [Green Version]
- Radell, P.J.; Remahl, S.; Nichols, D.G.; Eriksson, L.I. Effects of prolonged mechanical ventilation and inactivity on piglet diaphragm function. Intensive Care Med. 2002, 28, 358–364. [Google Scholar] [CrossRef]
- Schiaffino, S.; Reggiani, C. Molecular diversity of myofibrillar proteins: Gene regulation and functional significance. Physiol. Rev. 1996, 76, 371–423. [Google Scholar] [CrossRef]
- Rich, M.M.; Pinter, M.J.; Kraner, S.D.; Barchi, R.L. Loss of electrical excitability in an animal model of acute quadriplegic myopathy. Ann. Neurol. 1998, 43, 171–179. [Google Scholar] [CrossRef]
- Mozaffar, T.; Haddad, F.; Zeng, M.; Zhang, L.Y.; Adams, G.R.; Baldwin, K.M. Molecular and cellular defects of skeletal muscle in an animal model of acute quadriplegic myopathy. Muscle Nerve 2006, 35, 55–65. [Google Scholar] [CrossRef] [PubMed]
- Larsson, L. Experimental animal models of muscle wasting in intensive care unit patients. Crit. Care Med. 2007, 35, S484–S487. [Google Scholar] [CrossRef]
- Dworkin, B.R.; Dworkin, S.; Tang, X. Carotid and aortic baroreflexes of the rat: I. Open-loop steady-state properties and blood pressure variability. Am. J. Physiol. Integr. Comp. Physiol. 2000, 279, R1910–R1921. [Google Scholar] [CrossRef] [Green Version]
- Kalamgi, R.C.; Salah, H.; Gastaldello, S.; Martinez-Redondo, V.; Ruas, J.L.; Fury, W.; Bai, Y.; Gromada, J.; Sartori, R.; Guttridge, D.C.; et al. Mechano-signalling pathways in an experimental intensive critical illness myopathy model. J. Physiol. 2016, 594, 4371–4388. [Google Scholar] [CrossRef] [PubMed]
- Herridge, M.; Cheung, A.M.; Tansey, C.M.; Matte-Martyn, A.; Diaz-Granados, N.; Al-Saidi, F.; Cooper, A.B.; Guest, C.B.; Mazer, C.D.; Mehta, S.; et al. One-Year Outcomes in Survivors of the Acute Respiratory Distress Syndrome. N. Engl. J. Med. 2003, 348, 683–693. [Google Scholar] [CrossRef] [Green Version]
- Batt, J.; Herridge, M.S.; Dos Santos, C.C. From skeletal muscle weakness to functional outcomes following critical illness: A translational biology perspective. Thorax 2019, 74, 1091–1098. [Google Scholar] [CrossRef] [PubMed]
- McCarthy, J.J.; Esser, K.A. Anabolic and catabolic pathways regulating skeletal muscle mass. Curr. Opin. Clin. Nutr. Metab. Care 2010, 13, 230–235. [Google Scholar] [CrossRef] [Green Version]
- Klaude, M.; Mori, M.; Tjäder, I.; Gustafsson, T.; Wernerman, J.; Rooyackers, O. Protein metabolism and gene expression in skeletal muscle of critically ill patients with sepsis. Clin. Sci. 2011, 122, 133–142. [Google Scholar] [CrossRef] [Green Version]
- Puthucheary, Z.A.; Rawal, J.; McPhail, M.; Connolly, B.; Ratnayake, G.; Chan, P.; Hopkinson, N.S.; Padhke, R.; Dew, T.; Sidhu, P.S.; et al. Acute Skeletal Muscle Wasting in Critical Illness. JAMA 2013, 310, 1591–1600. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Gamrin-Gripenberg, L.; Rehal, M.S.; Olsson, D.; Grip, J.; Wernerman, J.; Rooyackers, O. An attenuated rate of leg muscle protein depletion and leg free amino acid efflux over time is seen in ICU long-stayers. Crit. Care 2018, 22, 13. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Lecker, S.H.; Goldberg, A.L.; Mitch, W.E. Protein Degradation by the Ubiquitin–Proteasome Pathway in Normal and Disease States. J. Am. Soc. Nephrol. 2006, 17, 1807–1819. [Google Scholar] [CrossRef] [PubMed]
- Murton, A.; Constantin, D.; Greenhaff, P. The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy. Biochim. Biophys. Acta (BBA)-Mol. Basis Dis. 2008, 1782, 730–743. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Passmore, L.A.; Barford, D. Getting into position: The catalytic mechanisms of protein ubiquitylation. Biochem. J. 2004, 379, 513–525. [Google Scholar] [CrossRef] [PubMed]
- Bodine, S.C.; Baehr, L.M. Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx/atrogin-1. Am. J. Physiol. Metab. 2014, 307, E469–E484. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Bodine, S.C. Identification of Ubiquitin Ligases Required for Skeletal Muscle Atrophy. Science 2001, 294, 1704–1708. [Google Scholar] [CrossRef] [PubMed]
- Li, Y.-P.; Chen, Y.; John, J.; Moylan, J.; Jin, B.; Mann, D.L.; Reid, M.B. TNF-α acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle. FASEB J. 2005, 19, 362–370. [Google Scholar] [CrossRef] [Green Version]
- Klaude, M.; Hammarqvist, F.; Wemerman, J. An assay of microsomal membrane-associated proteasomes demonstrates increased proteolytic activity in skeletal muscle of intensive care unit patients. Clin. Nutr. 2005, 24, 259–265. [Google Scholar] [CrossRef]
- Klaude, M.; Fredriksson, K.; Tjäder, I.; Hammarqvist, F.; Ahlman, B.; Rooyackers, O.; Wernerman, J. Proteasome proteolytic activity in skeletal muscle is increased in patients with sepsis. Clin. Sci. 2007, 112, 499–506. [Google Scholar] [CrossRef] [Green Version]
- Roth, G.A.; Moser, B.; Krenn, C.; Roth-Walter, F.; Hetz, H.; Richter, S.; Brunner, M.; Jensen-Jarolim, E.; Wolner, E.; Hoetzenecker, K.; et al. Heightened levels of circulating 20S proteasome in critically ill patients. Eur. J. Clin. Investig. 2005, 35, 399–403. [Google Scholar] [CrossRef] [PubMed]
- Constantin, D.; McCullough, J.; Mahajan, R.P.; Greenhaff, P.L. Novel events in the molecular regulation of muscle mass in critically ill patients. J. Physiol. 2011, 589, 3883–3895. [Google Scholar] [CrossRef] [PubMed]
- Tiao, G.; Hobler, S.; Wang, J.J.; A Meyer, T.; A Luchette, F.; E Fischer, J.; O Hasselgren, P. Sepsis is associated with increased mRNAs of the ubiquitin-proteasome proteolytic pathway in human skeletal muscle. J. Clin. Investig. 1997, 99, 163–168. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Llano-Diez, M.; Fury, W.; Okamoto, H.; Bai, Y.; Gromada, J.; Larsson, L. RNA-sequencing reveals altered skeletal muscle contraction, E3 ligases, autophagy, apoptosis, and chaperone expression in patients with critical illness myopathy. Skelet. Muscle 2019, 9, 9. [Google Scholar] [CrossRef]
- Vana, P.G.; Laporte, H.M.; Wong, Y.M.; Kennedy, R.H.; Gamelli, R.L.; Majetschak, M. Proteasome Inhibition After Burn Injury. J. Burn. Care Res. 2015, 37, 207–215. [Google Scholar] [CrossRef] [Green Version]
- Glick, D.; Barth, S.; MacLeod, K.F. Autophagy: Cellular and molecular mechanisms. J. Pathol. 2010, 221, 3–12. [Google Scholar] [CrossRef] [Green Version]
- Khandia, R.; Dadar, M.; Munjal, A.; Dhama, K.; Karthik, K.; Tiwari, R.; Yatoo, M.I.; Iqbal, H.M.; Singh, K.P.; Joshi, S.K.; et al. A Comprehensive Review of Autophagy and Its Various Roles in Infectious, Non-Infectious, and Lifestyle Diseases: Current Knowledge and Prospects for Disease Prevention, Novel Drug Design, and Therapy. Cells 2019, 8, 674. [Google Scholar] [CrossRef] [Green Version]
- Sandri, M. Protein breakdown in muscle wasting: Role of autophagy-lysosome and ubiquitin-proteasome. Int. J. Biochem. Cell Biol. 2013, 45, 2121–2129. [Google Scholar] [CrossRef] [Green Version]
- Sandri, M. Autophagy in health and disease. 3. Involvement of autophagy in muscle atrophy. Am. J. Physiol. Physiol. 2010, 298, C1291–C1297. [Google Scholar] [CrossRef] [Green Version]
- Masiero, E.; Agatea, L.; Mammucari, C.; Blaauw, B.; Loro, E.; Komatsu, M.; Metzger, D.; Reggiani, C.; Schiaffino, S.; Sandri, M. Autophagy Is Required to Maintain Muscle Mass. Cell Metab. 2009, 10, 507–515. [Google Scholar] [CrossRef]
- Masiero, E.; Sandri, M. Autophagy inhibition induces atrophy and myopathy in adult skeletal muscles. Autophagy 2010, 6, 307–309. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Wang, X.; Blagden, C.; Fan, J.; Nowak, S.J.; Taniuchi, I.; Littman, D.R.; Burden, S.J. Runx1 prevents wasting, myofibrillar disorganization, and autophagy of skeletal muscle. Genes Dev. 2005, 19, 1715–1722. [Google Scholar] [CrossRef] [Green Version]
- Vanhorebeek, I.; Gunst, J.; Derde, S.; Derese, I.; Boussemaere, M.; Güiza, F.; Martinet, W.; Timmermans, J.P.; D’hoore, A.; Wouters, P.J.; et al. Insufficient activation of autophagy allows cellular damage to accumulate in critically ill patients. J. Clin. Endocrinol. Metab. 2011, 96, E633–E645. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Thiessen, S.E.; Berghe, G.V.D.; Vanhorebeek, I. Mitochondrial and endoplasmic reticulum dysfunction and related defense mechanisms in critical illness-induced multiple organ failure. Biochim. Biophys. Acta (BBA)-Mol. Basis Dis. 2017, 1863, 2534–2545. [Google Scholar] [CrossRef]
- Picard, M.; Jung, B.; Liang, F.; Azuelos, I.; Hussain, S.; Goldberg, P.; Godin, R.; Danialou, G.; Chaturvedi, R.; Rygiel, K.; et al. Mitochondrial Dysfunction and Lipid Accumulation in the Human Diaphragm during Mechanical Ventilation. Am. J. Respir. Crit. Care Med. 2012, 186, 1140–1149. [Google Scholar] [CrossRef] [Green Version]
- Carré, J.E.; Orban, J.-C.; Re, L.; Felsmann, K.; Iffert, W.; Bauer, M.; Suliman, H.B.; Piantadosi, C.A.; Mayhew, T.M.; Breen, P.; et al. Survival in Critical Illness Is Associated with Early Activation of Mitochondrial Biogenesis. Am. J. Respir. Crit. Care Med. 2010, 182, 745–751. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Fredriksson, K.; Hammarqvist, F.; Strigård, K.; Hultenby, K.; Ljungqvist, O.; Wernerman, J.; Rooyackers, O. Derangements in mitochondrial metabolism in intercostal and leg muscle of critically ill patients with sepsis-induced multiple organ failure. Am. J. Physiol. Metab. 2006, 291, E1044–E1050. [Google Scholar] [CrossRef] [Green Version]
- Puthucheary, Z.A.; Astin, R.; McPhail, M.J.W.; Saeed, S.; Pasha, Y.; Bear, D.E.; Constantin, D.; Velloso, C.; Manning, S.; Calvert, L.; et al. Metabolic phenotype of skeletal muscle in early critical illness. Thorax 2018, 73, 926–935. [Google Scholar] [CrossRef]
- Jiroutkova, K.; Krajčová, A.; Ziak, J.; Fric, M.; Waldauf, P.; Džupa, V.; Gojda, J.; Němcová-Fürstová, V.; Kovář, J.; Elkalaf, M.; et al. Mitochondrial function in skeletal muscle of patients with protracted critical illness and ICU-acquired weakness. Crit. Care 2015, 19, 1–9. [Google Scholar] [CrossRef] [Green Version]
- Tuttle, C.S.; Thang, L.A.; Maier, A.B. Markers of inflammation and their association with muscle strength and mass: A systematic review and meta-analysis. Ageing Res. Rev. 2020, 64, 101185. [Google Scholar] [CrossRef] [PubMed]
- Conti, P.; Ronconi, G.; Caraffa, A.; Gallenga, C.E.; Ross, R.; Frydas, I.; Kritas, S.K. Induction of pro-inflammatory cytokines (IL-1 and IL-6) and lung inflammation by Coronavirus-19 (COVI-19 or SARS-CoV-2): Anti-inflammatory strategies. J. Biol. Regul. Homeost. Agents 2020, 34, 327–331. [Google Scholar] [PubMed]
- Morley, J.E.; Kalantar-Zadeh, K.; Anker, S.D. COVID-19: A major cause of cachexia and sarcopenia? J. Cachexia Sarcopenia Muscle 2020, 11, 863–865. [Google Scholar] [CrossRef] [PubMed]
- Madia, F.; Merico, B.; Primiano, G.; Cutuli, S.L.; De Pascale, G.; Servidei, S. Acute myopathic quadriplegia in patients with COVID-19 in the intensive care unit. Neurology 2020, 95, 492–494. [Google Scholar] [CrossRef]
- Winkelman, C. Inactivity and Inflammation. AACN Adv. Crit. Care 2004, 15, 74–82. [Google Scholar] [CrossRef]
- Li, Y.-P.; Reid, M.B. NF-κB mediates the protein loss induced by TNF-α in differentiated skeletal muscle myotubes. Am. J. Physiol. Integr. Comp. Physiol. 2000, 279, R1165–R1170. [Google Scholar] [CrossRef]
- Li, Y.-P.; Schwartz, R.J.; Waddell, I.D.; Holloway, B.R.; Reid, M.B. Skeletal muscle myocytes undergo protein loss and reactive oxygen-mediated NF-κB activation in response to tumor necrosis factor α. FASEB J. 1998, 12, 871–880. [Google Scholar] [CrossRef]
- Winkelman, C.; Johnson, K.D.; Gordon, N. Associations Between Muscle-Related Cytokines and Selected Patient Outcomes in the ICU. Biol. Res. Nurs. 2014, 17, 125–134. [Google Scholar] [CrossRef] [Green Version]
- Witteveen, E.; Wieske, L.; Verhamme, C.; Van Der Poll, T.; Van Schaik, I.; Schultz, M.; Horn, J. Increased early systemic inflammation in patients with ICU-acquired weakness. Crit. Care 2015, 19, P472. [Google Scholar] [CrossRef] [Green Version]
- Wang, L.; He, W.; Yu, X.; Hu, D.; Bao, M.; Liu, H.; Zhou, J.; Jiang, H. Coronavirus disease 2019 in elderly patients: Characteristics and prognostic factors based on 4-week follow-up. J. Infect. 2020, 80, 639–645. [Google Scholar] [CrossRef] [PubMed]
- Del Valle, D.M.; Kim-Schulze, S.; Huang, H.-H.; Beckmann, N.D.; Nirenberg, S.; Wang, B.; Lavin, Y.; Swartz, T.H.; Madduri, D.; Stock, A.; et al. An inflammatory cytokine signature predicts COVID-19 severity and survival. Nat. Med. 2020, 26, 1636–1643. [Google Scholar] [CrossRef] [PubMed]
- Cooney, R.N.; Maish, G.O.; Gilpin, T.; Shumate, M.L.; Lang, C.H.; Vary, T.C. Mechanism of il-1 induced inhibition of protein synthesis in skeletal muscle. Shock 1999, 11, 235–241. [Google Scholar] [CrossRef] [Green Version]
- Cooney, R.; Owens, E.; Jurasinski, C.; Gray, K.; Vannice, J.; Vary, T. Interleukin-1 receptor antagonist prevents sepsis-induced inhibition of protein synthesis. Am. J. Physiol. Metab. 1994, 267, E636–E641. [Google Scholar] [CrossRef] [PubMed]
- Shakoory, B.; Carcillo, J.A.; Chatham, W.W.; Amdur, R.L.; Zhao, H.; Dinarello, C.A.; Cron, R.Q.; Opal, S.M. Interleukin-1 Receptor Blockade Is Associated With Reduced Mortality in Sepsis Patients With Features of Macrophage Activation Syndrome. Crit. Care Med. 2016, 44, 275–281. [Google Scholar] [CrossRef] [Green Version]
- Friedrich, O.; Yi, B.; Edwards, J.N.; Reischl, B.; Wirth-Hücking, A.; Buttgereit, A.; Lang, R.; Weber, C.; Polyak, F.; Liu, I.; et al. IL-1α Reversibly Inhibits Skeletal Muscle Ryanodine Receptor. A Novel Mechanism for Critical Illness Myopathy? Am. J. Respir. Cell Mol. Biol. 2014, 50, 1096–1106. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Tufan, A.; Güler, A.A.; Matucci-Cerinic, M. COVID-19, immune system response, hyperinflammation and repurposing antirheumatic drugs. Turk. J. Med. Sci. 2020, 50, 620–632. [Google Scholar] [CrossRef] [PubMed]
- Tilg, H.; Dinarello, C.A.; Mier, J.W. IL-6 and APPs: Anti-inflammatory and immunosuppressive mediators. Immunol. Today 1997, 18, 428–432. [Google Scholar] [CrossRef]
- Van Hees, H.W.H.; Schellekens, W.-J.M.; Linkels, M.; Leenders, F.; Zoll, J.; Donders, A.; Dekhuijzen, P.R.; Van Der Hoeven, J.G.; Heunks, L.M.A. Plasma from septic shock patients induces loss of muscle protein. Crit. Care 2011, 15, R233. [Google Scholar] [CrossRef] [Green Version]
- Ruan, Q.; Yang, K.; Wang, W.; Jiang, L.; Song, J. Clinical predictors of mortality due to COVID-19 based on an analysis of data of 150 patients from Wuhan, China. Intensive Care Med. 2020, 46, 846–848. [Google Scholar] [CrossRef] [Green Version]
- Wang, J.; Zhang, H.; Qiao, R.; Ge, Q.; Zhang, S.; Zhao, Z.; Tian, C.; Ma, Q.; Shen, N. Thrombo-inflammatory features predicting mortality in patients with COVID-19: The FAD-85 score. J. Int. Med Res. 2020, 48, 48. [Google Scholar] [CrossRef]
- Chinese Clinical Trial Register (ChiCTR)—The World Health Organization International Clinical Trials Registered Organization Registered Platform. Available online: http://www.chictr.org.cn/showprojen.aspx?proj=49409 (accessed on 17 October 2020).
- Witteveen, E.; Wieske, L.; Van Der Poll, T.; Van Der Schaaf, M.; Van Schaik, I.N.; Schultz, M.J.; Verhamme, C.; Horn, J. Increased Early Systemic Inflammation in ICU-Acquired Weakness; A Prospective Observational Cohort Study*. Crit. Care Med. 2017, 45, 972–979. [Google Scholar] [CrossRef] [Green Version]
- Banduseela, V.C.; Chen, Y.-W.; Kultima, H.G.; Norman, H.S.; Aare, S.; Radell, P.; Eriksson, L.I.; Hoffman, E.P.; Larsson, L. Impaired autophagy, chaperone expression, and protein synthesis in response to critical illness interventions in porcine skeletal muscle. Physiol. Genom. 2013, 45, 477–486. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Larsson, L.; Friedrich, O. Critical Illness Myopathy (CIM) and Ventilator-Induced Diaphragm Muscle Dysfunction (VIDD): Acquired Myopathies Affecting Contractile Proteins. In Comprehensive Physiology; Wiley: Hoboken, NY, USA, 2016; Volume 7, pp. 105–112. [Google Scholar]
- Cacciani, N.; Salah, H.; Li, M.; Akkad, H.; Backeus, A.; Hedstrom, Y.; Jena, B.P.; Bergquist, J.; Larsson, L. Chaperone co-inducer BGP-15 mitigates early contractile dysfunction of the soleus muscle in a rat ICU model. Acta Physiol. 2019, 229, e13425. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Nathan, D.M.; Buse, J.B.; Davidson, M.B.; Ferrannini, E.; Holman, R.R.; Sherwin, R.; Zinman, B. Medical management of hyperglycemia in type 2 diabetes: A consensus algorithm for the initiation and adjustment of therapy. Diabetes Care 2009, 32, 193–203. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- De Santi, M.; Baldelli, G.; Diotallevi, A.; Galluzzi, L.; Schiavano, G.F.; Brandi, G. Metformin prevents cell tumorigenesis through autophagy-related cell death. Sci. Rep. 2019, 9, 1–11. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Cuomo, F.; Altucci, L.; Cobellis, G. Autophagy Function and Dysfunction: Potential Drugs as Anti-Cancer Therapy. Cancers 2019, 11, 1465. [Google Scholar] [CrossRef] [Green Version]
- Zhou, G.; Myers, R.; Li, Y.; Chen, Y.; Shen, X.; Fenyk-Melody, J.; Wu, M.; Ventre, J.; Doebber, T.; Fujii, N.; et al. Role of AMP-activated protein kinase in mechanism of metformin action. J. Clin. Investig. 2001, 108, 1167–1174. [Google Scholar] [CrossRef]
- Kourelis, T.V.; Siegel, R.D. Metformin and cancer: New applications for an old drug. Med. Oncol. 2011, 29, 1314–1327. [Google Scholar] [CrossRef]
- Musi, N.; Hirshman, M.F.; Nygren, J.; Svanfeldt, M.; Bavenholm, P.; Rooyackers, O.; Zhou, G.; Williamson, J.M.; Ljunqvist, O.; Efendic, S.; et al. Metformin Increases AMP-Activated Protein Kinase Activity in Skeletal Muscle of Subjects With Type 2 Diabetes. Diabetes 2002, 51, 2074–2081. [Google Scholar] [CrossRef] [Green Version]
- Yousuf, Y.; Datu, A.; Barnes, B.; Amini-Nik, S.; Jeschke, M.G. Metformin alleviates muscle wasting post-thermal injury by increasing Pax7-positive muscle progenitor cells. Stem Cell Res. Ther. 2020, 11, 18. [Google Scholar] [CrossRef]
- Wang, Y.; An, H.; Liu, T.; Qin, C.; Sesaki, H.; Guo, S.; Radovick, S.; Hussain, M.; Maheshwari, A.; Wondisford, F.E.; et al. Metformin Improves Mitochondrial Respiratory Activity through Activation of AMPK. Cell Rep. 2019, 29, 1511–1523.e5. [Google Scholar] [CrossRef]
- Zhang, L.; Zhang, Z.; Khan, A.; Zheng, H.; Yuan, C.; Jiang, H. Advances in drug therapy for mitochondrial diseases. Ann. Transl. Med. 2020, 8, 17. [Google Scholar] [CrossRef] [PubMed]
- Komen, J.C.; Thorburn, D.R. Turn up the power—pharmacological activation of mitochondrial biogenesis in mouse models. Br. J. Pharmacol. 2014, 171, 1818–1836. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Bastin, J.; Aubey, F.; Rötig, A.; Munnich, A.; Djouadi, F. Activation of Peroxisome Proliferator-Activated Receptor Pathway Stimulates the Mitochondrial Respiratory Chain and Can Correct Deficiencies in Patients’ Cells Lacking Its Components. J. Clin. Endocrinol. Metab. 2008, 93, 1433–1441. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Penna, F.; Bonetto, A.; Aversa, Z.; Minero, V.G.; Fanelli, F.R.; Costelli, P.; Molfino, A. Effect of the specific proteasome inhibitor bortezomib on cancer-related muscle wasting. J. Cachexia Sarcopenia Muscle 2015, 7, 345–354. [Google Scholar] [CrossRef] [PubMed]
- Guglielmi, V.; Nowis, D.; Tinelli, M.; Malatesta, M.; Paoli, L.; Marini, M.; Manganotti, P.; Sadowski, R.; Wilczynski, G.M.; Meneghini, V.; et al. Bortezomib-Induced Muscle Toxicity in Multiple Myeloma. J. Neuropathol. Exp. Neurol. 2017, 76, 620–630. [Google Scholar] [CrossRef] [PubMed]
- Ristimäki, A.; Narko, K.; Hla, T. Down-regulation of cytokine-induced cyclo-oxygenase-2 transcript isoforms by dexamethasone: Evidence for post-transcriptional regulation. Biochem. J. 1996, 318, 325–331. [Google Scholar] [CrossRef] [PubMed]
- Almawi, W.Y.; Melemedjian, O.K. Negative regulation of nuclear factor-κB activation and function by glucocorticoids. J. Mol. Endocrinol. 2002, 28, 69–78. [Google Scholar] [CrossRef] [Green Version]
- Yang, T.; Li, Z.; Jiang, L.; Xi, X. Corticosteroid use and intensive care unit-acquired weakness: A systematic review and meta-analysis. Crit. Care 2018, 22, 187. [Google Scholar] [CrossRef] [Green Version]
- Britt, R.C.; Devine, A.; Swallen, K.C.; Weireter, L.J.; Collins, J.N.; Cole, F.J.; Britt, L.D. Corticosteroid Use in the Intensive Care Unit. Arch. Surg. 2006, 141, 145–149. [Google Scholar] [CrossRef] [Green Version]
- Yang, Z.; Liu, J.; Zhou, Y.; Zhao, X.; Zhao, Q.; Liu, J. The effect of corticosteroid treatment on patients with coronavirus infection: A systematic review and meta-analysis. J. Infect. 2020, 81, e13–e20. [Google Scholar] [CrossRef]
- Yoon, M.-S. mTOR as a Key Regulator in Maintaining Skeletal Muscle Mass. Front. Physiol. 2017, 8, 788. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Sandri, M. Signaling in Muscle Atrophy and Hypertrophy. Physiology 2008, 23, 160–170. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Rennie, M.J. Anabolic resistance in critically ill patients. Crit. Care Med. 2009, 37, S398–S399. [Google Scholar] [CrossRef] [PubMed]
- Morton, R.W.; Traylor, D.A.; Weijs, P.J.; Phillips, S.M. Defining anabolic resistance. Curr. Opin. Crit. Care 2018, 24, 124–130. [Google Scholar] [CrossRef] [PubMed]
- Latronico, N.; Herridge, M.; Hopkins, R.O.; Angus, D.; Hart, N.; Hermans, G.; Iwashyna, T.; Arabi, Y.; Citerio, G.; Ely, E.W.; et al. The ICM research agenda on intensive care unit-acquired weakness. Intensive Care Med. 2017, 43, 1270–1281. [Google Scholar] [CrossRef]
- Parry, S.M.; Puthucheary, Z.A. The impact of extended bed rest on the musculoskeletal system in the critical care environment. Extreme Physiol. Med. 2015, 4, 1–8. [Google Scholar] [CrossRef] [Green Version]
- Girard, T.D.; Kress, J.P.; Fuchs, B.D.; Thomason, J.W.W.; Schweickert, W.D.; Pun, B.T.; Taichman, D.B.; Dunn, J.G.; Pohlman, A.S.; A Kinniry, P.; et al. Efficacy and safety of a paired sedation and ventilator weaning protocol for mechanically ventilated patients in intensive care (Awakening and Breathing Controlled trial): A randomised controlled trial. Lancet 2008, 371, 126–134. [Google Scholar] [CrossRef]
- Kress, J.P.; Pohlman, A.S.; O’Connor, M.F.; Hall, J.B. Daily Interruption of Sedative Infusions in Critically Ill Patients Undergoing Mechanical Ventilation. N. Engl. J. Med. 2000, 342, 1471–1477. [Google Scholar] [CrossRef] [Green Version]
- Cuthill, J.A.; Jarvie, L.; McGovern, C.; Shaw, M. The effects of sedation cessation within the first four hours of intensive care unit admission in mechanically ventilated critically ill patients—a quality improvement study. EClinicalMedicine 2020, 26, 100486. [Google Scholar] [CrossRef]
- Lönnqvist, P.-A.; Bell, M.; Karlsson, T.; Wiklund, L.; Höglund, A.-S.; Larsson, L. Does prolonged propofol sedation of mechanically ventilated COVID-19 patients contribute to critical illness myopathy? Br. J. Anaesth. 2020, 125, e334–e336. [Google Scholar] [CrossRef]
- Denehy, L.; Lanphere, J.; Needham, D.M. Ten reasons why ICU patients should be mobilized early. Intensive Care Med. 2016, 43, 86–90. [Google Scholar] [CrossRef] [PubMed]
- Jin, P.; Liu, C.; Hou, Q.; Li, L.; Tang, C.; Chen, Z. Scandium carbides/cyanides in the boron cage: Computational prediction of X@B80(X = Sc2C2, Sc3C2, Sc3CN and Sc3C2CN). Phys. Chem. Chem. Phys. 2016, 18, 21398–21411. [Google Scholar] [CrossRef] [PubMed]
- Fuke, R.; Hifumi, T.; Kondo, Y.; Hatakeyama, J.; Takei, T.; Yamakawa, K.; Inoue, S.; Nishida, O. Early rehabilitation to prevent postintensive care syndrome in patients with critical illness: A systematic review and meta-analysis. BMJ Open 2018, 8, e019998. [Google Scholar] [CrossRef] [Green Version]
- Tipping, C.J.; Harrold, M.; Holland, A.; Romero, L.; Nisbet, T.; Hodgson, C.L. The effects of active mobilisation and rehabilitation in ICU on mortality and function: A systematic review. Intensive Care Med. 2016, 43, 171–183. [Google Scholar] [CrossRef] [PubMed]
- Zhang, L.; Hu, W.; Cai, Z.; Liu, J.; Wu, J.; Deng, Y.; Yu, K.; Chen, X.; Zhu, L.; Ma, J.; et al. Early mobilization of critically ill patients in the intensive care unit: A systematic review and meta-analysis. PLoS ONE 2019, 14, e0223185. [Google Scholar] [CrossRef] [Green Version]
- Bear, D.E.; Parry, S.M.; Puthucheary, Z.A. Can the critically ill patient generate sufficient energy to facilitate exercise in the ICU? Curr. Opin. Clin. Nutr. Metab. Care 2018, 21, 110–115. [Google Scholar] [CrossRef]
- Lee, C.M.; Fan, E. ICU-acquired weakness: What is preventing its rehabilitation in critically ill patients? BMC Med. 2012, 10, 115. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Zanotti, E.; Felicetti, G.; Maini, M.; Fracchia, C. Peripheral Muscle Strength Training in Bed-Bound Patients with COPD Receiving Mechanical Ventilation: Effect of Electrical Stimulation. Cardiopulm. Phys. Ther. J. 2003, 14, 29. [Google Scholar] [CrossRef]
- Burtin, C.; Clerckx, B.; Robbeets, C.; Ferdinande, P.; Langer, D.; Troosters, T.; Hermans, G.; Decramer, M.; Gosselink, R. Early exercise in critically ill patients enhances short-term functional recovery*. Crit. Care Med. 2009, 37, 2499–2505. [Google Scholar] [CrossRef]
- Woo, K.; Kim, J.; Kim, H.B.; Choi, H.; Kim, K.; Lee, D.; Na, S. The effect of electrical muscle stimulation and in-bed cycling on muscle strength and mass of mechanically ventilated patients: A pilot study. Acute Crit. Care 2018, 33, 16–22. [Google Scholar] [CrossRef]
- Reid, J.C.; Unger, J.; McCaskell, D.; Childerhose, L.; Zorko, D.J.; Kho, M.E. Physical rehabilitation interventions in the intensive care unit: A scoping review of 117 studies. J. Intensive Care 2018, 6, 1–12. [Google Scholar] [CrossRef] [Green Version]
- Villet, S.; Chiolero, R.L.; Bollmann, M.D.; Revelly, J.-P.; Rn, M.-C.C.; Delarue, J.; Berger, M.M. Negative impact of hypocaloric feeding and energy balance on clinical outcome in ICU patients. Clin. Nutr. 2005, 24, 502–509. [Google Scholar] [CrossRef] [PubMed]
- McClave, S.A.; Martindale, R.G.; Vanek, V.W.; McCarthy, M.; Roberts, P.; Taylor, B.; Ochoa, J.B.; Napolitano, L.; Cresci, G.; Directors, T.A.B.O.; et al. Guidelines for the Provision and Assessment of Nutrition Support Therapy in the Adult Critically Ill Patient. J. Parenter. Enter. Nutr. 2009, 33, 277–316. [Google Scholar] [CrossRef]
- Volkert, D.; Berner, Y.; Berry, E.; Cederholm, T.; Bertrand, P.C.; Milne, A.; Palmblad, J.; Schneider, S.; Sobotka, L.; Stanga, Z.; et al. ESPEN Guidelines on Enteral Nutrition: Geriatrics. Clin. Nutr. 2006, 25, 330–360. [Google Scholar] [CrossRef] [PubMed]
- Ferrie, S.; Allman-Farinelli, M.; Daley, M.; Smith, K. Protein Requirements in the Critically Ill. J. Parenter. Enter. Nutr. 2015, 40, 795–805. [Google Scholar] [CrossRef]
- Casaer, M.P.; Mesotten, D.; Hermans, G.; Wouters, P.J.; Schetz, M.; Meyfroidt, G.; Van Cromphaut, S.; Ingels, C.; Meersseman, P.; Muller, J.; et al. Early versus Late Parenteral Nutrition in Critically Ill Adults. N. Engl. J. Med. 2011, 365, 506–517. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hermans, G.; Casaer, M.P.; Clerckx, B.; Güiza, F.; Vanhullebusch, T.; Derde, S.; Meersseman, P.; Derese, I.; Mesotten, D.; Wouters, P.; et al. Effect of tolerating macronutrient deficit on the development of intensive-care unit acquired weakness: A subanalysis of the EPaNIC trial. Lancet Respir. Med. 2013, 1, 621–629. [Google Scholar] [CrossRef]
- Oldani, M.; Sandini, M.; Nespoli, L.; Coppola, S.; Bernasconi, D.P.; Gianotti, L. Glutamine Supplementation in Intensive Care Patients. Medicine 2015, 94, e1319. [Google Scholar] [CrossRef]
- Heyland, D.; Muscedere, J.; Wischmeyer, P.; Cook, D.; Jones, G.; Albert, M.; Elke, G.; Berger, M.M.; Day, A.G. A Randomized Trial of Glutamine and Antioxidants in Critically Ill Patients. N. Engl. J. Med. 2013, 368, 1489–1497. [Google Scholar] [CrossRef] [Green Version]
- Fink, J.; Schoenfeld, B.J.; Nakazato, K. The role of hormones in muscle hypertrophy. Physician Sportsmed. 2017, 46, 129–134. [Google Scholar] [CrossRef]
- Herman, B.; Wilmer, A.; Meersseman, W.; Milants, I.; Wouters, P.J.; Bobbaers, H.; Bruyninckx, F.; Berghe, G.V.D. Impact of Intensive Insulin Therapy on Neuromuscular Complications and Ventilator Dependency in the Medical Intensive Care Unit. Am. J. Respir. Crit. Care Med. 2007, 175, 480–489. [Google Scholar] [CrossRef]
- Berghe, G.V.D.; Wilmer, A.; Hermans, G.; Meersseman, W.; Wouters, P.J.; Milants, I.; Van Wijngaerden, E.; Bobbaers, H.; Bouillon, R. Intensive Insulin Therapy in the Medical ICU. N. Engl. J. Med. 2006, 354, 449–461. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Berghe, G.V.D.; Wouters, P.; Weekers, F.; Verwaest, C.; Bruyninckx, F.; Schetz, M.; Vlasselaers, D.; Ferdinande, P.; Lauwers, P.; Bouillon, R. Intensive Insulin Therapy in Critically Ill Patients. N. Engl. J. Med. 2001, 345, 1359–1367. [Google Scholar] [CrossRef] [PubMed]
- Finfer, S. Intensive versus conventional glucose control in critically ill patients with traumatic brain injury: Long-term follow-up of a subgroup of patients from the NICE-SUGAR study. Intensive Care Med. 2015, 41, 1037–1047. [Google Scholar] [CrossRef]
- Weber-Carstens, S.; Schneider, J.; Wollersheim, T.; Assmann, A.; Bierbrauer, J.; Marg, A.; Al-Hasani, H.; Chadt, A.; Wenzel, K.; Koch, S.; et al. Critical Illness Myopathy and GLUT4. Am. J. Respir. Crit. Care Med. 2013, 187, 387–396. [Google Scholar] [CrossRef] [PubMed]
- Berghe, G.V.D.; Schoonheydt, K.; Becx, P.; Bruyninckx, F.; Wouters, P.J. Insulin therapy protects the central and peripheral nervous system of intensive care patients. Neurology 2005, 64, 1348–1353. [Google Scholar] [CrossRef] [PubMed]
- Elijah, I.E.; Branski, L.K.; Finnerty, C.C.; Herndon, D.N. The GH/IGF-1 system in critical illness. Best Pr. Res. Clin. Endocrinol. Metab. 2011, 25, 759–767. [Google Scholar] [CrossRef] [Green Version]
- Takala, J.; Ruokonen, E.; Webster, N.R.; Nielsen, M.S.; Zandstra, D.F.; Vundelinckx, G.; Hinds, C.J. Increased Mortality Associated with Growth Hormone Treatment in Critically Ill Adults. N. Engl. J. Med. 1999, 341, 785–792. [Google Scholar] [CrossRef]
- Nierman, D.M.; Mechanick, J.I. Hypotestosteronemia in chronically critically ill men. Crit. Care Med. 1999, 27, 2418–2421. [Google Scholar] [CrossRef]
- Bech, A.; Van Leeuwen, H.; De Boer, H. Etiology of low testosterone levels in male patients with severe sepsis requiring mechanical ventilation. Crit. Care 2013, 17, P448. [Google Scholar] [CrossRef] [Green Version]
- Almoosa, K.F.; Gupta, A.; Pedroza, C.; Watts, N.B. Low Testosterone Levels are Frequent in Patients with Acute Respiratory Failure and are Associated with Poor Outcomes. Endocr. Pr. 2014, 20, 1057–1063. [Google Scholar] [CrossRef] [PubMed]
- Basualto-Alarcón, C.; Jorquera, G.; Altamirano, F.; Jaimovich, E.; Estrada, M. Testosterone Signals through mTOR and Androgen Receptor to Induce Muscle Hypertrophy. Med. Sci. Sports Exerc. 2013, 45, 1712–1720. [Google Scholar] [CrossRef] [PubMed]
- Wang, J.; Wu, T. Testosterone improves muscle function of the extensor digitorum longus in rats with sepsis. Biosci. Rep. 2020, 40, 40. [Google Scholar] [CrossRef] [PubMed]
- Owen, A.M.; Patel, S.P.; Smith, J.D.; Balasuriya, B.K.; Mori, S.F.; Hawk, G.S.; Stromberg, A.J.; Kuriyama, N.; Kaneki, M.; Rabchevsky, A.G.; et al. Chronic muscle weakness and mitochondrial dysfunction in the absence of sustained atrophy in a preclinical sepsis model. eLife 2019, 8, 1–25. [Google Scholar] [CrossRef] [PubMed]
- Rocheteau, P.; Chatre, L.; Briand, D.; Mebarki, M.; Jouvion, G.; Bardon, J.; Crochemore, C.; Serrani, P.; Lecci, P.P.; Latil, M.; et al. Sepsis induces long-term metabolic and mitochondrial muscle stem cell dysfunction amenable by mesenchymal stem cell therapy. Nat. Commun. 2015, 6, 10145. [Google Scholar] [CrossRef] [Green Version]
- Hughes, L.; Paton, B.; Rosenblatt, B.; Gissane, C.; Patterson, S.D. Blood flow restriction training in clinical musculoskeletal rehabilitation: A systematic review and meta-analysis. Br. J. Sports Med. 2017, 51, 1003–1011. [Google Scholar] [CrossRef]
- Centner, C.; Wiegel, P.; Gollhofer, A.; König, D. Effects of Blood Flow Restriction Training on Muscular Strength and Hypertrophy in Older Individuals: A Systematic Review and Meta-Analysis. Sports Med. 2018, 49, 95–108. [Google Scholar] [CrossRef] [Green Version]
- Slysz, J.; Stultz, J.; Burr, J. The efficacy of blood flow restricted exercise: A systematic review & meta-analysis. J. Sci. Med. Sport 2016, 19, 669–675. [Google Scholar] [CrossRef] [Green Version]
- Walsh, C.J.; Batt, J.; Herridge, M.; Mathur, S.; Bader, G.D.; Hu, P.; Dos Santos, C. Transcriptomic analysis reveals abnormal muscle repair and remodeling in survivors of critical illness with sustained weakness. Sci. Rep. 2016, 6, 29334. [Google Scholar] [CrossRef] [Green Version]
- Qiu, H.; Wang, F.; Liu, C.; Xu, X.; Liu, B. TEAD1-dependent expression of the FoxO3a gene in mouse skeletal muscle. BMC Mol. Biol. 2011, 12, 1. [Google Scholar] [CrossRef] [Green Version]
- Wang, F.; Wang, H.; Wu, H.; Qiu, H.; Zeng, C.; Sun, L.; Liu, B. TEAD1 controls C2C12 cell proliferation and differentiation and regulates three novel target genes. Cell. Signal. 2013, 25, 674–681. [Google Scholar] [CrossRef]
- Fan, E.; Dowdy, D.W.; Colantuoni, E.; Mendez-Tellez, P.A.; Sevransky, J.E.; Shanholtz, C.; Himmelfarb, C.R.D.; Desai, S.V.; Ciesla, N.; Herridge, M.S.; et al. Physical Complications in Acute Lung Injury Survivors. Crit. Care Med. 2014, 42, 849–859. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Schiaffino, S.; Dyar, K.A.; Ciciliot, S.; Blaauw, B.; Sandri, M. Mechanisms regulating skeletal muscle growth and atrophy. FEBS J. 2013, 280, 4294–4314. [Google Scholar] [CrossRef] [PubMed]
- Powers, S.K.; Lynch, G.S.; Murphy, K.T.; Reid, M.B.; Zijdewind, I. Disease-Induced Skeletal Muscle Atrophy and Fatigue. Med. Sci. Sports Exerc. 2016, 48, 2307–2319. [Google Scholar] [CrossRef]
- Psychogios, N.; Hau, D.D.; Peng, J.; Guo, A.C.; Mandal, R.; Bouatra, S.; Sinelnikov, I.; Krishnamurthy, R.; Eisner, R.; Gautam, B.; et al. The Human Serum Metabolome. PLoS ONE 2011, 6, e16957. [Google Scholar] [CrossRef] [Green Version]
- Burch, P.M.; Pogoryelova, O.; Goldstein, R.; Bennett, D.; Guglieri, M.; Straub, V.; Bushby, K.; Lochmüller, H.; Morris, C. Muscle-Derived Proteins as Serum Biomarkers for Monitoring Disease Progression in Three Forms of Muscular Dystrophy. J. Neuromuscul. Dis. 2015, 2, 241–255. [Google Scholar] [CrossRef] [Green Version]
- Baird, M.F.; Graham, S.M.; Baker, J.S.; Bickerstaff, G.F. Creatine-Kinase- and Exercise-Related Muscle Damage Implications for Muscle Performance and Recovery. J. Nutr. Metab. 2012, 2012, 1–13. [Google Scholar] [CrossRef] [Green Version]
- Kim, E.Y.; Lee, J.W.; Suh, M.R.; Choi, W.A.; Kang, S.-W.; Oh, H.J. Correlation of Serum Creatine Kinase Level With Pulmonary Function in Duchenne Muscular Dystrophy. Ann. Rehabil. Med. 2017, 41, 306–312. [Google Scholar] [CrossRef] [Green Version]
- Emmerson, P.J.; Duffin, K.L.; Chintharlapalli, S.; Wu, X. GDF15 and Growth Control. Front. Physiol. 2018, 9, 1712. [Google Scholar] [CrossRef] [Green Version]
- Bloch, S.; Lee, J.Y.; Wort, S.J.; Polkey, M.I.; Kemp, P.R.; Griffiths, M.J. Sustained Elevation of Circulating Growth and Differentiation Factor-15 and a Dynamic Imbalance in Mediators of Muscle Homeostasis Are Associated With the Development of Acute Muscle Wasting Following Cardiac Surgery*. Crit. Care Med. 2013, 41, 982–989. [Google Scholar] [CrossRef]
- Bloch, S.A.A.; Lee, J.Y.; Syburra, T.; Rosendahl, U.; Griffiths, M.J.D.; Kemp, P.R.; Polkey, M.I. Increased expression of GDF-15 may mediate ICU-acquired weakness by down-regulating muscle microRNAs. Thorax 2014, 70, 219–228. [Google Scholar] [CrossRef] [Green Version]
- Buendgens, L.; Yagmur, E.; Bruensing, J.; Herbers, U.; Baeck, C.; Trautwein, C.; Koch, A.; Tacke, F. Growth Differentiation Factor-15 Is a Predictor of Mortality in Critically Ill Patients with Sepsis. Dis. Markers 2017, 2017, 1–10. [Google Scholar] [CrossRef] [Green Version]
- Xie, Y.; Liu, S.; Zheng, H.; Cao, L.; Liu, K.; Li, X. Utility of Plasma GDF-15 for Diagnosis and Prognosis Assessment of ICU-Acquired Weakness in Mechanically Ventilated Patients: Prospective Observational Study. BioMed Res. Int. 2020, 2020, 3630568. [Google Scholar] [CrossRef]
- Ito, T.; Nakanishi, Y.; Yamaji, N.; Murakami, S.; Schaffer, S.W. Induction of Growth Differentiation Factor 15 in Skeletal Muscle of Old Taurine Transporter Knockout Mouse. Biol. Pharm. Bull. 2018, 41, 435–439. [Google Scholar] [CrossRef] [Green Version]
- Ortega, M.A.; Fernández-Garibay, X.; Castaño, A.G.; De Chiara, F.; Hernández-Albors, A.; Balaguer-Trias, J.; Ramón-Azcón, J. Muscle-on-a-chip with an on-site multiplexed biosensing system for in situ monitoring of secreted IL-6 and TNF-α. Lab Chip 2019, 19, 2568–2580. [Google Scholar] [CrossRef]
- Von Maltzahn, J.; Renaud, J.-M.; Parise, G.; Rudnicki, M.A. Wnt7a treatment ameliorates muscular dystrophy. Proc. Natl. Acad. Sci. USA 2012, 109, 20614–20619. [Google Scholar] [CrossRef] [Green Version]
- A DiMasi, J.; Hansen, R.W.; Grabowski, H.G. The price of innovation: New estimates of drug development costs. J. Heal. Econ. 2003, 22, 151–185. [Google Scholar] [CrossRef] [Green Version]
- McGreevy, J.W.; Hakim, C.H.; McIntosh, M.A.; Duan, D. Animal models of Duchenne muscular dystrophy: From basic mechanisms to gene therapy. Dis. Model. Mech. 2015, 8, 195–213. [Google Scholar] [CrossRef] [Green Version]
- Young, J.; Margaron, Y.; Fernandes, M.; Duchemin-Pelletier, E.; Michaud, J.; Flaender, M.; Lorintiu, O.; Degot, S.; Poydenot, P. MyoScreen, a High-Throughput Phenotypic Screening Platform Enabling Muscle Drug Discovery. SLAS Discov. Adv. Life Sci. R&D 2018, 23, 790–806. [Google Scholar] [CrossRef]
- Pampaloni, F.; Reynaud, E.G.; Stelzer, E.H.K. The third dimension bridges the gap between cell culture and live tissue. Nat. Rev. Mol. Cell Biol. 2007, 8, 839–845. [Google Scholar] [CrossRef]
- Duval, K.; Grover, H.; Han, L.-H.; Mou, Y.; Pegoraro, A.F.; Fredberg, J.; Chen, Z. Modeling Physiological Events in 2D vs. 3D Cell Culture. Physiology 2017, 32, 266–277. [Google Scholar] [CrossRef]
- Collinsworth, A.M.; Torgan, C.E.; Nagda, S.N.; Rajalingam, R.J.; Kraus, W.E.; Truskey, G.A. Orientation and length of mammalian skeletal myocytes in response to a unidirectional stretch. Cell Tissue Res. 2000, 302, 243–251. [Google Scholar] [CrossRef]
- Sengupta, D.; Gilbert, P.M.; Johnson, K.J.; Blau, H.M.; Heilshorn, S.C. Protein-Engineered Biomaterials to Generate Human Skeletal Muscle Mimics. Adv. Heal. Mater. 2012, 1, 785–789. [Google Scholar] [CrossRef] [Green Version]
- Wang, P.-Y.; Yu, H.-T.; Tsai, W.-B. Modulation of alignment and differentiation of skeletal myoblasts by submicron ridges/grooves surface structure. Biotechnol. Bioeng. 2010, 106, 285–294. [Google Scholar] [CrossRef]
- Clark, P.; Coles, D.; Peckham, M. Preferential adhesion to and survival on patterned laminin organizes myogenesis in vitro. Exp. Cell Res. 1997, 230, 275–283. [Google Scholar] [CrossRef]
- Bian, W.; Juhas, M.; Pfeiler, T.W.; Bursac, N. Local Tissue Geometry Determines Contractile Force Generation of Engineered Muscle Networks. Tissue Eng. Part A 2012, 18, 957–967. [Google Scholar] [CrossRef] [Green Version]
- Bakooshli, M.A.; Lippmann, E.S.; Mulcahy, B.; Tung, K.; Pegoraro, E.; Ahn, H.; Ginsberg, H.; Zhen, M.; Ashton, R.S.; Gilbert, P.M. A 3D model of human skeletal muscle innervated with stem cell-derived motor neurons enables epsilon-subunit targeted myasthenic syndrome studies. bioRxiv 2018, 275545. [Google Scholar] [CrossRef] [Green Version]
- VanDenburgh, H.; Shansky, J.; Be, F.B.; Ba, V.B.; Reid, J.; Thorrez, L.; Valentini, R.; Crawford, G. Drug-screening platform based on the contractility of tissue-engineered muscle. Muscle Nerve 2008, 37, 438–447. [Google Scholar] [CrossRef] [Green Version]
- Legant, W.R.; Pathak, A.; Yang, M.T.; Deshpande, V.S.; Mcmeeking, R.M.; Chen, C.S. Microfabricated tissue gauges to measure and manipulate forces from 3D microtissues. Proc. Natl. Acad. Sci. USA 2009, 106, 10097–10102. [Google Scholar] [CrossRef] [Green Version]
- Afshar, M.E.; Abraha, H.Y.; Bakooshli, M.A.; Davoudi, S.; Thavandiran, N.; Tung, K.; Ahn, H.; Ginsberg, H.J.; Zandstra, P.W.; Gilbert, P.M. A 96-well culture platform enables longitudinal analyses of engineered human skeletal muscle microtissue strength. Sci. Rep. 2020, 10, 1–16. [Google Scholar] [CrossRef] [Green Version]
- Eschenhagen, T.; Zimmermann, W.H. Engineering Myocardial Tissue. Circ. Res. 2005, 97, 1220–1231. [Google Scholar] [CrossRef] [Green Version]
- Madden, L.; Juhas, M.; E Kraus, W.; Truskey, G.A.; Bursac, N. Bioengineered human myobundles mimic clinical responses of skeletal muscle to drugs. eLife 2015, 4, 3–5. [Google Scholar] [CrossRef] [Green Version]
- Shima, A.; Morimoto, Y.; Sweeney, H.L.; Takeuchi, S. Three-dimensional contractile muscle tissue consisting of human skeletal myocyte cell line. Exp. Cell Res. 2018, 370, 168–173. [Google Scholar] [CrossRef]
- Chen, T.-W.; Wardill, T.J.; Sun, Y.; Pulver, S.R.; Renninger, S.L.; Baohan, A.; Schreiter, E.R.; Kerr, R.A.; Orger, M.B.; Jayaraman, V.; et al. Ultrasensitive fluorescent proteins for imaging neuronal activity. Nat. Cell Biol. 2013, 499, 295–300. [Google Scholar] [CrossRef] [Green Version]
- Bakooshli, M.A.; Lippmann, E.S.; Mulcahy, B.; Iyer, N.; Nguyen, C.T.; Tung, K.; Stewart, B.A.; van den Dorpel, H.; Fuehrmann, T.; Shoichet, M.; et al. A 3D culture model of innervated human skeletal muscle enables studies of the adult neuromuscular junction. eLife 2019, 8. [Google Scholar] [CrossRef]
ICU Model | Strain | Sex | Age | ICUAW Interventions and Triggers | Duration of Mechanical Ventilation | ICUAW Hallmarks Replicated | Affected Muscle Groups |
---|---|---|---|---|---|---|---|
Porcine | Sus scrofa [46] | F [46,47,48,49,50] | Piglets | Neuromuscular blocking agent [47,48,49] | 27 h [51] | Reduced force generation [47,50,52] | Diaphragm [52] |
Mechanical ventilation [47,48,49,50,51,52,53] | 48 h [53] | Decreased muscle membrane excitability [47,48,51,53] | Limb [47,48,49,50,51,52,53] | ||||
Corticosteroids [47,48,49] | 72 h [52] | Masseter [48,49] | |||||
Sepsis [47,48,49,50,51,52,53] | 5 days [46,47,49,50] | ||||||
All * [47,48] | |||||||
Rat | Sprague- Dawley [54,55,56,57,58] | F [54,56,58] | - | Neuromuscular blocking agent [54,55,56,57,58] | 0–≥14 days [54,55,56,57,58] | Muscle Atrophy [54,55,56,57,58] | Diaphragm [54,57] |
Mechanical ventilation [54,55,56,57,58] | Preferential loss of myosin [54,56,57,58] | Limb [55,56,57,58] | |||||
Reduced force generation [54,56,58] | Masseter [57] |
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Lad, H.; Saumur, T.M.; Herridge, M.S.; dos Santos, C.C.; Mathur, S.; Batt, J.; Gilbert, P.M. Intensive Care Unit-Acquired Weakness: Not Just Another Muscle Atrophying Condition. Int. J. Mol. Sci. 2020, 21, 7840. https://doi.org/10.3390/ijms21217840
Lad H, Saumur TM, Herridge MS, dos Santos CC, Mathur S, Batt J, Gilbert PM. Intensive Care Unit-Acquired Weakness: Not Just Another Muscle Atrophying Condition. International Journal of Molecular Sciences. 2020; 21(21):7840. https://doi.org/10.3390/ijms21217840
Chicago/Turabian StyleLad, Heta, Tyler M. Saumur, Margaret S. Herridge, Claudia C. dos Santos, Sunita Mathur, Jane Batt, and Penney M. Gilbert. 2020. "Intensive Care Unit-Acquired Weakness: Not Just Another Muscle Atrophying Condition" International Journal of Molecular Sciences 21, no. 21: 7840. https://doi.org/10.3390/ijms21217840