{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,4]],"date-time":"2026-06-04T16:01:57Z","timestamp":1780588917906,"version":"3.54.1"},"reference-count":188,"publisher":"Walter de Gruyter GmbH","issue":"1","license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,1,23]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec id=\"j_med-2025-1342_abs_001\">\n                    <jats:title>Background<\/jats:title>\n                    <jats:p>Sepsis-induced myopathy (SIM)significantly contributes to long-term disability and mortality among sepsis survivors. A comprehensive understanding of both the molecular mechanisms and rehabilitation strategies is crucial for effective management.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec id=\"j_med-2025-1342_abs_002\">\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>A review of pertinent studies was conducted, focusing on the molecular pathogenesis, therapeutic strategies, and rehabilitation interventions for SIM, with particular attention to clinical and translational advancements.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec id=\"j_med-2025-1342_abs_003\">\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>Current management strategies encompass infection control, modulation of inflammation, nutritional support, and structured rehabilitation programs, including early mobilization and physiotherapy. Emerging therapies that target inflammation, cellular protection, and regeneration\u00a0\u2013\u00a0such as stem cell therapy and gene-editing techniques\u00a0\u2013\u00a0demonstrate potential. Furthermore, advancements in personalized medicine, including genomics, transcriptomics, and individualized metabolic interventions, may further improve outcomes.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec id=\"j_med-2025-1342_abs_004\">\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>Optimizing both mechanistic and rehabilitation strategies is essential for enhancing functional recovery and quality of life in patients with SIM. An integrated clinical and molecular approach presents the most promising path forward. Keywords: sepsis-induced myopathy, sepsis.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1515\/med-2025-1342","type":"journal-article","created":{"date-parts":[[2026,3,5]],"date-time":"2026-03-05T17:17:38Z","timestamp":1772731058000},"source":"Crossref","is-referenced-by-count":0,"title":["Beyond muscle weakness: pathogenesis of sepsis-induced myopathy and its management"],"prefix":"10.1515","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8135-131X","authenticated-orcid":false,"given":"Yukun","family":"Liu","sequence":"first","affiliation":[{"name":"Department of Plastic and Aesthetic Surgery , Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology , Wuhan , China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xuan","family":"Zhao","sequence":"additional","affiliation":[{"name":"Division of Trauma Surgery , Emergency Surgery & Surgical Critical, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology , Wuhan , China"},{"name":"Trauma Center, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology , Wuhan , China"},{"name":"Department of Emergency and Critical Care Medicine , Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology , Wuhan , China"},{"name":"Sino-German Research Institute of Disaster Medicine , Wuhan , China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhikai","family":"Xu","sequence":"additional","affiliation":[{"name":"Division of Trauma Surgery , Emergency Surgery & Surgical Critical, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology , Wuhan , China"},{"name":"Trauma Center, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology , Wuhan , China"},{"name":"Department of Emergency and Critical Care Medicine , Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology , Wuhan , China"},{"name":"Sino-German Research Institute of Disaster Medicine , Wuhan , China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-4888-7677","authenticated-orcid":false,"given":"Qinxin","family":"Liu","sequence":"additional","affiliation":[{"name":"Division of Trauma Surgery , Emergency Surgery & Surgical Critical, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology , Wuhan , China"},{"name":"Trauma Center, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology , Wuhan , China"},{"name":"Department of Emergency and Critical Care Medicine , Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology , Wuhan , China"},{"name":"Sino-German Research Institute of Disaster Medicine , Wuhan , China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0947-9823","authenticated-orcid":false,"given":"Yuchang","family":"Wang","sequence":"additional","affiliation":[{"name":"Division of Trauma Surgery , Emergency Surgery & Surgical Critical, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology , Wuhan , China"},{"name":"Trauma Center, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology , Wuhan , China"},{"name":"Department of Emergency and Critical Care Medicine , Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology , Wuhan , China"},{"name":"Sino-German Research Institute of Disaster Medicine , Wuhan , China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"374","published-online":{"date-parts":[[2026,3,6]]},"reference":[{"key":"2026060415215147228_j_med-2025-1342_ref_001","doi-asserted-by":"crossref","unstructured":"Hermans, G, Van den Berghe, G. Clinical review: intensive care unit acquired weakness. Crit Care 2015;19:274. https:\/\/doi.org\/10.1186\/s13054-015-0993-7.","DOI":"10.1186\/s13054-015-0993-7"},{"key":"2026060415215147228_j_med-2025-1342_ref_002","doi-asserted-by":"crossref","unstructured":"Dinglas, VD, Aronson Friedman, L, Colantuoni, E, Mendez-Tellez, PA, Shanholtz, CB, Ciesla, ND, et al.. Muscle weakness and 5-year survival in acute respiratory distress syndrome survivors. Crit Care Med 2017;45:446\u201353. https:\/\/doi.org\/10.1097\/ccm.0000000000002208.","DOI":"10.1097\/CCM.0000000000002208"},{"key":"2026060415215147228_j_med-2025-1342_ref_003","doi-asserted-by":"crossref","unstructured":"Xue, Q, Zhang, D, Zou, J, Wang, H, Shi, R, Dong, L. Treatment advances of sepsis-induced myopathy (Review). 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The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol Cell Biol 2008;28:5747\u201363. https:\/\/doi.org\/10.1128\/mcb.02070-07.","DOI":"10.1128\/MCB.02070-07"},{"key":"2026060415215147228_j_med-2025-1342_ref_066","doi-asserted-by":"crossref","unstructured":"Dumitru, A, Radu, BM, Radu, M, Cretoiu, SM. Muscle changes during atrophy. Adv Exp Med Biol 2018;1088:73\u201392. https:\/\/doi.org\/10.1007\/978-981-13-1435-3_4.","DOI":"10.1007\/978-981-13-1435-3_4"},{"key":"2026060415215147228_j_med-2025-1342_ref_067","doi-asserted-by":"crossref","unstructured":"Raben, N, Hill, V, Shea, L, Takikita, S, Baum, R, Mizushima, N, et al.. Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in pompe disease. Hum Mol Genet 2008;17:3897\u2013908. https:\/\/doi.org\/10.1093\/hmg\/ddn292.","DOI":"10.1093\/hmg\/ddn292"},{"key":"2026060415215147228_j_med-2025-1342_ref_068","doi-asserted-by":"crossref","unstructured":"Green, DR, Galluzzi, L, Kroemer, G. Mitochondria and the autophagy-inflammation-cell death axis in organismal aging. Science 2011;333:1109\u201312. https:\/\/doi.org\/10.1126\/science.1201940.","DOI":"10.1126\/science.1201940"},{"key":"2026060415215147228_j_med-2025-1342_ref_069","doi-asserted-by":"crossref","unstructured":"Sun, N, Youle, RJ, Finkel, T. The mitochondrial basis of aging. Mol Cell 2016;61:654\u201366. https:\/\/doi.org\/10.1016\/j.molcel.2016.01.028.","DOI":"10.1016\/j.molcel.2016.01.028"},{"key":"2026060415215147228_j_med-2025-1342_ref_070","doi-asserted-by":"crossref","unstructured":"Saito, T, Sadoshima, J. Molecular mechanisms of mitochondrial autophagy\/mitophagy in the heart. 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FASEB J 2018;32:1428\u201339. official publication of the Federation of American Societies for Experimental Biology. https:\/\/doi.org\/10.1096\/fj.201700493r.","DOI":"10.1096\/fj.201700493R"},{"key":"2026060415215147228_j_med-2025-1342_ref_078","doi-asserted-by":"crossref","unstructured":"Sebasti\u00e1n, D, Sorianello, E, Segal\u00e9s, J, Irazoki, A, Ruiz-Bonilla, V, Sala, D, et al.. Mfn2 deficiency links age-related sarcopenia and impaired autophagy to activation of an adaptive mitophagy pathway. EMBO J 2016;35:1677\u201393. https:\/\/doi.org\/10.15252\/embj.201593084.","DOI":"10.15252\/embj.201593084"},{"key":"2026060415215147228_j_med-2025-1342_ref_079","doi-asserted-by":"crossref","unstructured":"Goll, DE, Thompson, VF, Li, H, Wei, W, Cong, J. The calpain system. 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Calpain and caspase-3 are required for sepsis-induced diaphragmatic weakness. J\u00a0Appl Physiol 1985)2009;107:1369. https:\/\/doi.org\/10.1152\/japplphysiol.00920.2009.","DOI":"10.1152\/japplphysiol.00920.2009"},{"key":"2026060415215147228_j_med-2025-1342_ref_112","doi-asserted-by":"crossref","unstructured":"Wang, XH, Zhang, L, Mitch, WE, LeDoux, JM, Hu, J, Du, J. Caspase-3 cleaves specific 19\u00a0S proteasome subunits in skeletal muscle stimulating proteasome activity. J\u00a0Biol Chem 2010;285:21249\u201357. https:\/\/doi.org\/10.1074\/jbc.m109.041707.","DOI":"10.1074\/jbc.M109.041707"},{"key":"2026060415215147228_j_med-2025-1342_ref_113","doi-asserted-by":"crossref","unstructured":"Wang, XH, Mitch, WE. Mechanisms of muscle wasting in chronic kidney disease. 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Medicine (Baltim) 2018;97:e9859. https:\/\/doi.org\/10.1097\/md.0000000000009859.","DOI":"10.1097\/MD.0000000000009859"},{"key":"2026060415215147228_j_med-2025-1342_ref_116","doi-asserted-by":"crossref","unstructured":"Liu, Y, Wang, D, Li, T, Yang, F, Li, Z, Bai, X, et al.. The role of NLRP3 inflammasome in inflammation-related skeletal muscle atrophy. Front Immunol 2022;13:1035709. https:\/\/doi.org\/10.3389\/fimmu.2022.1035709.","DOI":"10.3389\/fimmu.2022.1035709"},{"key":"2026060415215147228_j_med-2025-1342_ref_117","doi-asserted-by":"crossref","unstructured":"Liu, Y, Zhang, Y, Liu, Q, Li, T, Wang, W, Li, H, et al.. Inhibition of DDX3X ameliorated CD4(+) T\u00a0cells pyroptosis and improves survival in septic mice. Mol Immunol 2023;154:54\u201360. https:\/\/doi.org\/10.1016\/j.molimm.2022.12.014.","DOI":"10.1016\/j.molimm.2022.12.014"},{"key":"2026060415215147228_j_med-2025-1342_ref_118","doi-asserted-by":"crossref","unstructured":"Yu, P, Zhang, X, Liu, N, Tang, L, Peng, C, Chen, X. Pyroptosis: mechanisms and diseases. Signal Transduct Target Ther 2021;6:128. https:\/\/doi.org\/10.1038\/s41392-021-00507-5.","DOI":"10.1038\/s41392-021-00507-5"},{"key":"2026060415215147228_j_med-2025-1342_ref_119","doi-asserted-by":"crossref","unstructured":"Liu, Y, Zhang, Y, Feng, Q, Liu, Q, Xie, J, Li, H, et al.. GPA peptide attenuates sepsis-induced acute lung injury in mice via inhibiting oxidative stress and pyroptosis of alveolar macrophage. Oxid Med Cell Longev 2021;2021:5589472. https:\/\/doi.org\/10.1155\/2021\/5589472.","DOI":"10.1155\/2021\/5589472"},{"key":"2026060415215147228_j_med-2025-1342_ref_120","doi-asserted-by":"crossref","unstructured":"Wang, YC, Liu, QX, Zheng, Q, Liu, T, Xu, XE, Liu, XH, et al.. Dihydromyricetin alleviates sepsis-induced acute lung injury through inhibiting NLRP3\u00a0inflammasome-dependent pyroptosis in mice model. Inflammation 2019;42:1301\u201310. https:\/\/doi.org\/10.1007\/s10753-019-00990-7.","DOI":"10.1007\/s10753-019-00990-7"},{"key":"2026060415215147228_j_med-2025-1342_ref_121","doi-asserted-by":"crossref","unstructured":"Zhang, Y, Liu, Y, Xie, Z, Liu, Q, Zhuang, Y, Xie, W, et al.. Inhibition of PFKFB3 preserves intestinal barrier function in sepsis by inhibiting NLRP3\/GSDMD. 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Selenomethionine attenuates sepsis-induced skeletal muscle atrophy by inhibiting ROS\/NLRP3 signaling. Shock 2025. https:\/\/doi.org\/10.1097\/shk.0000000000002690.","DOI":"10.1097\/SHK.0000000000002690"},{"key":"2026060415215147228_j_med-2025-1342_ref_125","doi-asserted-by":"crossref","unstructured":"Liu, Y, Liu, Q, Xu, Z, Zhao, X, Yang, F, Li, Z, et al.. P2X7 receptor acts as a novel target for ameliorating sepsis-induced skeletal muscle atrophy in mice model. Shock 2025. https:\/\/doi.org\/10.1097\/shk.0000000000002703.","DOI":"10.1097\/SHK.0000000000002703"},{"key":"2026060415215147228_j_med-2025-1342_ref_126","doi-asserted-by":"crossref","unstructured":"Friedrich, O, Reid, MB, Van den Berghe, G, Vanhorebeek, I, Hermans, G, Rich, MM, et al.. The sick and the weak: neuropathies\/myopathies in the critically ill. Physiol Rev 2015;95:1025\u2013109. https:\/\/doi.org\/10.1152\/physrev.00028.2014.","DOI":"10.1152\/physrev.00028.2014"},{"key":"2026060415215147228_j_med-2025-1342_ref_127","doi-asserted-by":"crossref","unstructured":"Maestraggi, Q, Lebas, B, Clere-Jehl, R, Ludes, PO, Chamaraux-Tran, TN, Schneider, F, et al.. Skeletal muscle and lymphocyte mitochondrial dysfunctions in septic shock trigger ICU-acquired weakness and sepsis-induced immunoparalysis. BioMed Res Int 2017;2017:7897325\u201312. https:\/\/doi.org\/10.1155\/2017\/7897325.","DOI":"10.1155\/2017\/7897325"},{"key":"2026060415215147228_j_med-2025-1342_ref_128","doi-asserted-by":"crossref","unstructured":"Chan, DC. Fusion and fission: interlinked processes critical for mitochondrial health. 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[Decreased Expression of Mitochondrial Calcium Uptake Protein 1 Leads to Skeletal Muscle Dysfunction in Septic Mice]. Sichuan Da Xue Xue Bao Yi Xue Ban 2023;54:552\u20137. https:\/\/doi.org\/10.12182\/20230560102."},{"key":"2026060415215147228_j_med-2025-1342_ref_132","doi-asserted-by":"crossref","unstructured":"Rocheteau, P, Chatre, L, Briand, D, Mebarki, M, Jouvion, G, Bardon, J, et al.. Sepsis induces long-term metabolic and mitochondrial muscle stem cell dysfunction amenable by mesenchymal stem cell therapy. Nat Commun 2015;6:10145. https:\/\/doi.org\/10.1038\/ncomms10145.","DOI":"10.1038\/ncomms10145"},{"key":"2026060415215147228_j_med-2025-1342_ref_133","doi-asserted-by":"crossref","unstructured":"Owen, AM, Patel, SP, Smith, JD, Balasuriya, BK, Mori, SF, Hawk, GS, et al.. Chronic muscle weakness and mitochondrial dysfunction in the absence of sustained atrophy in a preclinical sepsis model. eLife 2019;8:e49920. https:\/\/doi.org\/10.7554\/elife.49920.","DOI":"10.7554\/eLife.49920"},{"key":"2026060415215147228_j_med-2025-1342_ref_134","doi-asserted-by":"crossref","unstructured":"Kingren, MS, Keeble, AR, Galvan-Lara, AM, Ogle, JM, Ungvari, Z, St Clair, DK, et al.. Post-sepsis chronic muscle weakness can be prevented by pharmacological protection of mitochondria. Mol Med 2024;30:221. https:\/\/doi.org\/10.1186\/s10020-024-00982-w.","DOI":"10.1186\/s10020-024-00982-w"},{"key":"2026060415215147228_j_med-2025-1342_ref_135","doi-asserted-by":"crossref","unstructured":"Cao, C, Zhang, Y, Zuo, S, Zhao, W, Wu, Y, Ma, X. Enteral nutrition alleviated lipopolysaccharides-induced hypercatabolism through ghrelin\/GHS-R1alpha-POMC. 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Trials 2020;21:221. https:\/\/doi.org\/10.1186\/s13063-020-4136-3.","DOI":"10.1186\/s13063-020-4136-3"},{"key":"2026060415215147228_j_med-2025-1342_ref_140","doi-asserted-by":"crossref","unstructured":"Borges, RC, Barbeiro, HV, Barbeiro, DF, Soriano, FG. Muscle degradation, vitamin D and systemic inflammation in hospitalized septic patients. J\u00a0Crit Care 2020;56:125\u201331. https:\/\/doi.org\/10.1016\/j.jcrc.2019.12.017.","DOI":"10.1016\/j.jcrc.2019.12.017"},{"key":"2026060415215147228_j_med-2025-1342_ref_141","doi-asserted-by":"crossref","unstructured":"Moon, SJ, Ko, RE, Park, CM, Suh, GY, Hwang, J, Chung, CR. The effectiveness of early enteral nutrition on clinical outcomes in critically ill sepsis patients: a systematic review. 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J\u00a0Appl Physiol 1985)2019;126:1636\u201345. https:\/\/doi.org\/10.1152\/japplphysiol.00917.2018.","DOI":"10.1152\/japplphysiol.00917.2018"},{"key":"2026060415215147228_j_med-2025-1342_ref_146","doi-asserted-by":"crossref","unstructured":"Galimov, A, Merry, TL, Luca, E, Rushing, EJ, Mizbani, A, Turcekova, K, et al.. MicroRNA-29a in adult muscle stem cells controls skeletal muscle regeneration during injury and exercise downstream of fibroblast growth Factor-2. Stem Cell 2016;34:768\u201380. https:\/\/doi.org\/10.1002\/stem.2281.","DOI":"10.1002\/stem.2281"},{"key":"2026060415215147228_j_med-2025-1342_ref_147","doi-asserted-by":"crossref","unstructured":"Marcotte, GR, West, DW, Baar, K. The molecular basis for load-induced skeletal muscle hypertrophy. 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Nutrition 2009;25:125\u20139. https:\/\/doi.org\/10.1016\/j.nut.2008.09.002.","DOI":"10.1016\/j.nut.2008.09.002"},{"key":"2026060415215147228_j_med-2025-1342_ref_161","doi-asserted-by":"crossref","unstructured":"Lee, JH, Kim, SW, Kim, JH, Kim, HJ, Um, J, Jung, DW, et al.. Lithium chloride protects against sepsis-induced skeletal muscle atrophy and cancer cachexia. Cells 2021;10:1017. https:\/\/doi.org\/10.3390\/cells10051017.","DOI":"10.3390\/cells10051017"},{"key":"2026060415215147228_j_med-2025-1342_ref_162","doi-asserted-by":"crossref","unstructured":"Cheng, M, Gao, T, Xi, F, Cao, C, Chen, Y, Zhao, C, et al.. Dexmedetomidine ameliorates muscle wasting and attenuates the alteration of hypothalamic neuropeptides and inflammation in endotoxemic rats. 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Regulation of muscle pyruvate dehydrogenase complex in insulin resistance: effects of exercise and dichloroacetate. Diabetes Metab J 2013;37:301\u201314. https:\/\/doi.org\/10.4093\/dmj.2013.37.5.301.","DOI":"10.4093\/dmj.2013.37.5.301"},{"key":"2026060415215147228_j_med-2025-1342_ref_166","doi-asserted-by":"crossref","unstructured":"Mignemi, NA, McClatchey, PM, Kilchrist, KV, Williams, IM, Millis, BA, Syring, KE, et al.. Rapid changes in the microvascular circulation of skeletal muscle impair insulin delivery during sepsis. Am J Physiol Endocrinol Metab 2019;316:E1012\u20133. https:\/\/doi.org\/10.1152\/ajpendo.00501.2018.","DOI":"10.1152\/ajpendo.00501.2018"},{"key":"2026060415215147228_j_med-2025-1342_ref_167","doi-asserted-by":"crossref","unstructured":"Nystrom, G, Pruznak, A, Huber, D, Frost, RA, Lang, CH. Local insulin-like growth factor I prevents sepsis-induced muscle atrophy. 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