{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T22:43:39Z","timestamp":1791585819447,"version":"4.3.4"},"reference-count":39,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2025,4,4]],"date-time":"2025-04-04T00:00:00Z","timestamp":1743724800000},"content-version":"vor","delay-in-days":3,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2025,4,1]],"date-time":"2025-04-01T00:00:00Z","timestamp":1743465600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["J cachexia sarcopenia muscle"],"published-print":{"date-parts":[[2025,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Background<\/jats:title>\n                    <jats:p>Programmed cell death plays a critical role in skeletal muscle atrophy. Ferroptosis, an iron\u2010dependent form of programmed cell death driven by lipid peroxidation, has been implicated in various diseases, but its role in skeletal muscle atrophy remains unclear.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>\n                      Ferroptosis in skeletal muscle atrophy was investigated using two models: dexamethasone (Dex)\u2010induced atrophy (\n                      <jats:italic>n<\/jats:italic>\n                      \u2009=\u20096 independent cell cultures per group) and simulated microgravity (\n                      <jats:italic>n<\/jats:italic>\n                      \u2009=\u20096 mice per group). Conditional Nestin knockout (KO) mice were generated using CRISPR\/Cas9 (\n                      <jats:italic>n<\/jats:italic>\n                      \u2009=\u20096\u20138 mice per group), with wild\u2010type (WT) controls (\n                      <jats:italic>n<\/jats:italic>\n                      \u2009=\u20096\u20138). Phenotypic analyses included histopathology (HE staining), functional assessments (muscle strength, weight analysis, treadmill), and dystrophy evaluation (dystrophin staining). Molecular analyses involved flow cytometry, ELISA, transmission electron microscopy, PI staining, and IP\/MS to delineate Nestin\u2010regulated ferroptosis pathways in skeletal muscle atrophy.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      Ferroptosis was significantly activated in both atrophy models, with a 2.5\u2010fold increase in lipid peroxidation (\n                      <jats:italic>p<\/jats:italic>\n                      \u2009&lt;\u20090.01), a 2\u2010fold accumulation of Fe\n                      <jats:sup>2+<\/jats:sup>\n                      (\n                      <jats:italic>p<\/jats:italic>\n                      \u2009&lt;\u20090.01) and a 50% reduction in Nestin expression (\n                      <jats:italic>p<\/jats:italic>\n                      \u2009&lt;\u20090.001). Nestin KO mice exhibited exacerbated muscle atrophy, showing a 40% decrease in muscle weight (\n                      <jats:italic>p<\/jats:italic>\n                      \u2009&lt;\u20090.01) and a 30% reduction in muscle strength (\n                      <jats:italic>p<\/jats:italic>\n                      \u2009&lt;\u20090.05) compared to WT mice. Nestin overexpression mitigated Dex\u2010induced ferroptosis, reducing lipid peroxidation by 40%, decreasing Fe\n                      <jats:sup>2+<\/jats:sup>\n                      accumulation by 50% (\n                      <jats:italic>p<\/jats:italic>\n                      \u2009&lt;\u20090.01), and improving muscle function by 30% (\n                      <jats:italic>p<\/jats:italic>\n                      \u2009&lt;\u20090.05). Mechanistically, Nestin interacted with MAP 1LC3B (LC3B) to catalyse LC3B polyubiquitination at lysine\u201051, reducing LC3B availability for autophagy and inhibiting autophagy flux by 60% (\n                      <jats:italic>p<\/jats:italic>\n                      \u2009&lt;\u20090.01), leading to a 50% reduction in ferroptosis (\n                      <jats:italic>p<\/jats:italic>\n                      \u2009&lt;\u20090.001).\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>Our study identifies Nestin as a critical regulator of ferroptosis\u2010autophagy crosstalk in skeletal muscle atrophy. Targeting Nestin\u2010LC3B ubiquitination may offer novel therapeutic strategies for preventing muscle wasting in diseases such as cachexia and sarcopenia.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1002\/jcsm.13779","type":"journal-article","created":{"date-parts":[[2025,4,5]],"date-time":"2025-04-05T09:05:58Z","timestamp":1743843958000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["RETRACTED: Nestin Regulates Autophagy\u2010Dependent Ferroptosis Mediated Skeletal Muscle Atrophy by Ubiquitinating MAP 1LC3B"],"prefix":"10.1002","volume":"16","author":[{"given":"Shunshun","family":"Han","sequence":"first","affiliation":[{"name":"College of Animal Science and Technology Key Laboratory of Livestock and Poultry Multi\u2010Omics, Ministry of Agriculture and Rural Affairs Sichuan Agricultural University  Chengdu Sichuan China"},{"name":"Farm Animal Genetic Resources Exploration and Innovation Key Laboratory of Sichuan Province Sichuan Agricultural University  Chengdu Sichuan China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiyu","family":"Zhao","sequence":"additional","affiliation":[{"name":"College of Animal Science and Technology Key Laboratory of Livestock and Poultry Multi\u2010Omics, Ministry of Agriculture and Rural Affairs Sichuan Agricultural University  Chengdu Sichuan China"},{"name":"Farm Animal Genetic Resources Exploration and Innovation Key Laboratory of Sichuan Province Sichuan Agricultural University  Chengdu Sichuan China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chunlin","family":"Yu","sequence":"additional","affiliation":[{"name":"Animal Breeding and Genetics Key Laboratory of Sichuan Province Sichuan Animal Science Academy  Chengdu China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Can","family":"Cui","sequence":"additional","affiliation":[{"name":"College of Animal Science and Technology Key Laboratory 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