{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T02:43:31Z","timestamp":1789008211671,"version":"build-2803163510"},"reference-count":70,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2020,10,31]],"date-time":"2020-10-31T00:00:00Z","timestamp":1604102400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>Taurine is a nonproteinogenic amino sulfonic acid in mammals. Interestingly, skeletal muscle is unable to synthesize taurine endogenously, and the processing of muscular taurine changes throughout ageing and under specific pathophysiological conditions, such as muscular dystrophy. Ageing and disease are also associated with altered iron metabolism, especially when there is an excess of labile iron. The present study addresses the question of whether taurine connects cytoprotective effects and redox homeostasis in a previously unknown iron-dependent manner. Using cultured differentiated C2C12 myotubes, the impact of taurine on markers of lipid peroxidation, redox-sensitive enzymes and iron-related proteins was studied. Significant increases in the heme protein myoglobin and the iron storage protein ferritin were observed in response to taurine treatment. Taurine supplementation reduced lipid peroxidation and BODIPY oxidation by ~60 and 25%, respectively. Furthermore, the mRNA levels of redox-sensitive heme oxygenase (Hmox1), catalase (Cat) and glutamate-cysteine ligase (Gclc) and the total cellular glutathione content were lower in taurine-supplemented cells than they were in the control cells. We suggest that taurine may inhibit the initiation and propagation of lipid peroxidation by lowering basal levels of cellular stress, perhaps through reduction of the cellular labile iron pool.<\/jats:p>","DOI":"10.3390\/antiox9111071","type":"journal-article","created":{"date-parts":[[2020,10,31]],"date-time":"2020-10-31T21:39:56Z","timestamp":1604180396000},"page":"1071","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Taurine Enhances Iron-Related Proteins and Reduces Lipid Peroxidation in Differentiated C2C12 Myotubes"],"prefix":"10.3390","volume":"9","author":[{"given":"Ulrike","family":"Seidel","sequence":"first","affiliation":[{"name":"Institute of Human Nutrition and Food Science, University of Kiel, 24118 Kiel, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kai","family":"L\u00fcersen","sequence":"additional","affiliation":[{"name":"Institute of Human Nutrition and Food Science, University of Kiel, 24118 Kiel, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patricia","family":"Huebbe","sequence":"additional","affiliation":[{"name":"Institute of Human Nutrition and Food Science, University of Kiel, 24118 Kiel, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7888-4684","authenticated-orcid":false,"given":"Gerald","family":"Rimbach","sequence":"additional","affiliation":[{"name":"Institute of Human Nutrition and Food Science, University of Kiel, 24118 Kiel, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,10,31]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1097\/00005792-197001000-00002","article-title":"Ferrokinetics in man","volume":"49","author":"Finch","year":"1970","journal-title":"Medicine"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1038\/nature08301","article-title":"Function and biogenesis of iron-sulphur proteins","volume":"460","author":"Lill","year":"2009","journal-title":"Nature"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"25122","DOI":"10.1074\/jbc.M003797200","article-title":"Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: In vivo role of ferritin ferroxidase activity","volume":"275","author":"Cozzi","year":"2000","journal-title":"J. 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