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Cachexia is characterized by loss of body weight and muscle atrophy. Increased skeletal muscle mitochondrial reactive oxygen species (ROS) is a contributing factor to loss of muscle mass in cachectic patients. Mice inoculated with Lewis lung carcinoma (LLC) cells lose weight, muscle mass, and have lower muscle sirtuin\u20101 (sirt1) expression. Nicotinic acid (NA) is a precursor to nicotinamide dinucleotide (NAD+) which is exhausted in cachectic muscle and is a direct activator of sirt1. Mice lost body and muscle weight and exhibited reduced skeletal muscle sirt1 expression after inoculation with LLC cells. C2C12 myotubes treated with LLC\u2010conditioned media (LCM) had lower myotube diameter. We treated C2C12 myotubes with LCM for 24\u2009h with or without NA for 24\u2009h. C2C12 myotubes treated with NA maintained myotube diameter, sirt1 expression, and had lower mitochondrial superoxide. We then used a sirt1\u2010specific small molecule activator SRT1720 to increase sirt1 activity. C2C12 myotubes treated with SRT1720 maintained myotube diameter, prevented loss of sirt1 expression, and attenuated mitochondrial superoxide production. Our data provides evidence that NA may be beneficial in combating cancer cachexia by maintaining sirt1 expression and decreasing mitochondrial superoxide production.<\/jats:p>","DOI":"10.14814\/phy2.16103","type":"journal-article","created":{"date-parts":[[2024,7,1]],"date-time":"2024-07-01T08:59:06Z","timestamp":1719824346000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Preventing loss of sirt1 lowers mitochondrial oxidative stress and preserves <scp>C2C12<\/scp> myotube diameter in an in\u00a0vitro model of cancer cachexia"],"prefix":"10.14814","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4007-8403","authenticated-orcid":false,"given":"Brian A.","family":"Hain","sequence":"first","affiliation":[{"name":"Department of Cellular and Molecular Physiology Penn State College of Medicine  Hershey Pennsylvania USA"},{"name":"Penn State Cancer Institute Penn State College of Medicine  Hershey Pennsylvania USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2149-7189","authenticated-orcid":false,"given":"Scot R.","family":"Kimball","sequence":"additional","affiliation":[{"name":"Department of Cellular and Molecular Physiology Penn State College of Medicine  Hershey Pennsylvania USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3858-7623","authenticated-orcid":false,"given":"David L.","family":"Waning","sequence":"additional","affiliation":[{"name":"Department of Cellular and Molecular Physiology Penn State College of Medicine  Hershey Pennsylvania USA"},{"name":"Penn State Cancer Institute Penn State College of Medicine  Hershey Pennsylvania USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2024,7]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M109.022749"},{"key":"e_1_2_10_3_1","doi-asserted-by":"publisher","DOI":"10.1155\/2016\/9579868"},{"key":"e_1_2_10_4_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0140403"},{"key":"e_1_2_10_5_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrdp.2017.105"},{"key":"e_1_2_10_6_1","doi-asserted-by":"publisher","DOI":"10.3390\/cells10113150"},{"key":"e_1_2_10_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-37595-6"},{"key":"e_1_2_10_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.freeradbiomed.2007.10.006"},{"key":"e_1_2_10_9_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.C200171200"},{"key":"e_1_2_10_10_1","doi-asserted-by":"publisher","DOI":"10.1002\/jcsm.12615"},{"key":"e_1_2_10_11_1","doi-asserted-by":"publisher","DOI":"10.1002\/jcsm.12232"},{"key":"e_1_2_10_12_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1094637"},{"key":"e_1_2_10_13_1","doi-asserted-by":"publisher","DOI":"10.1038\/nature07813"},{"key":"e_1_2_10_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.lfs.2011.04.018"},{"key":"e_1_2_10_15_1","doi-asserted-by":"publisher","DOI":"10.1186\/s12967-023-04369-z"},{"key":"e_1_2_10_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.pharmthera.2018.03.004"},{"key":"e_1_2_10_17_1","doi-asserted-by":"publisher","DOI":"10.1084\/jem.20190745"},{"key":"e_1_2_10_18_1","doi-asserted-by":"publisher","DOI":"10.4103\/0973-029X.86670"},{"key":"e_1_2_10_19_1","first-page":"1734","article-title":"Knockdown of NADPH oxidase 4 reduces mitochondrial oxidative stress and neuronal pyroptosis following intracerebral hemorrhage","volume":"18","author":"Ding B. 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