{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,4]],"date-time":"2026-05-04T04:25:08Z","timestamp":1777868708711,"version":"3.51.4"},"reference-count":55,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2026,1,11]],"date-time":"2026-01-11T00:00:00Z","timestamp":1768089600000},"content-version":"vor","delay-in-days":10,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"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 Biochem &amp;amp; Molecular Tox"],"published-print":{"date-parts":[[2026,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>Skeletal muscle is highly susceptible to hypobaric hypoxia linked muscle protein loss due to disturbed proteostasis and redox homeostasis. Carnosine, an endogenous dipeptide possesses antioxidant, anti\u2010inflammatory, anti\u2010glycation and pH buffering properties. The present study investigated the beneficial efficacy of carnosine in amelioration of muscle protein loss during chronic hypobaric hypoxia exposure in rats. Further, probable molecular mechanism for it's protective efficacy was also established via molecular docking study along with support of in\u2010vivo study. Male Sprague\u2010Dawley rats were divided into three groups: Control (unexposed rats), HH (07d hypobaric hypoxia exposed rats), HH\u2009+\u2009CAR (Carnosine supplement rats with 07d hypobaric hypoxia exposure 50\u2009mg\/kg supplemented). Carnosine administration downregulated myostatin expression levels while IGF\u20101 level was upregulated and this was accompanied with an increase in total protein content. The expression levels of FOXO, MAFbx, MuRF1, markers of muscle atrophy were also declined on carnosine supplementation. Further, myogenesis markers, myoG, and mTOR were found increased in carnosine supplemented rats. Along with these activities, carnosine also managed excessive reactive oxygen species (ROS) production, protein oxidation and damage. Ergo, molecular docking study supported the fact that carnosine has the ability to bind with IGFBP and myostatin, a negative regulator of muscle atrophy. Carnosine attenuates muscle protein loss via enhancing myogenesis, managing redox, and protein homeostasis. All these activities together enhances protein concentration and ameliorates hypobaric hypoxia induced muscle protein loss. Therefore, carnosine supplementation can be an effective therapeutic strategy in combating skeletal muscle protein loss linked with high altitude induced hypobaric hypoxia.<\/jats:p>","DOI":"10.1002\/jbt.70690","type":"journal-article","created":{"date-parts":[[2026,1,12]],"date-time":"2026-01-12T06:06:39Z","timestamp":1768197999000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Establishing Molecular Mechanism of Carnosine Against Hypobaric Hypoxia Induced Muscle Protein Loss via In\u2010Silico and In\u2010Vivo Approach"],"prefix":"10.1002","volume":"40","author":[{"given":"Akshita","family":"Kumar","sequence":"first","affiliation":[{"name":"Soldier Performance Department Defence Institute of Physiology and Allied Sciences New Delhi India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Geetha","family":"Suryakumar","sequence":"additional","affiliation":[{"name":"Soldier Performance Department Defence Institute of Physiology and Allied Sciences New Delhi India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0402-9516","authenticated-orcid":false,"given":"Richa","family":"Rathor","sequence":"additional","affiliation":[{"name":"Soldier Performance Department Defence Institute of Physiology and Allied Sciences New Delhi India"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2026,1,11]]},"reference":[{"key":"e_1_2_11_2_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-1-4612-4654-1"},{"key":"e_1_2_11_3_1","doi-asserted-by":"publisher","DOI":"10.14429\/dsj.50.3421"},{"key":"e_1_2_11_4_1","doi-asserted-by":"publisher","DOI":"10.1055\/s-2004-817858"},{"key":"e_1_2_11_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.resp.2007.03.013"},{"key":"e_1_2_11_6_1","doi-asserted-by":"publisher","DOI":"10.1055\/s-0028-1103284"},{"key":"e_1_2_11_7_1","doi-asserted-by":"publisher","DOI":"10.1249\/MSS.0b013e31826d5aa2"},{"issue":"1","key":"e_1_2_11_8_1","first-page":"16","article-title":"Oxidative Stress in Humans During and After 4 Hours of Hypoxia at a Simulated Altitude of 5500 m","volume":"75","author":"Magalh\u00e3es J.","year":"2004","journal-title":"Aviation, Space, and Environmental Medicine"},{"key":"e_1_2_11_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0300-483X(02)00385-2"},{"key":"e_1_2_11_10_1","doi-asserted-by":"publisher","DOI":"10.1007\/s12192-017-0795-8"},{"key":"e_1_2_11_11_1","doi-asserted-by":"publisher","DOI":"10.1186\/rr60"},{"key":"e_1_2_11_12_1","doi-asserted-by":"publisher","DOI":"10.1093\/annonc\/mdt551"},{"key":"e_1_2_11_13_1","doi-asserted-by":"publisher","DOI":"10.1007\/s11010-011-1210-x"},{"key":"e_1_2_11_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.freeradbiomed.2020.09.001"},{"key":"e_1_2_11_15_1","doi-asserted-by":"publisher","DOI":"10.1152\/physrev.00039.2012"},{"key":"e_1_2_11_16_1","doi-asserted-by":"publisher","DOI":"10.1021\/jf103258p"},{"issue":"7","key":"e_1_2_11_17_1","first-page":"757","article-title":"Role of Histidine\u2010Related Compounds as Intracellular Proton Buffering Constituents in Vertebrate Muscle","volume":"65","author":"Abe H.","year":"2000","journal-title":"Biochemistry. 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