{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,11]],"date-time":"2026-07-11T13:20:12Z","timestamp":1783776012570,"version":"3.55.0"},"reference-count":56,"publisher":"Oxford University Press (OUP)","issue":"8","license":[{"start":{"date-parts":[[2019,6,27]],"date-time":"2019-06-27T00:00:00Z","timestamp":1561593600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"name":"Cobb-Vantress, Inc","award":["#2013-01953"],"award-info":[{"award-number":["#2013-01953"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2019,7,30]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Oxidative stress is an unavoidable consequence of aerobic metabolism. Whereas high amounts of mitochondrial reactive oxygen species (ROS) can cause oxidation, low levels play important roles in signal transduction. In a Pedigree male (PedM) broiler model of feed efficiency (FE), the low FE phenotype was characterized by increased ROS in isolated mitochondria (muscle, liver, and duodenum) with a pervasive protein oxidation in mitochondria and tissues. Subsequent proteogenomic studies in muscle revealed evidence of enhanced mitoproteome abundance, enhanced mitochondrial phosphocreatine shuttling expression, and enhanced ribosome assembly in the high FE phenotype. Surprisingly, an enhanced infrastructure would foster greater repair of damaged proteins or organelles through the autophagy and proteosome pathways in the high FE phenotype. Although protein and organelle degradation, recycling, and reconstruction would be energetically expensive, it is possible that energy invested into maintaining optimal function of proteins and organelles contributes to cellular efficiency in the high FE phenotype. New findings in mitochondrial physiology have been reported in the last several years. Reverse electron transport (RET), once considered an artifact of in vitro conditions, now is recognized to play significant roles in inflammation, ischemia\u2013reperfusion, muscle differentiation, and energy utilization. A topology of ROS production indicates that ROS derived from Complex I of the respiratory chain primarily causes oxidation, whereas ROS generated from Complex III are primarily involved in cell signaling. It is also apparent that there is a constant fission and fusion process that mitochondria undergo that help maintain optimal mitochondrial function and enables mitochondria to adjust to periods of nutrient limitation and nutrient excess. Understanding the balancing act that mitochondria play in health and disease will continue to be a vital biological component in health-production efficiency and disease in commercial animal agriculture.<\/jats:p>","DOI":"10.1093\/jas\/skz219","type":"journal-article","created":{"date-parts":[[2019,7,16]],"date-time":"2019-07-16T17:16:15Z","timestamp":1563297375000},"page":"3169-3179","source":"Crossref","is-referenced-by-count":15,"title":["BOARD INVITED REVIEW: Oxidative stress and efficiency: the tightrope act of mitochondria in health and disease1,2"],"prefix":"10.1093","volume":"97","author":[{"given":"Walter G","family":"Bottje","sequence":"first","affiliation":[{"name":"Department of Poultry Science, Center of Excellence for Poultry Science, University of Arkansas, Fayetteville, AR"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2019,6,27]]},"reference":[{"key":"2019073016504614800_CIT0001","doi-asserted-by":"publisher","first-page":"529","DOI":"10.1016\/j.molcel.2008.10.021","article-title":"Respiratory active mitochondrial supercomplexes","volume":"32","author":"Ac\u00edn-P\u00e9rez","year":"2008","journal-title":"Mol. 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