{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T20:50:20Z","timestamp":1760215820398},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1988,2,1]]},"abstract":"<jats:p>The activity and turnover of dihydrolipoamide dehydrogenase (E3), the common component of the three 2-oxoacid dehydrogenase complexes, were measured during the differentiation of 3T3-L1 preadipocytes into 3T3-L1 adipocytes. The specific activity of E3 increased approx. 3-4-fold in 3T3-L1 adipocytes differentiated under a regimen of insulin, dexamethasone and 3-isobutyl-1-methylxanthine for 48 h, followed by insulin alone thereafter. A rabbit antibody to pig heart E3 quantitatively precipitated the enzyme from 3T3-L1 adipocytes. By using immunoprecipitation and gel electrophoresis, a 3.3-fold increase was observed in E3 protein in 3T3-L1 adipocytes as compared with 3T3-L1 preadipocytes, on a DNA basis. Pulse-labelling experiments with L-[35S]methionine revealed a 3.5-fold increase in the rate of synthesis of E3 in 3T3-L1 adipocytes compared with that observed in 3T3-L1 preadipocytes. In contrast, the apparent half-lives of the E3 in 3T3-L1 preadipocytes (43 h) and 3T3-L1 adipocytes (33 h) were not significantly different. Therefore, the 3-4-fold increase in the specific activity of E3 in 3T3-L1 adipocytes resulted from an increased rate of synthesis of the enzyme.<\/jats:p>","DOI":"10.1042\/bj2490897","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:10:03Z","timestamp":1439241003000},"page":"897-902","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Induction of dihydrolipoamide dehydrogenase in 3T3-L1 cells during differentiation"],"prefix":"10.1042","volume":"249","author":[{"given":"D J","family":"Carothers","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G","family":"Pons","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M S","family":"Patel","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/249\/3\/897\/592393\/bj2490897.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/249\/3\/897\/592393\/bj2490897.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T18:01:19Z","timestamp":1637863279000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/249\/3\/897\/23892\/Induction-of-dihydrolipoamide-dehydrogenase-in-3T3"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1988,2,1]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1988,2,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2490897","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1988,2,1]]}}}