{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,4]],"date-time":"2026-05-04T04:27:13Z","timestamp":1777868833482,"version":"3.51.4"},"reference-count":0,"publisher":"S. Karger AG","license":[{"start":{"date-parts":[[2017,8,11]],"date-time":"2017-08-11T00:00:00Z","timestamp":1502409600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/karger.com\/pages\/terms-and-conditions"},{"start":{"date-parts":[[2017,8,11]],"date-time":"2017-08-11T00:00:00Z","timestamp":1502409600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/karger.com\/pages\/terms-and-conditions"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Enzyme"],"abstract":"<jats:p>Changes in transcription\/accumulation of ferritin mRNA accompany cell differentiation\nand development as cells establish the pattern of iron storage and metabolism that\nmatches their specialized features. Signals which induce changes in ferritin gene expression\ninclude hormones (thyrotropin in thyroid cells), monokines (tumor necrosis factor a in myoblasts,\nand preadipocytes), phagocytosis and\/or inducing agents (erythrophagocytosis in\nmacrophages, phorbol esters in promyelocytes, and dimethyslulfoxide in proerythroblasts),\nheat shock (in red cells) and light (in leaf mesophyll). Iron, which has a major effect on the\ntranslation of ferritin mRNA, also leads to synthesis and\/or accumulation of ferritin mRNA\nin hepatocytes, adult red cells, HeLa cells, and undifferentiated plant cells. Iron-induced\nchanges in ferritin mRNA composition allow cells to synthesize large amounts of different\nferritins in response to excess iron. Whether iron will act both on translation and transcription\nmay relate to the uses of stored iron by the cell (iron reserve for other cells? detoxification?)\nand the magnitude of the iron signal relative to the existing pool of ferritin mRNA.\nTranslational regulation of ferritin mRNA depends on two distinctive features of the RNA:\n(1) conserved regulatory sequence of 28 nucleotides occurs in the 5' noncoding region (iron\n\u2018regulatory\u2019 or \u2018responsive\u2019 element, IRE) which interacts with cytoplasmic regulator proteins,\npresent in animal cells, that block initiation; sequences in the 3' untranslated region\ncan modulate translation when the IRE is present. (2) Ferritin mRNA, either deregulated by\niron induction in cells or isolated from cells (polyA^+), forms initiation complexes efficiently\ncompared to other cellular mRNAs. The structure of the IRE, which is also found in the 3'\nuntranslated region of the iron-destabilized transferrin receptor mRNA, has begun to be analyzed by computer prediction, site-directed mutagenesis, and solution behavior. The\nresults to date show that the IRE is a hairpin with bulges and loops that is stacked upon a\nbase-paired flanking region (FL) with varying sequence. Interactions of the IRE+FL with\nother parts of ferritin mRNA are indicated by comparing the reactivity of natural ferritin\nmRNA with an oligomer (n = 55). The structure of the stem nearest the hairpin loop is\nsequence-dependent and flexible. Variations in the distance of the IRE from the cap in\nvarious ferritin mRNAs, compensated by the length of FL, and the structural properties of\nthe IRE+FL suggest that the 5' regulatory structure of ferritin mRNA includes the\nIRE+FL.<\/jats:p>","DOI":"10.1159\/000468748","type":"journal-article","created":{"date-parts":[[2017,8,11]],"date-time":"2017-08-11T17:21:10Z","timestamp":1502472070000},"page":"68-82","source":"Crossref","is-referenced-by-count":18,"title":["Ferritin mRNA Translation, Structure, and Gene Transcription\nduring Development of Animals and Plants"],"prefix":"10.1159","author":[{"given":"Elizabeth C.","family":"Theil","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"127","published-online":{"date-parts":[[2017,8,11]]},"container-title":["Enzyme"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/karger.com\/article-pdf\/doi\/10.1159\/000468748","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T12:45:25Z","timestamp":1777553125000},"score":1,"resource":{"primary":{"URL":"https:\/\/karger.com\/article\/doi\/10.1159\/000468748"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,8,11]]},"references-count":0,"URL":"https:\/\/doi.org\/10.1159\/000468748","archive":["Portico"],"relation":{},"ISSN":["0013-9432","2504-2564"],"issn-type":[{"value":"0013-9432","type":"print"},{"value":"2504-2564","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,8,11]]}}}