{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T08:20:53Z","timestamp":1789114853857,"version":"build-2803163510"},"reference-count":65,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T00:00:00Z","timestamp":1789084800000},"content-version":"vor","delay-in-days":253,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"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"}],"funder":[{"DOI":"10.13039\/501100004608","name":"Natural Science Foundation of Jiangsu Province","doi-asserted-by":"publisher","award":["BK20231145"],"award-info":[{"award-number":["BK20231145"]}],"id":[{"id":"10.13039\/501100004608","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["82370342"],"award-info":[{"award-number":["82370342"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Cardiovascular Therapeutics"],"published-print":{"date-parts":[[2026,1]]},"abstract":"<jats:p>\n                    Ferritin heavy Chain 1 (FTH1) is a key protective factor against ferroptosis in the heart, yet its protein abundance can diverge from transcript levels in cardiac ferroptosis contexts. Since resistance to ferroptosis depends on FTH1 protein abundance rather than transcript levels and its ferroxidase activity cannot be readily compensated by other ferritin subunits, this mismatch is functionally consequential. This review organizes the evidence into three regulatory layers acting downstream of transcription. Iron regulatory protein\/iron\u2010responsive element (IRP\/IRE) signaling gates ribosome recruitment at the 5\u2009\n                    <jats:sup>\u2032<\/jats:sup>\n                    \u2010untranslated region before translation begins. Epitranscriptomic marks and RNA\u2010binding proteins (RBPs) then route the transcript toward decay or translation, with the N\n                    <jats:sup>6<\/jats:sup>\n                    \u2010methyladenosine (m\n                    <jats:sup>6<\/jats:sup>\n                    A) reader YTHDF2 acting in opposite directions across cardiac contexts. Finally, nuclear receptor Coactivator 4 (NCOA4) delivers assembled ferritin for lysosomal degradation, depleting FTH1 protein independently of transcript level. Together, these mechanisms provide an integrated framework for understanding the mRNA\u2013protein discordance of FTH1 and its contribution to cardiac ferroptosis susceptibility. We also discuss how this framework may inform layer\u2010specific therapeutic strategies and identify the measurements that are missing (labile iron pool, ferritin iron loading, and ferritinophagic flux) before mechanistic insight can translate into clinical cardioprotection.\n                  <\/jats:p>","DOI":"10.1155\/cdr\/8306021","type":"journal-article","created":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T07:24:45Z","timestamp":1789111485000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["FTH1 mRNA\u2013Protein Discordance in Cardiac Ferroptosis: Multilayer Posttranscriptional and Degradative 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