{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,10]],"date-time":"2026-07-10T16:03:13Z","timestamp":1783699393407,"version":"3.55.0"},"reference-count":92,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"1","content-domain":{"domain":["www.ahajournals.org"],"crossmark-restriction":true},"short-container-title":["Circulation"],"published-print":{"date-parts":[[2025,7,8]]},"abstract":"<jats:sec>\n                    <jats:title>BACKGROUND:<\/jats:title>\n                    <jats:p>Myocardial ischemia\/reperfusion (I\/R) injury is a substantial challenge to the management of ischemic heart disease, the leading cause of mortality worldwide. Arachidonic acid (AA) is a prominent polyunsaturated fatty acid in the human body and plays an important role in various physiological and pathological conditions. AA metabolic enzymes determine AA levels; however, currently there is no comprehensive analysis of AA enzymes in cardiac I\/R injury.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>METHODS:<\/jats:title>\n                    <jats:p>The profiling of AA metabolic enzymes was analyzed with the RNA sequencing transcriptome data from the mouse heart tissues with I\/R injury. Cultured neonatal and adult rat ventricular myocytes, human embryonic stem cell\u2013derived cardiomyocytes, and in vivo mouse I\/R models were used to confirm the role of L-PGDS (lipocalin-type prostaglandin D2 synthase)\/15d-PGJ2 in I\/R injury. A biotin-tagged 15d-PGJ2 analog combined with liquid chromatography\u2013tandem mass spectrometry was used to identify the downstream signaling of L-PGDS\/15d-PGJ2.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>RESULTS:<\/jats:title>\n                    <jats:p>\n                      Based on the transcriptome data and experimental validations, L-PGDS, together with its downstream metabolite 15d-PGJ2, was downregulated in cardiac tissue with I\/R injury. Functionally, L-PGDS overexpression mitigates myocardial I\/R injury, whereas knockdown exacerbates the damage. Supplementation of 15d-PGJ2 alleviated I\/R injury. Mechanistically, 15d-PGJ2 covalently bound to the CaMKII (Ca\n                      <jats:sup>2+<\/jats:sup>\n                      \/calmodulin dependent protein kinase II) and induced lipoxidation of its cysteine 495 (CaMKII-\u03b49) to dampen the formation of CaMKII oligomers and alleviate its overactivation, consequently ameliorating cardiomyocyte death and cardiac injury.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>CONCLUSIONS:<\/jats:title>\n                    <jats:p>Our study uncovered L-PGDS\/15d-PGJ2\/CaMKII signaling as a new mechanism underlying I\/R-induced cardiomyocyte death. This provides new mechanistic insights and therapeutic targets for myocardial I\/R injury and subsequent heart failure. We also showed that lipoxidation is a new post-translational modification type for CaMKII, deepening our understanding of the regulation of its activity.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1161\/circulationaha.124.070936","type":"journal-article","created":{"date-parts":[[2025,5,21]],"date-time":"2025-05-21T05:00:58Z","timestamp":1747803658000},"page":"41-57","update-policy":"https:\/\/doi.org\/10.1161\/crossmarkpolicy","source":"Crossref","is-referenced-by-count":11,"title":["Intracellular L-PGDS\u2013Derived 15d-PGJ2 Inhibits CaMKII Through Lipoxidation to Alleviate Cardiac Ischemia\/Reperfusion Injury"],"prefix":"10.1161","volume":"152","author":[{"ORCID":"https:\/\/orcid.org\/0009-0005-2034-7487","authenticated-orcid":true,"given":"Qingmei","family":"Hu","sequence":"first","affiliation":[{"name":"State Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology (Q.H., J.L., F.L., L.J., P.X., W. 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