{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T23:17:46Z","timestamp":1787008666173,"version":"build-2736575974"},"reference-count":32,"publisher":"Oxford University Press (OUP)","issue":"17","license":[{"start":{"date-parts":[[2022,6,16]],"date-time":"2022-06-16T00:00:00Z","timestamp":1655337600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"name":"Sheikh Khalifa bin Hamad Al Thani Foundation"},{"name":"University of Z\u00fcrich"},{"DOI":"10.13039\/501100001711","name":"Swiss National Science Foundation","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100001711","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Swiss Heart Foundation"},{"DOI":"10.13039\/501100012654","name":"Olga Mayenfisch Foundation","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100012654","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100013161","name":"Swiss Life Foundation","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100013161","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Kurt und Senta Hermann-Stiftung"},{"name":"EMDO Stiftung and the Schweizerische Diabetes-Stiftung"},{"DOI":"10.13039\/501100017295","name":"Holcim Foundation","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100017295","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2023,1,18]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Aims<\/jats:title>\n                    <jats:p>Methylation of non-histone proteins is emerging as a central regulatory mechanism in health and disease. The methyltransferase SETD7 has shown to methylate and alter the function of a variety of proteins in vitro; however, its function in the heart is poorly understood. The present study investigates the role of SETD7 in myocardial ischaemic injury.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods and results<\/jats:title>\n                    <jats:p>Experiments were performed in neonatal rat ventricular myocytes (NRVMs), SETD7 knockout mice (SETD7\u2212\/\u2212) undergoing myocardial ischaemia\/reperfusion (I\/R) injury, left ventricular (LV) myocardial samples from patients with ischaemic cardiomyopathy (ICM), and peripheral blood mononuclear cells (PBMCs) from patients with ST-elevation MI (STEMI). We show that SETD7 is activated upon energy deprivation in cultured NRVMs and methylates the Hippo pathway effector YAP, leading to its cytosolic retention and impaired transcription of antioxidant genes manganese superoxide dismutase (MnSOD) and catalase (CAT). Such impairment of antioxidant defence was associated with mitochondrial reactive oxygen species (mtROS), organelle swelling, and apoptosis. Selective pharmacological inhibition of SETD7 by (R)-PFI-2 restored YAP nuclear localization, thus preventing mtROS, mitochondrial damage, and apoptosis in NRVMs. In mice, genetic deletion of SETD7 attenuated myocardial I\/R injury, mtROS, and LV dysfunction by restoring YAP-dependent transcription of MnSOD and CAT. Moreover, in cardiomyocytes isolated from I\/R mice and ICM patients, (R)-PFI-2 prevented mtROS accumulation, while improving Ca2+-activated tension. Finally, SETD7 was up-regulated in PBMCs from STEMI patients and negatively correlated with MnSOD and CAT.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion<\/jats:title>\n                    <jats:p>We show a methylation-dependent checkpoint regulating oxidative stress during myocardial ischaemia. SETD7 inhibition may represent a valid therapeutic strategy in this setting.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1093\/cvr\/cvac102","type":"journal-article","created":{"date-parts":[[2022,6,16]],"date-time":"2022-06-16T14:40:31Z","timestamp":1655390431000},"page":"3374-3385","source":"Crossref","is-referenced-by-count":29,"title":["Methylation of the Hippo effector YAP by the methyltransferase SETD7 drives myocardial ischaemic injury: a translational study"],"prefix":"10.1093","volume":"118","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2112-1122","authenticated-orcid":false,"given":"Samuele","family":"Ambrosini","sequence":"first","affiliation":[{"name":"Center for Molecular Cardiology, University of Z\u00fcrich , Wagistrasse 12, 8952 Schlieren , Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0823-8729","authenticated-orcid":false,"given":"Fabrizio","family":"Montecucco","sequence":"additional","affiliation":[{"name":"First Clinic of Internal Medicine, Department of Internal Medicine, University of Genoa , viale Benedetto XV, 16132, Genoa , Italy"},{"name":"IRCCS Ospedale Policlinico San Martino Genova-Italian Cardiovascular Network , Largo Rosanna Benzi, 10, 16132 Genova , Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Detmar","family":"Kolijn","sequence":"additional","affiliation":[{"name":"Institute of Physiology, Ruhr University , Universit\u00e4tsstra\u00dfe 150, 44801 Bochum , Germany"},{"name":"Molecular and Experimental Cardiology, Ruhr University , Universit\u00e4tsstra\u00dfe 150, 44801 Bochum , Germany"},{"name":"Department of Cardiology, St-Josef Hospital, Ruhr University , Gudrunstra\u00dfe 56, 44791 Bochum , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniela","family":"Pedicino","sequence":"additional","affiliation":[{"name":"Dipartimento di Scienze Cardiovascolari e Toraciche, Universit\u00e0 Cattolica del Sacro Cuore , Largo Agostino Gemelli 8, 00168, Rome , Italy"},{"name":"Fondazione Policlinico Universitario A. 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