{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T15:05:55Z","timestamp":1787065555055,"version":"build-2736575974"},"reference-count":56,"publisher":"American Society for Clinical Investigation","issue":"22","funder":[{"DOI":"10.13039\/100000050","name":"National Heart, Lung, and Blood Institute","doi-asserted-by":"crossref","award":["the Intramural Research Program"],"award-info":[{"award-number":["the Intramural Research Program"]}],"id":[{"id":"10.13039\/100000050","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2018,11,15]]},"abstract":"<jats:p>\n                    Mono-ADP-ribosylation of an (arginine) protein catalyzed by ADP-ribosyltransferase 1 (ART1) \u2014 i.e., transfer of ADP-ribose from NAD to arginine \u2014 is reversed by ADP-ribosylarginine hydrolase 1 (ARH1) cleavage of the ADP-ribose\u2013arginine bond.\n                    <jats:italic>ARH1<\/jats:italic>\n                    -deficient mice developed cardiomyopathy with myocardial fibrosis, decreased myocardial function under dobutamine stress, and increased susceptibility to ischemia\/reperfusion injury. The membrane repair protein TRIM72 was identified as a substrate for ART1 and ARH1; ADP-ribosylated TRIM72 levels were greater in\n                    <jats:italic>ARH1<\/jats:italic>\n                    -deficient mice following ischemia\/reperfusion injury. To understand better the role of TRIM72 and ADP-ribosylation, we used C2C12 myocytes.\n                    <jats:italic>ARH1<\/jats:italic>\n                    knockdown in C2C12 myocytes increased ADP-ribosylation of TRIM72 and delayed wound healing in a scratch assay. Mutant TRIM72 (R207K, R260K) that is not ADP-ribosylated interfered with assembly of TRIM72 repair complexes at a site of laser-induced injury. The regulatory enzymes ART1 and ARH1 and their substrate TRIM72 were found in multiple complexes, which were coimmunoprecipitated from mouse heart lysates. In addition, the mono-ADP-ribosylation inhibitors vitamin K\n                    <jats:sub>1<\/jats:sub>\n                    and novobiocin inhibited oligomerization of TRIM72, the mechanism by which TRIM72 is recruited to the site of injury. We propose that a mono-ADP-ribosylation cycle involving recruitment of TRIM72 and other regulatory factors to sites of membrane damage is critical for membrane repair and wound healing following myocardial injury.\n                  <\/jats:p>","DOI":"10.1172\/jci.insight.97898","type":"journal-article","created":{"date-parts":[[2018,11,14]],"date-time":"2018-11-14T11:01:38Z","timestamp":1542193298000},"source":"Crossref","is-referenced-by-count":25,"title":["Role of a TRIM72 ADP-ribosylation cycle in myocardial injury and membrane repair"],"prefix":"10.1172","volume":"3","author":[{"given":"Hiroko","family":"Ishiwata-Endo","sequence":"first","affiliation":[{"name":"Pulmonary Branch,"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiro","family":"Kato","sequence":"additional","affiliation":[{"name":"Pulmonary Branch,"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akihiko","family":"Tonouchi","sequence":"additional","affiliation":[{"name":"Pulmonary 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