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CD147 function is regulated by posttranslational modifications of which glycosylation has attracted the most attention. In this study, we demonstrated that glycosylated CD147 was the dominant form in heart tissue, and its levels were markedly elevated in response to transverse aortic constriction (TAC). Adeno\u2010associated virus 9\u2010mediated, cardiac\u2010specific overexpression of wild\u2010type CD147 in mice significantly promoted pressure overload\u2010induced pathological cardiac remodeling accompanied by augmented oxidative stress and ferroptosis. By contrast, mutations of CD147 glycosylation sites notably weakened these detrimental effects of CD147. Mechanistically, CD147 exacerbated TAC\u2010induced pathological cardiac remodeling via direct binding with the adaptor molecule TRAF2 and subsequent activation of TAK1 signalling, which was dependent on glycosylation of CD147. Collectively, our findings provide the first evidence that CD147 promoted pathological cardiac remodeling and dysfunction in a glycosylation\u2010dependent manner through binding the adaptor protein TRAF2 and activating the downstream TRAF2\u2010TAK1 signalling pathway. Thus, glycosylation of CD147 may be a potent interventional target for heart failure treatment.<\/jats:p>","DOI":"10.1155\/2022\/6603296","type":"journal-article","created":{"date-parts":[[2022,1,20]],"date-time":"2022-01-20T20:51:09Z","timestamp":1642711869000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["The Role of CD147 in Pathological Cardiac Hypertrophy Is Regulated by 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