{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T17:42:12Z","timestamp":1788975732828,"version":"build-2803163510"},"reference-count":190,"publisher":"Bioscientifica","issue":"3","content-domain":{"domain":["joe.bioscientifica.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2023,7,13]]},"abstract":"<jats:p>Angiotensin-converting enzyme 2 (ACE2) is not only the viral receptor for the novel coronavirus severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) but is also classically known as a key carboxypeptidase, which through multiple interacting partners plays vital physiological roles in the heart, kidney, lung, and gastrointestinal tract. An accumulating body of evidence has implicated the dysregulation of ACE2 abundance and activity in the pathophysiology of multiple disease states. ACE2 has recently regained attention due to its evolving role in driving the susceptibility and disease severity of coronavirus disease 2019 (COVID-19). This narrative review outlines the current knowledge of the structure and tissue distribution of ACE2, its role in mediating SARS-CoV-2 cellular entry, its interacting partners, and functions. It also highlights how SARS-CoV-2-mediated dysregulation of membrane-bound and circulating soluble ACE2 during infection plays an important role in the pathogenesis of COVID-19. We explore contemporary evidence for the dysregulation of ACE2 in populations that have emerged as most vulnerable to COVID-19 morbidity and mortality, including the elderly, men, and pregnant women, and draw attention to ACE2 dynamics and discrepancies across the mRNA, protein (membrane-bound and circulating), and activity levels. This review highlights the need for improved understanding of the basic biology of ACE2 in populations vulnerable to COVID-19 to best ensure their clinical management and the appropriate prescription of targeted therapeutics.<\/jats:p>","DOI":"10.1530\/joe-22-0262","type":"journal-article","created":{"date-parts":[[2023,7,13]],"date-time":"2023-07-13T08:18:33Z","timestamp":1689236313000},"update-policy":"https:\/\/doi.org\/10.1530\/crossmarkpolicy-5","source":"Crossref","is-referenced-by-count":6,"title":["Impact of ACE2 on the susceptibility and vulnerability to COVID-19"],"prefix":"10.1530","volume":"258","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6770-0496","authenticated-orcid":true,"given":"Kirsty G","family":"Pringle","sequence":"first","affiliation":[{"name":"School of Biomedical Sciences & Pharmacy, College of Health, Medicine and Wellbeing, University of Newcastle, Newcastle, New South Wales, Australia"},{"name":"Mothers and Babies Research Program, Hunter Medical Research Institute, New Lambton Heights, New South Wales, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8365-295X","authenticated-orcid":true,"given":"Lisa K","family":"Philp","sequence":"additional","affiliation":[{"name":"Australian Prostate Cancer Research Centre - Queensland, Centre for Genomics and Personalised Health & School of Biomedical Sciences, Faculty of Health, Queensland University of Technology, Princess Alexandra Hospital, Translational Research Institute, Brisbane, Queensland, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"416","reference":[{"key":"bib1","series-title":"Cancer Research","first-page":"1686","article-title":"Catalytic cleavage of the androgen-regulated TMPRSS2 protease results in its secretion by prostate and prostate cancer epithelia","volume":"61","author":"Afar","year":"2001","unstructured":"Afar DEVivanco IHubert RSKuo JChen ESaffran DCRaitano AB & Jakobovits A2001Catalytic cleavage of the androgen-regulated TMPRSS2 protease results in its secretion by prostate and prostate cancer epithelia. 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