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Endocrinol."],"abstract":"<jats:p>Murine Serpina3c belongs to the family of serine protease inhibitors (Serpins), clade \u201cA\u201d and its human homologue is SerpinA3. Serpina3c is involved in some physiological processes, including insulin secretion and adipogenesis. In the pathophysiological process, the deletion of Serpina3c leads to more severe metabolic disorders, such as aggravated non-alcoholic fatty liver disease (NAFLD), insulin resistance and obesity. In addition, Serpina3c can improve atherosclerosis and regulate cardiac remodeling after myocardial infarction. Many of these processes are directly or indirectly mediated by its inhibition of serine protease activity. Although its function has not been fully revealed, recent studies have shown its potential research value. Here, we aimed to summarize recent studies to provide a clearer view of the biological roles and the underlying mechanisms of Serpina3c.<\/jats:p>","DOI":"10.3389\/fendo.2023.1189007","type":"journal-article","created":{"date-parts":[[2023,5,23]],"date-time":"2023-05-23T05:31:13Z","timestamp":1684819873000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":13,"title":["The versatile role of Serpina3c in physiological and pathological processes: a review of recent studies"],"prefix":"10.3389","volume":"14","author":[{"given":"Yang","family":"Li","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Liang","family":"Guo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2023,5,23]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","DOI":"10.1016\/S0888-7543(02)00041-1","article-title":"A review and comparison of the murine alpha1-antitrypsin and alpha1-antichymotrypsin multigene clusters with the human clade a serpins","volume":"81","author":"Forsyth","year":"2003","journal-title":"Genomics"},{"key":"B2","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1991.tb07945.x","article-title":"The murine spi-2 proteinase inhibitor locus: a multigene family with a hypervariable reactive site domain","volume":"10","author":"Inglis","year":"1991","journal-title":"EMBO J"},{"key":"B3","doi-asserted-by":"publisher","first-page":"101500","DOI":"10.1016\/j.molmet.2022.101500","article-title":"SERPINA3C ameliorates adipose tissue inflammation through the cathepsin G\/Integrin\/AKT pathway","volume":"61","author":"Li","year":"2022","journal-title":"Mol Metab"},{"key":"B4","doi-asserted-by":"publisher","first-page":"100961","DOI":"10.1016\/j.isci.2020.100961","article-title":"Serpina3c regulates adipogenesis by modulating insulin growth factor 1 and integrin signaling","volume":"23","author":"Choi","year":"2020","journal-title":"iScience"},{"key":"B5","doi-asserted-by":"publisher","first-page":"109745","DOI":"10.1016\/j.cellsig.2020.109745","article-title":"Serpina3c protects against high-fat diet-induced pancreatic dysfunction through the JNK-related pathway","volume":"75","author":"Ji","year":"2020","journal-title":"Cell Signal"},{"key":"B6","doi-asserted-by":"publisher","first-page":"110299","DOI":"10.1016\/j.cellsig.2022.110299","article-title":"Serpina3c regulates adipose differentiation","volume":"93","author":"Guo","year":"2022","journal-title":"via Wnt\/\u03b2-catenin-PPAR\u03b3 pathway. 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