{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,29]],"date-time":"2026-06-29T11:11:20Z","timestamp":1782731480331,"version":"3.54.5"},"reference-count":40,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2019,4,22]],"date-time":"2019-04-22T00:00:00Z","timestamp":1555891200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>UbiA prenyltransferase domain-containing protein 1 (UBIAD1) is a vitamin K2 biosynthetic enzyme. We previously showed the lethality of this enzyme in UBIAD1 knockout mice during the embryonic stage. However, the biological effects of UBIAD1 deficiency after birth remain unclear. In the present study, we used a tamoxifen-inducible systemic UBIAD1 knockout mouse model to determine the role of UBIAD1 in adult mice. UBIAD1 knockout resulted in the death of the mice within about 60 days of administration of tamoxifen. The pancreas presented with the most prominent abnormality in the tamoxifen-induced UBIAD1 knockout mice. The pancreas was reduced remarkably in size; furthermore, the pancreatic acinar cells disappeared and were replaced by vacuoles. Further analysis revealed that the vacuoles were adipocytes. UBIAD1 deficiency in the pancreatic acinar cells caused an increase in oxidative stress and autophagy, leading to apoptotic cell death in the tamoxifen-induced UBIAD 1 knockout mice. These results indicate that UBIAD1 is essential for maintaining the survival of pancreatic acinar cells in the pancreas.<\/jats:p>","DOI":"10.3390\/ijms20081971","type":"journal-article","created":{"date-parts":[[2019,4,22]],"date-time":"2019-04-22T11:02:53Z","timestamp":1555930973000},"page":"1971","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["UBIAD1 Plays an Essential Role in the Survival of Pancreatic Acinar Cells"],"prefix":"10.3390","volume":"20","author":[{"given":"Kimie","family":"Nakagawa","sequence":"first","affiliation":[{"name":"Laboratory of Hygienic Sciences, Kobe Pharmaceutical University, Kobe 658-8558, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kiyomi","family":"Fujiwara","sequence":"additional","affiliation":[{"name":"Laboratory of Hygienic Sciences, Kobe Pharmaceutical University, Kobe 658-8558, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akihiro","family":"Nishimura","sequence":"additional","affiliation":[{"name":"Laboratory of Hygienic Sciences, Kobe Pharmaceutical University, Kobe 658-8558, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chinami","family":"Murakami","sequence":"additional","affiliation":[{"name":"Laboratory of Hygienic Sciences, Kobe Pharmaceutical University, Kobe 658-8558, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kanaha","family":"Kawamoto","sequence":"additional","affiliation":[{"name":"Laboratory of Hygienic Sciences, Kobe Pharmaceutical University, Kobe 658-8558, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chihiro","family":"Ichinose","sequence":"additional","affiliation":[{"name":"Laboratory of Hygienic Sciences, Kobe Pharmaceutical University, Kobe 658-8558, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yumi","family":"Kunitou","sequence":"additional","affiliation":[{"name":"Laboratory of Hygienic Sciences, Kobe Pharmaceutical University, Kobe 658-8558, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4770-2910","authenticated-orcid":false,"given":"Yoshitomo","family":"Suhara","sequence":"additional","affiliation":[{"name":"Laboratory of Organic Synthesis and Medicinal Chemistry, College of Systems Engineering and Science, Faculty of Bioscience and Engineering, Shibaura Institute of Technology, Saitama 337-8570, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Toshio","family":"Okano","sequence":"additional","affiliation":[{"name":"Laboratory of Hygienic Sciences, Kobe Pharmaceutical University, Kobe 658-8558, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2014-8737","authenticated-orcid":false,"given":"Hiroshi","family":"Hasegawa","sequence":"additional","affiliation":[{"name":"Laboratory of Hygienic Sciences, Kobe Pharmaceutical University, Kobe 658-8558, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,4,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1798","DOI":"10.1182\/blood.V93.6.1798.406k22_1798_1808","article-title":"Vitamin K-dependent biosynthesis of gamma-carboxyglutamic acid","volume":"93","author":"Furie","year":"1999","journal-title":"Blood"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"13262","DOI":"10.1021\/bi981031y","article-title":"Role of the propeptide and gamma-glutamic acid domain of factor IX for in vitro carboxylation by the vitamin K-dependent carboxylase","volume":"37","author":"Stanley","year":"1998","journal-title":"Biochemistry"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1507\/endocrj.K09E-108","article-title":"Vitamin K2 suppresses proliferation and motility of hepatocellular carcinoma cells by activating steroid and xenobiotic receptor","volume":"56","author":"Azuma","year":"2009","journal-title":"Endocrine. 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