{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T23:30:11Z","timestamp":1772839811838,"version":"3.50.1"},"reference-count":44,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2019,10,5]],"date-time":"2019-10-05T00:00:00Z","timestamp":1570233600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2019,11]]},"abstract":"<jats:p>\n                    Polycystic kidney disease (PKD) is characterized by the expansion of fluid\u2010filled cysts in the kidney, which impair the function of kidney and eventually leads to end\u2010stage renal failure. It has been previously demonstrated that transgenic overexpression of prothymosin \u03b1 (ProT) induces the development of PKD; however, the underlying mechanisms remain unclear. In this study, we used a mouse PKD model that sustains kidney\u2010specific low\u2010expression of\n                    <jats:italic>Pkd1<\/jats:italic>\n                    to illustrate that aberrant up\u2010regulation of ProT occurs in cyst\u2010lining epithelial cells, and we further developed an\n                    <jats:italic>in vitro<\/jats:italic>\n                    cystogenesis model to demonstrate that the suppression of ProT is sufficient to reduce cyst formation. Next, we found that the expression of ProT was accompanied with prominent augmentation of protein acetylation in PKD, which results in the activation of downstream signal transducer and activator of transcription (STAT) 3. The pathologic role of STAT3 in PKD has been previously reported. We determined that this molecular mechanism of protein acetylation is involved with the interaction between ProT and STAT3; consequently, it causes the deprivation of histone deacetylase 3 from the indicated protein. Conclusively, these results elucidate the significant role of ProT, including protein acetylation and STAT3 activation in PKD, which represent potential for ameliorating the disease progression of PKD.\u2014Chen, Y.\u2010C., Su, Y.\u2010C., Shieh, G.\u2010S., Su, B.\u2010H., Su, W.\u2010C., Huang, P.\u2010H., Jiang, S.\u2010T., Shiau, A.\u2010L., Wu, C.\u2010L. Prothymosin \u03b1 promotes STAT3 acetylation to induce cystogenesis in Pkd1\u2010deficient mice. FASEB J. 33, 13051\u201313061 (2019).\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.fasebj.org\">www.fasebj.org<\/jats:ext-link>\n                  <\/jats:p>","DOI":"10.1096\/fj.201900504r","type":"journal-article","created":{"date-parts":[[2019,10,7]],"date-time":"2019-10-07T16:40:40Z","timestamp":1570466440000},"page":"13051-13061","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Prothymosin \u03b1 promotes STAT3 acetylation to induce cystogenesis in Pkd1\u2010deficient mice"],"prefix":"10.1096","volume":"33","author":[{"given":"Yi\u2010Cheng","family":"Chen","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yu\u2010Chu","family":"Su","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology"},{"name":"Department of Otolaryngology National Cheng Kung University Hospital"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gia\u2010Shing","family":"Shieh","sequence":"additional","affiliation":[{"name":"Department of Urology Tainan Hospital, Ministry of Health and Welfare, Executive Yuan Tainan Taiwan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bing\u2010Hua","family":"Su","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wen\u2010Cheng","family":"Su","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pei\u2010Hsin","family":"Huang","sequence":"additional","affiliation":[{"name":"Department of Pathology National Taiwan University Hospital Taipei Taiwan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Si\u2010Tse","family":"Jiang","sequence":"additional","affiliation":[{"name":"National Laboratory Animal Center, National Applied Research Laboratories Taipei Taiwan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ai\u2010Li","family":"Shiau","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology College of Medicine, National Cheng Kung University Tainan Taiwan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chao\u2010Liang","family":"Wu","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2019,10,5]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.med.60.101707.125712"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.3390\/cells4040687"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a028209"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-319-51436-9_11"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-981-10-2041-4_5"},{"key":"e_1_2_8_7_1","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2369-13-109"},{"key":"e_1_2_8_8_1","doi-asserted-by":"publisher","DOI":"10.1002\/j.2040-4603.2017.tb00760.x"},{"key":"e_1_2_8_9_1","first-page":"92","article-title":"Surfing on prothymosin alpha proliferation and anti\u2010apoptotic properties","volume":"53","author":"Letsas K. 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