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ZFP36 promotes VDR mRNA degradation to facilitate cell death in oral and colonic epithelial cells

Authors
  • Wang, Xiangyu1, 2, 3
  • Ge, Xuejun1, 2
  • Liao, Wang4
  • Cao, Yong5
  • Li, Ran1, 2
  • Zhang, Fang1, 3
  • Zhao, Bin1, 3
  • Du, Jie1, 3, 6
  • 1 Shanxi Medical University School and Hospital of Stomatology, No. 63 Xinjian South Road, Taiyuan, Shanxi, 030001, China , Taiyuan (China)
  • 2 Shanxi Medical University School and Hospital of Stomatology, Taiyuan, Shanxi, China , Taiyuan (China)
  • 3 Shanxi Medical University School and Hospital of Stomatology, No. 56 Xinjian South Road, Taiyuan, Shanxi, 030001, China , Taiyuan (China)
  • 4 Hainan Clinical Medicine Research Institution, Haikou, China , Haikou (China)
  • 5 Shengjing Hospital of China Medical University, Shenyang, Liaoning, China , Shenyang (China)
  • 6 Shanxi Medical University, Taiyuan, Shanxi, China , Taiyuan (China)
Type
Published Article
Journal
Cell Communication and Signaling
Publisher
BioMed Central
Publication Date
Aug 11, 2021
Volume
19
Issue
1
Identifiers
DOI: 10.1186/s12964-021-00765-4
Source
Springer Nature
Keywords
Disciplines
  • Research
License
Green

Abstract

BackgroundVitamin D receptor (VDR) plays a vital protective role in oral and colonic epithelial cells. Albeit we know that VDR expression is reduced in the mucosal epithelial layers of autoimmune diseases, the mechanism by which VDR is decreased remains elusive.MethodsVDR and zinc finger protein 36 (ZFP36) levels in human samples and cell lines were detected by real-time PCR, western blot and immunostaining. Luciferase report assay was used to test cis-elements in VDR gene promoter, real-time PCR was applied to measure mRNA decay and western blot was performed to evaluate protein degradation. RNA affinity chromatography assay was used to test protein-mRNA interaction. Co-immunoprecipitation was used to detect protein–protein interaction. The role of ZFP36 in AU-rich elements (AREs) in the 3′ untranslated region (UTR) of VDR mRNA was also measured by luciferase report assay.ResultsWe identify ZFP36 can bind with the AREs in the 3’UTR of VDR mRNA, leading to mRNA degradation in oral and colonic epithelial cells under inflammatory circumstance. Either ZFP36 protein or AREs of VDR mRNA mutation abolishes this protein-mRNA binding process. After the key amino acid’s mutation, ZFP36 fails to decrease VDR mRNA expression. We also find that VDR physically binds with Y box-binding protein 1 (YBX-1) to block YBX-1’s nuclear translocation and ameliorate cell death in the presence of inflammation.ConclusionThese findings provide insights into the cause of VDR decrease in oral and colonic epithelial cells under inflammatory condition and explain how VDR maintains cell viability in these cells.6BzbZFy5QCY-oJ2EBzKUxNVideo abstract

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