Characterization and function analysis of retinoic acid receptor (RAR) in prosobranch gastropods

2014 Fiscal Year Final Research Report

• Project/Area Number: 24380110
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Partial Multi-year Fund
• Section: 一般
• Research Field: General fisheries
• Research Institution: National Institute for Environmental Studies
• Principal Investigator: HORIGUCHI Toshihiro 独立行政法人国立環境研究所, 環境リスク研究センター, 室長 (30260186)
• Co-Investigator(Kenkyū-buntansha): OHTA Yasuhiko 鳥取大学, 農学部, 教授 (60069078) ; MORISHITA Fumihiro 広島大学, 理学(系)研究科(研究院), 助教 (20210164)
• Co-Investigator(Renkei-kenkyūsha): IGUCHI Taisen 大学共同利用機関法人自然科学研究機構, 岡崎統合バイオサイエンスセンター, 教授 (90128588)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: 軟体動物 / 前鰓類 / レチノイン酸受容体（RAR） / レチノイドX受容体（RXR） / インポセックス

Outline of Final Research Achievements

We isolated a retinoic acid receptor (RAR)-like cDNA (TcRAR) in the rock shell, Thais clavigera, and examined the transcriptional activity of the TcRAR protein by using all-trans retinoic acid (ATRA). However, no ligand-dependent transactivation was observed by this protein. We also examined the transcriptional activity of the TcRAR-ligand binding domain fused with the GAL4-DNA binding domain by using retinoic acids, retinol, and organotins and again saw no noteworthy transcriptional induction by these chemicals. Use of a mammalian two-hybrid assay to assess the interaction of the TcRAR protein with the TcRXR isoforms suggested TcRAR might form a heterodimer with the RXR isoforms. The transcriptional activity of domain-swapped TcRAR chimeric proteins (the A/B domain of TcRAR combined with the D–F domain of human RARα) was also examined and found to be ATRA-dependent. These results suggest TcRAR is not activated by retinoic acids, but can form a heterodimer with TcRXR isoforms.

Free Research Field

海洋生態毒性学