Development of a Human Estrogen Receptor Dimerization Assay for the Estrogenic Endocrine-Disrupting Chemicals Using Bioluminescence Resonance Energy Transferopen access
- Authors
- Kim, Hye Mi; Seo, Hyeyeong; Park, Yooheon; Lee, Hee-Seok; Lee, Seok-Hee; Ko, Kwang Suk
- Issue Date
- Aug-2021
- Publisher
- MDPI
- Keywords
- estrogenic endocrine-disrupting chemical; estrogen receptor; bioluminescence resonance energy transfer; risk assessment
- Citation
- INTERNATIONAL JOURNAL OF ENVIRONMENTAL RESEARCH AND PUBLIC HEALTH, v.18, no.16
- Journal Title
- INTERNATIONAL JOURNAL OF ENVIRONMENTAL RESEARCH AND PUBLIC HEALTH
- Volume
- 18
- Number
- 16
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/62245
- DOI
- 10.3390/ijerph18168875
- ISSN
- 1661-7827
1660-4601
- Abstract
- Endocrine-disrupting chemicals (EDCs) are found in food and various other substances, including pesticides and plastics. EDCs are easily absorbed into the body and have the ability to mimic or block hormone function. The radioligand binding assay based on the estrogen receptors binding affinity is widely used to detect estrogenic EDCs but is limited to radioactive substances and requires specific conditions. As an alternative, we developed a human cell-based dimerization assay for detecting EDC-mediated ER-alpha (ER alpha) dimerization using bioluminescence resonance energy transfer (BRET). The resultant novel BRET-based on the ER alpha dimerization assay was used to identify the binding affinity of 17 beta-estradiol (E2), 17 alpha-estradiol, corticosterone, diethylhexyl phthalate, bisphenol A, and 4-nonylphenol with ER alpha by measuring the corresponding BRET signals. Consequently, the BRET signals from five chemicals except corticosterone showed a dose-dependent sigmoidal curve for ER alpha, and these chemicals were suggested as positive chemicals for ER alpha. In contrast, corticosterone, which induced a BRET signal comparable to that of the vehicle control, was suggested as a negative chemical for ER alpha. Therefore, these results were consistent with the results of the existing binding assay for ER alpha and suggested that a novel BRET system can provide information about EDCs-mediated dimerization to ER alpha.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - ETC > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/62245)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.