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Title 

A simple ELISA for screening ligands of peroxisome proliferator-activated receptorγ

Authors 

Min Chul ChoHae Sook LeeJae Wha KimYong Kyung ChoeJ T HongS G PaikDo Young Yoon

Publisher 

Springer Verlag (Germany)

Issue Date 

2003

Citation 

Journal of Biochemistry and Molecular Biology, vol. 36, no. 2, pp. 207-213

Keywords 

enzyme-linked immunosorbent assayglutathione s-transferaseperoxisome proliferator-activated receptor-γ2steroid receptor coactivator-1cell receptorhistone acetyltransferaseindometacinligandrecombinant proteinsteroid receptor coactivator 1

Abstract 

Peroxisome proliferator-activated receptors (PPARs) are orphan nuclear hormone receptors that are known to control the expression of genes that are involved in lipid homeostasis and energy balance. PPARs activate gene transcription in response to a variety of compounds, including hypolipidemic drugs. Most of these compounds have high affinity to the ligand-binding domain (LBD) of PPARs and cause a conformational change within PPARs. As a result, the receptor is converted to an activated mode that promotes the recruitment of co-activators such as the steroid receptor co-activator-1 (SRC-1). Based on the activation mechanism of PPARs (the ligand binding to PPARγ induces interactions of the receptor with transcriptional co-activators), we performed Western blot and ELISA. These showed that the indomethacin, a PPARγ ligand, increased the binding between PPARγ and SRC-1 in a ligand dose-dependent manner. These results suggested that the in vitro conformational change of PPARγ by ligands was also induced, and increased the levels of the ligand-dependent interaction with SRC-1. Collectively, we developed a novel and useful ELISA system for the mass screening of PPARγ ligands. This screening system (based on the interaction between PPARγ and SRC-1) may be a promising system in the development of drugs for metabolic disorders.

ISSN 

1225-8687

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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