Glucocorticoid Receptor (GR) is a steroid protein with tertiary structure and belongs to the nuclear receptor superfamily. The structure includes an amino terminal independent ligand binding domain (NTD), a highly conserved DNA binding domain (DBD), a carboxyl terminal ligand binding domain (LBD), and a hinge domain. GR is expressed in almost all vertebrate cells, and it directly up-regulates and down-regulates genes in thousands of different cell types, controlling development, metabolism, stress, inflammation, and other key tissue and organ physiological responses.

GR is involved in regulating the development of breast cancer. In ERα positive cancer cells, GR inhibits ERα transcription in A compound manner by directly binding to ERα, promoting its polyacylation (S) and copressure factor recruitment (A), or by directly binding to AP-1 (B). Activation of GR dimer also induces the expression of several typical anti-inflammatory proteins and cytokines, including MKP-1, GILZ, annexin 1, CDKN1C, IκBα, and IL-10, which inhibit the transcription of inflammatory genes and achieve anti-inflammatory effects. GR is also reported to be closely related to the pathogenesis of many common cardiovascular diseases, such as heart failure, atherosclerosis, sepsis, and myocardial ischemia. At present, The ICE has developed a relevant detection platform for GR targets and completed an in vitro screening model for GR targets drugs to help in the discovery of new drugs.

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DOI: 10.3390/cells8101227