The GR is expressed in almost every cell in the body and regulates genes controlling the development, metabolism, and immune response. Because the receptor gene is expressed in several forms, it has many different (pleiotropic) effects in different parts of the body.
When glucocorticoids bind to GR, its primary mechanism of action is the regulation of gene transcription.[5][6] The unbound receptor resides in the cytosol of the cell. After the receptor is bound to glucocorticoid, the receptor-glucocorticoid complex can take either of two paths. The activated GR complex up-regulates the expression of anti-inflammatory proteins in the nucleus or represses the expression of pro-inflammatory proteins in the cytosol (by preventing the translocation of other transcription factors from the cytosol into the nucleus).
In the absence of hormone, the glucocorticoid receptor (GR) resides in the cytosol complexed with a variety of proteins including heat shock protein 90 (hsp90), the heat shock protein 70 (hsp70) and the protein FKBP4 (FK506-binding protein 4).[11] The endogenous glucocorticoid hormone cortisol diffuses through the cell membrane into the cytoplasm and binds to the glucocorticoid receptor (GR) resulting in release of the heat shock proteins. The resulting activated form GR has two principal mechanisms of action, transactivation and transrepression,[12][13] described below.
In the absence of activated GR, other transcription factors such as NF-κB or AP-1 themselves are able to transactivate target genes.[14] However activated GR can complex with these other transcription factors and prevent them from binding their target genes and hence repress the expression of genes that are normally upregulated by NF-κB or AP-1. This indirect mechanism of action is referred to as transrepression.[citation needed] GR transrepression via NF-κB and AP-1 is restricted only to certain cell types, and is not considered the universal mechanism for IκBα repression. [15][16]
In central nervous system structures, the glucocorticoid receptor is gaining interest as a novel representative of neuroendocrine integration, functioning as a major component of endocrine influence - specifically the stress response - upon the brain. The receptor is now implicated in both short and long-term adaptations seen in response to stressors and may be critical to the understanding of psychological disorders, including some or all subtypes of depression and post-traumatic stress disorder (PTSD).[18] Indeed, long-standing observations such as the mood dysregulations typical of Cushing's disease demonstrate the role of corticosteroids in regulating psychologic state; recent advances have demonstrated interactions with norepinephrine and serotonin at the neural level.[19][20]
In preeclampsia (a hypertensive disorder commonly occurring in pregnant women), the level of a miRNA sequence possibly targeting this protein is elevated in the blood of the mother. Rather, the placenta elevates the level of exosomes containing this miRNA, which can result in inhibition of translation of molecule. Clinical significance of this information is not yet clarified.[21]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Lu NZ, Wardell SE, Burnstein KL, Defranco D, Fuller PJ, Giguere V, et al. (December 2006). "International Union of Pharmacology. LXV. The pharmacology and classification of the nuclear receptor superfamily: glucocorticoid, mineralocorticoid, progesterone, and androgen receptors". Pharmacological Reviews. 58 (4): 782–797. doi:10.1124/pr.58.4.9. PMID17132855. S2CID28626145. [Free full text]
^Rhen T, Cidlowski JA (October 2005). "Antiinflammatory action of glucocorticoids--new mechanisms for old drugs". The New England Journal of Medicine. 353 (16): 1711–1723. doi:10.1056/NEJMra050541. PMID16236742. S2CID5744727.
^Kumar R, Thompson EB (April 2005). "Gene regulation by the glucocorticoid receptor: structure:function relationship". The Journal of Steroid Biochemistry and Molecular Biology. 94 (5): 383–394. doi:10.1016/j.jsbmb.2004.12.046. PMID15876404. S2CID25315991.
^Pratt WB, Morishima Y, Murphy M, Harrell M (2006). "Chaperoning of glucocorticoid receptors". Molecular Chaperones in Health and Disease. Handbook of Experimental Pharmacology. Vol. 172. pp. 111–138. doi:10.1007/3-540-29717-0_5. ISBN978-3-540-25875-9. PMID16610357.
^Hayashi R, Wada H, Ito K, Adcock IM (October 2004). "Effects of glucocorticoids on gene transcription". European Journal of Pharmacology. 500 (1–3): 51–62. doi:10.1016/j.ejphar.2004.07.011. PMID15464020.
^Boruk M, Savory JG, Haché RJ (November 1998). "AF-2-dependent potentiation of CCAAT enhancer binding protein beta-mediated transcriptional activation by glucocorticoid receptor". Molecular Endocrinology. 12 (11): 1749–1763. doi:10.1210/mend.12.11.0191. PMID9817600.
^Almlöf T, Wallberg AE, Gustafsson JA, Wright AP (June 1998). "Role of important hydrophobic amino acids in the interaction between the glucocorticoid receptor tau 1-core activation domain and target factors". Biochemistry. 37 (26): 9586–9594. doi:10.1021/bi973029x. PMID9649342.
^Jibard N, Meng X, Leclerc P, Rajkowski K, Fortin D, Schweizer-Groyer G, et al. (March 1999). "Delimitation of two regions in the 90-kDa heat shock protein (Hsp90) able to interact with the glucocorticosteroid receptor (GR)". Experimental Cell Research. 247 (2): 461–474. doi:10.1006/excr.1998.4375. PMID10066374.
^van den Berg JD, Smets LA, van Rooij H (February 1996). "Agonist-free transformation of the glucocorticoid receptor in human B-lymphoma cells". The Journal of Steroid Biochemistry and Molecular Biology. 57 (3–4): 239–249. doi:10.1016/0960-0760(95)00271-5. PMID8645634. S2CID20582144.
Adcock IM, Ito K (June 2000). "Molecular mechanisms of corticosteroid actions". Monaldi Archives for Chest Disease = Archivio Monaldi per le Malattie del Torace. 55 (3): 256–266. PMID10948677.
Torrego A, Pujols L, Picado C (September 2002). "[Response to glucocorticoid treatment in asthma. The role of alpha and beta isoforms of the glucocorticoid receptor]". Archivos de Bronconeumologia. 38 (9): 436–440. doi:10.1016/S0300-2896(02)75258-7. PMID12237016.
Bray PJ, Cotton RG (June 2003). "Variations of the human glucocorticoid receptor gene (NR3C1): pathological and in vitro mutations and polymorphisms". Human Mutation. 21 (6): 557–568. doi:10.1002/humu.10213. PMID12754700. S2CID26191891.
Andersen JL, Planelles V (January 2005). "The role of Vpr in HIV-1 pathogenesis". Current HIV Research. 3 (1): 43–51. doi:10.2174/1570162052772988. PMID15638722.
Chrousos GP, Kino T (October 2005). "Intracellular glucocorticoid signaling: a formerly simple system turns stochastic". Science's STKE. 2005 (304): pe48. doi:10.1126/stke.3042005pe48. PMID16204701. S2CID23148406.
Plotkin LL, Labutin AL, Lebedev LV, Khanukov LA, Zelikson OS (1975). "[Balloon probe for the removal of emboli and thrombi]". Meditsinskaya Tekhnika (3): 42–43. PMID1152650.
Subramaniam M, Colvard D, Keeting PE, Rasmussen K, Riggs BL, Spelsberg TC (December 1992). "Glucocorticoid regulation of alkaline phosphatase, osteocalcin, and proto-oncogenes in normal human osteoblast-like cells". Journal of Cellular Biochemistry. 50 (4): 411–424. doi:10.1002/jcb.240500410. PMID1469072. S2CID21381419.
Scherrer LC, Pratt WB (March 1992). "Association of the transformed glucocorticoid receptor with a cytoskeletal protein complex". The Journal of Steroid Biochemistry and Molecular Biology. 41 (3–8): 719–721. doi:10.1016/0960-0760(92)90411-B. hdl:2027.42/30199. PMID1562545. S2CID43672040.
Cadepond F, Gasc JM, Delahaye F, Jibard N, Schweizer-Groyer G, Segard-Maurel I, et al. (July 1992). "Hormonal regulation of the nuclear localization signals of the human glucocorticosteroid receptor". Experimental Cell Research. 201 (1): 99–108. doi:10.1016/0014-4827(92)90352-9. PMID1612132.
1gdc: REFINED SOLUTION STRUCTURE OF THE GLUCOCORTICOID RECEPTOR DNA-BINDING DOMAIN
1glu: CRYSTALLOGRAPHIC ANALYSIS OF THE INTERACTION OF THE GLUCOCORTICOID RECEPTOR WITH DNA
1m2z: Crystal structure of a dimer complex of the human glucocorticoid receptor ligand-binding domain bound to dexamethasone and a TIF2 coactivator motif
1nhz: Crystal Structure of the Antagonist Form of Glucocorticoid Receptor
1p93: CRYSTAL STRUCTURE OF THE AGONIST FORM OF GLUCOCORTICOID RECEPTOR
1r4o: Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
1r4r: Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
1rgd: STRUCTURE REFINEMENT OF THE GLUCOCORTICOID RECEPTOR-DNA BINDING DOMAIN FROM NMR DATA BY RELAXATION MATRIX CALCULATIONS
2gda: REFINED SOLUTION STRUCTURE OF THE GLUCOCORTICOID RECEPTOR DNA-BINDING DOMAIN
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