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Glukokortikoidni receptor — разлика између измена

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== Agonisti i antagonisti ==
== Agonisti i antagonisti ==
[[Deksametazon]] je agonist, a [[RU486]] i [[ciproteron]] su antagonisti GR. Isto tako, [[progesteron]] i [[DHEA]] deluju kao antagonisti na GR.
[[Deksametazon]] je agonist, a [[RU486]] i [[ciproteron]] su antagonisti GR. Isto tako, [[progesteron]] i [[DHEA]] deluju kao antagonisti na GR.

==Interactions==
Glukokortikoidni receptor može da formira [[Protein-protein interakcija|interakcije]] sa:
{{Columns-list|5|
* -{[[BAG1]]}-,<ref name="pmid9603979">{{cite journal | author = Kullmann M, Schneikert J, Moll J, Heck S, Zeiner M, Gehring U, Cato AC | title = RAP46 is a negative regulator of glucocorticoid receptor action and hormone-induced apoptosis | journal = J. Biol. Chem. | volume = 273 | issue = 23 | pages = 14620–5 | year = 1998 | month = June | pmid = 9603979 | doi = 10.1074/jbc.273.23.14620 | url = | issn = }}</ref><ref name="pmid11101523">{{cite journal | author = Schneikert J, Hübner S, Langer G, Petri T, Jäättelä M, Reed J, Cato AC | title = Hsp70-RAP46 interaction in downregulation of DNA binding by glucocorticoid receptor | journal = EMBO J. | volume = 19 | issue = 23 | pages = 6508–16 | year = 2000 | month = December | pmid = 11101523 | pmc = 305849 | doi = 10.1093/emboj/19.23.6508 | url = | issn = }}</ref>
* -{[[CEBPB]]}-,<ref name="pmid9817600">{{cite journal | author = Boruk M, Savory JG, Haché RJ | title = AF-2-dependent potentiation of CCAAT enhancer binding protein beta-mediated transcriptional activation by glucocorticoid receptor | journal = Mol. Endocrinol. | volume = 12 | issue = 11 | pages = 1749–63 | year = 1998 | month = November | pmid = 9817600 | doi = 10.1210/me.12.11.1749 | url = | issn = }}</ref>
* [[CREB vezujući protein|-{CREBBP}-]],<ref name="pmid9649342">{{cite journal | author = Almlöf T, Wallberg AE, Gustafsson JA, Wright AP | title = Role of important hydrophobic amino acids in the interaction between the glucocorticoid receptor tau 1-core activation domain and target factors | journal = Biochemistry | volume = 37 | issue = 26 | pages = 9586–94 | year = 1998 | month = June | pmid = 9649342 | doi = 10.1021/bi973029x | url = | issn = }}</ref>
* -{[[DAP3]]}-,<ref name="pmid10903152">{{cite journal | author = Hulkko SM, Wakui H, Zilliacus J | title = The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the glucocorticoid receptor and affects the receptor function | journal = Biochem. J. | volume = Pt 3 | issue = | pages = 885–93 | year = 2000 | series = 349 | month = August | pmid = 10903152 | pmc = 1221218 | doi = | url = | issn = }}</ref>
* [[Protein vezan za smrt 6|-{DAXX}-]],<ref name="pmid12595526">{{cite journal | author = Lin DY, Lai MZ, Ann DK, Shih HM | title = Promyelocytic leukemia protein (PML) functions as a glucocorticoid receptor co-activator by sequestering Daxx to the PML oncogenic domains (PODs) to enhance its transactivation potential | journal = J. Biol. Chem. | volume = 278 | issue = 18 | pages = 15958–65 | year = 2003 | month = May | pmid = 12595526 | doi = 10.1074/jbc.M300387200 | url = | issn = }}</ref>
* [[Protein toplotnog šoka 90 kDa alfa (citosolni), član A1|-{HSP90AA1}-]],<ref name=pmid10903152/><ref name="pmid10066374">{{cite journal | author = Jibard N, Meng X, Leclerc P, Rajkowski K, Fortin D, Schweizer-Groyer G, Catelli MG, Baulieu EE, Cadepond F | title = Delimitation of two regions in the 90-kDa heat shock protein (Hsp90) able to interact with the glucocorticosteroid receptor (GR) | journal = Exp. Cell Res. | volume = 247 | issue = 2 | pages = 461–74 | year = 1999 | month = March | pmid = 10066374 | doi = 10.1006/excr.1998.4375 | url = | issn = }}</ref><ref name="pmid12093808">{{cite journal | author = Kanelakis KC, Shewach DS, Pratt WB | title = Nucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assembly | journal = J. Biol. Chem. | volume = 277 | issue = 37 | pages = 33698–703 | year = 2002 | month = September | pmid = 12093808 | doi = 10.1074/jbc.M204164200 | url = | issn = }}</ref><ref name="pmid9334248">{{cite journal | author = Hecht K, Carlstedt-Duke J, Stierna P, Gustafsson J, Brönnegârd M, Wikström AC | title = Evidence that the beta-isoform of the human glucocorticoid receptor does not act as a physiologically significant repressor | journal = J. Biol. Chem. | volume = 272 | issue = 42 | pages = 26659–64 | year = 1997 | month = October | pmid = 9334248 | doi = 10.1074/jbc.272.42.26659 | url = | issn = }}</ref><ref name="pmid8898375">{{cite journal | author = de Castro M, Elliot S, Kino T, Bamberger C, Karl M, Webster E, Chrousos GP | title = The non-ligand binding beta-isoform of the human glucocorticoid receptor (hGR beta): tissue levels, mechanism of action, and potential physiologic role | journal = Mol. Med. | volume = 2 | issue = 5 | pages = 597–607 | year = 1996 | month = September | pmid = 8898375 | pmc = 2230188 | doi = | url = | issn = }}</ref><ref name="pmid8645634">{{cite journal | author = van den Berg JD, Smets LA, van Rooij H | title = Agonist-free transformation of the glucocorticoid receptor in human B-lymphoma cells | journal = J. Steroid Biochem. Mol. Biol. | volume = 57 | issue = 3-4 | pages = 239–49 | year = 1996 | month = February | pmid = 8645634 | doi = 10.1016/0960-0760(95)00271-5 | url = | issn = }}</ref><ref name="pmid8621522">{{cite journal | author = Stancato LF, Silverstein AM, Gitler C, Groner B, Pratt WB | title = Use of the thiol-specific derivatizing agent N-iodoacetyl-3-[125I]iodotyrosine to demonstrate conformational differences between the unbound and hsp90-bound glucocorticoid receptor hormone binding domain | journal = J. Biol. Chem. | volume = 271 | issue = 15 | pages = 8831–6 | year = 1996 | month = April | pmid = 8621522 | doi = 10.1074/jbc.271.15.8831 | url = | issn = }}</ref>
* -{[[HNRPU]]}-,<ref name="pmid9353307">{{cite journal | author = Eggert M, Michel J, Schneider S, Bornfleth H, Baniahmad A, Fackelmayer FO, Schmidt S, Renkawitz R | title = The glucocorticoid receptor is associated with the RNA-binding nuclear matrix protein hnRNP U | journal = J. Biol. Chem. | volume = 272 | issue = 45 | pages = 28471–8 | year = 1997 | month = November | pmid = 9353307 | doi = 10.1074/jbc.272.45.28471 | url = | issn = }}</ref>
* -{[[MED1]]}-,<ref name=pmid11266503/><ref name=pmid10508170/>
* -{[[MED14]]}-,<ref name="pmid10508170">{{cite journal | author = Hittelman AB, Burakov D, Iñiguez-Lluhí JA, Freedman LP, Garabedian MJ | title = Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins | journal = EMBO J. | volume = 18 | issue = 19 | pages = 5380–8 | year = 1999 | month = October | pmid = 10508170 | pmc = 1171607 | doi = 10.1093/emboj/18.19.5380 | url = | issn = }}</ref>
* [[Mineralokortikoidni receptor]],<ref name="pmid11154266">{{cite journal | author = Savory JG, Préfontaine GG, Lamprecht C, Liao M, Walther RF, Lefebvre YA, Haché RJ | title = Glucocorticoid receptor homodimers and glucocorticoid-mineralocorticoid receptor heterodimers form in the cytoplasm through alternative dimerization interfaces | journal = Mol. Cell. Biol. | volume = 21 | issue = 3 | pages = 781–93 | year = 2001 | month = February | pmid = 11154266 | pmc = 86670 | doi = 10.1128/MCB.21.3.781-793.2001 | url = | issn = }}</ref>
* -{[[NRIP1]]}-,<ref name=pmid11266503/><ref name="pmid12773562">{{cite journal | author = Tazawa H, Osman W, Shoji Y, Treuter E, Gustafsson JA, Zilliacus J | title = Regulation of subnuclear localization is associated with a mechanism for nuclear receptor corepression by RIP140 | journal = Mol. Cell. Biol. | volume = 23 | issue = 12 | pages = 4187–98 | year = 2003 | month = June | pmid = 12773562 | pmc = 156128 | doi = 10.1128/MCB.23.12.4187-4198.2003 | url = | issn = }}</ref><ref name="pmid10364267">{{cite journal | author = Subramaniam N, Treuter E, Okret S | title = Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids | journal = J. Biol. Chem. | volume = 274 | issue = 25 | pages = 18121–7 | year = 1999 | month = June | pmid = 10364267 | doi = 10.1074/jbc.274.25.18121 | url = | issn = }}</ref>
* [[Korepresor nuklearnog receptora 1|-{NCOR1}-]],<ref name="pmid12569182">{{cite journal | author = Stevens A, Garside H, Berry A, Waters C, White A, Ray D | title = Dissociation of steroid receptor coactivator 1 and nuclear receptor corepressor recruitment to the human glucocorticoid receptor by modification of the ligand-receptor interface: the role of tyrosine 735 | journal = Mol. Endocrinol. | volume = 17 | issue = 5 | pages = 845–59 | year = 2003 | month = May | pmid = 12569182 | doi = 10.1210/me.2002-0320 | url = | issn = }}</ref><ref name="pmid12011091">{{cite journal | author = Schulz M, Eggert M, Baniahmad A, Dostert A, Heinzel T, Renkawitz R | title = RU486-induced glucocorticoid receptor agonism is controlled by the receptor N terminus and by corepressor binding | journal = J. Biol. Chem. | volume = 277 | issue = 29 | pages = 26238–43 | year = 2002 | month = July | pmid = 12011091 | doi = 10.1074/jbc.M203268200 | url = | issn = }}</ref>
* [[Koaktivator nuklearnog receptora 1|-{NCOA1}-]],<ref name=pmid11266503/><ref name="pmid12118039">{{cite journal | author = Kucera T, Waltner-Law M, Scott DK, Prasad R, Granner DK | title = A point mutation of the AF2 transactivation domain of the glucocorticoid receptor disrupts its interaction with steroid receptor coactivator 1 | journal = J. Biol. Chem. | volume = 277 | issue = 29 | pages = 26098–102 | year = 2002 | month = July | pmid = 12118039 | doi = 10.1074/jbc.M204013200 | url = | issn = }}</ref>
* [[Koaktivator nuklearnog receptora 2|-{NCOA2}-]],<ref name="pmid11266503">{{cite journal | author = Zilliacus J, Holter E, Wakui H, Tazawa H, Treuter E, Gustafsson JA | title = Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140 | journal = Mol. Endocrinol. | volume = 15 | issue = 4 | pages = 501–11 | year = 2001 | month = April | pmid = 11266503 | doi = 10.1210/me.15.4.501 | url = | issn = }}</ref><ref name="pmid12151000">{{cite journal | author = Bledsoe RK, Montana VG, Stanley TB, Delves CJ, Apolito CJ, McKee DD, Consler TG, Parks DJ, Stewart EL, Willson TM, Lambert MH, Moore JT, Pearce KH, Xu HE | title = Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition | journal = Cell | volume = 110 | issue = 1 | pages = 93–105 | year = 2002 | month = July | pmid = 12151000 | doi = 10.1016/S0092-8674(02)00817-6 | url = | issn = }}</ref>
* [[Koaktivator nuklearnog receptora 3|-{NCOA3}-]],<ref name=pmid11266503/><ref name="pmid12917342">{{cite journal | author = Hsiao PW, Fryer CJ, Trotter KW, Wang W, Archer TK | title = BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation | journal = Mol. Cell. Biol. | volume = 23 | issue = 17 | pages = 6210–20 | year = 2003 | month = September | pmid = 12917342 | pmc = 180928 | doi = 10.1128/MCB.23.17.6210-6220.2003 | url = | issn = }}</ref>
* -{[[POU2F1]]}-,<ref name=pmid10480874>{{cite journal |doi=10.1074/jbc.274.38.26713 |last=Préfontaine |first=G G |authorlink= |coauthors=Walther R, Giffin W, Lemieux M E, Pope L, Haché R J |year=1999|month=Sep. |title=Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter |journal=J. Biol. Chem. |volume=274 |issue=38 |pages=26713–9 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 10480874 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name="pmid10480874">{{cite journal | author = Préfontaine GG, Walther R, Giffin W, Lemieux ME, Pope L, Haché RJ | title = Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter | journal = J. Biol. Chem. | volume = 274 | issue = 38 | pages = 26713–9 | year = 1999 | month = September | pmid = 10480874 | doi = 10.1074/jbc.274.38.26713| url = | issn = }}</ref><ref name="pmid9584182">{{cite journal | author = Préfontaine GG, Lemieux ME, Giffin W, Schild-Poulter C, Pope L, LaCasse E, Walker P, Haché RJ | title = Recruitment of octamer transcription factors to DNA by glucocorticoid receptor | journal = Mol. Cell. Biol. | volume = 18 | issue = 6 | pages = 3416–30 | year = 1998 | month = June | pmid = 9584182 | pmc = 108923 | doi = | url = | issn = }}</ref>
* -{[[RANBP9]]}-,<ref name=pmid12361945>{{cite journal |last=Rao |first=Mira A |authorlink= |coauthors=Cheng Helen, Quayle Alandra N, Nishitani Hideo, Nelson Colleen C, Rennie Paul S |year=2002|month=Dec. |title=RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor |journal=J. Biol. Chem. |volume=277 |issue=50 |pages=48020–7 |publisher= |location = United States| issn = 0021-9258| pmid = 12361945 |doi = 10.1074/jbc.M209741200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>
* -{[[RELA]]}-,<ref name="pmid12361945">{{cite journal | author = Rao MA, Cheng H, Quayle AN, Nishitani H, Nelson CC, Rennie PS | title = RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor | journal = J. Biol. Chem. | volume = 277 | issue = 50 | pages = 48020–7 | year = 2002 | month = December | pmid = 12361945 | doi = 10.1074/jbc.M209741200 | url = | issn = }}</ref><ref name="pmid10995388">{{cite journal | author = Nissen RM, Yamamoto KR | title = The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain | journal = Genes Dev. | volume = 14 | issue = 18 | pages = 2314–29 | year = 2000 | month = September | pmid = 10995388 | pmc = 316928 | doi = 10.1101/gad.827900 | url = | issn = }}</ref><ref name="pmid7659084">{{cite journal | author = Caldenhoven E, Liden J, Wissink S, Van de Stolpe A, Raaijmakers J, Koenderman L, Okret S, Gustafsson JA, Van der Saag PT | title = Negative cross-talk between RelA and the glucocorticoid receptor: a possible mechanism for the antiinflammatory action of glucocorticoids | journal = Mol. Endocrinol. | volume = 9 | issue = 4 | pages = 401–12 | year = 1995 | month = April | pmid = 7659084 | doi = 10.1210/me.9.4.401 | url = | issn = }}</ref>
* -{[[SMAD3]]}-,<ref name="pmid12902338">{{cite journal | author = Li G, Wang S, Gelehrter TD | title = Identification of glucocorticoid receptor domains involved in transrepression of transforming growth factor-beta action | journal = J. Biol. Chem. | volume = 278 | issue = 43 | pages = 41779–88 | year = 2003 | month = October | pmid = 12902338 | doi = 10.1074/jbc.M305350200 | url = | issn = }}</ref><ref name="pmid10518526">{{cite journal | author = Song CZ, Tian X, Gelehrter TD | title = Glucocorticoid receptor inhibits transforming growth factor-beta signaling by directly targeting the transcriptional activation function of Smad3 | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 96 | issue = 21 | pages = 11776–81 | year = 1999 | month = October | pmid = 10518526 | pmc = 18362 | doi = 10.1073/pnas.96.21.11776 | url = | issn = }}</ref>
* -{[[SMARCD1]]}-,<ref name=pmid12917342/>
* -{[[SMARCA4]]}-<ref name=pmid12917342/><ref name="pmid10688647">{{cite journal | author = Wallberg AE, Neely KE, Hassan AH, Gustafsson JA, Workman JL, Wright AP | title = Recruitment of the SWI-SNF chromatin remodeling complex as a mechanism of gene activation by the glucocorticoid receptor tau1 activation domain | journal = Mol. Cell. Biol. | volume = 20 | issue = 6 | pages = 2004–13 | year = 2000 | month = March | pmid = 10688647 | pmc = 110817 | doi = 10.1128/MCB.20.6.2004-2013.2000 | url = | issn = }}</ref>
* -{[[STAT3]]}-,<ref name="pmid14522952">{{cite journal | author = Lerner L, Henriksen MA, Zhang X, Darnell JE | title = STAT3-dependent enhanceosome assembly and disassembly: synergy with GR for full transcriptional increase of the alpha 2-macroglobulin gene | journal = Genes Dev. | volume = 17 | issue = 20 | pages = 2564–77 | year = 2003 | month = October | pmid = 14522952 | pmc = 218150 | doi = 10.1101/gad.1135003 | url = | issn = }}</ref><ref name="pmid9388192">{{cite journal | author = Zhang Z, Jones S, Hagood JS, Fuentes NL, Fuller GM | title = STAT3 acts as a co-activator of glucocorticoid receptor signaling | journal = J. Biol. Chem. | volume = 272 | issue = 49 | pages = 30607–10 | year = 1997 | month = December | pmid = 9388192 | doi = 10.1074/jbc.272.49.30607 | url = | issn = }}</ref>
* -{[[STAT5B]]}-,<ref name="pmid8878484">{{cite journal | author = Stöcklin E, Wissler M, Gouilleux F, Groner B | title = Functional interactions between Stat5 and the glucocorticoid receptor | journal = Nature | volume = 383 | issue = 6602 | pages = 726–8 | year = 1996 | month = October | pmid = 8878484 | doi = 10.1038/383726a0 | url = | issn = }}</ref>
* [[Tioredoksin]],<ref name="pmid9915858">{{cite journal | author = Makino Y, Yoshikawa N, Okamoto K, Hirota K, Yodoi J, Makino I, Tanaka H | title = Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function | journal = J. Biol. Chem. | volume = 274 | issue = 5 | pages = 3182–8 | year = 1999 | month = January | pmid = 9915858 | doi = 10.1074/jbc.274.5.3182 | url = | issn = }}</ref>
* -{[[TRIM28]]}-,<ref name="pmid9742105">{{cite journal | author = Chang CJ, Chen YL, Lee SC | title = Coactivator TIF1beta interacts with transcription factor C/EBPbeta and glucocorticoid receptor to induce alpha1-acid glycoprotein gene expression | journal = Mol. Cell. Biol. | volume = 18 | issue = 10 | pages = 5880–7 | year = 1998 | month = October | pmid = 9742105 | pmc = 109174 | doi = | url = | issn = }}</ref> and
* -{[[YWHAH]]}-.<ref name="pmid9079630">{{cite journal | author = Wakui H, Wright AP, Gustafsson J, Zilliacus J | title = Interaction of the ligand-activated glucocorticoid receptor with the 14-3-3 eta protein | journal = J. Biol. Chem. | volume = 272 | issue = 13 | pages = 8153–6 | year = 1997 | month = March | pmid = 9079630 | doi = 10.1074/jbc.272.13.8153 | url = | issn = }}</ref>
}}


== Reference ==
== Reference ==

Верзија на датум 7. новембар 2013. у 20:47

Nuklearni receptor potfamilije 3, grupa C, član 1 (glukokortikoidni receptor)
Kristalografska struktura DNK vezujućeg domena glukokortikoidnog receptora (DBD, levo, 1R4O​ vezan za DNK) i ligand vezujući domen [LBD, desno, 1M2Z​ vezan za deksametazon (beli štapići) i TIF2 koaktivatorski protein (crveno)]. Isprekidane žute linije predstavljaju interakcije vodoničnog vezivanja između receptora i liganda. 2D struktura deksametazona je takođe prikazana u dole desno.
Dostupne strukture
1M2Z​, 1NHZ​, 1P93​, 3BQD​, 3CLD​, 3E7C​, 3H52​, 3K22​, 3K23​, 4HN5​, 4HN6​
Identifikatori
Simboli NR3C1; GCCR; GCR; GR; GRL
Vanjski ID OMIM: 138040 MGI: 95824 HomoloGene: 30960 IUPHAR: GeneCards: NR3C1 Gene
Pregled RNK izražavanja
podaci
Ortolozi
Vrsta Čovek Miš
Entrez 2908 14815
Ensembl ENSG00000113580 ENSMUSG00000024431
UniProt P04150 E9PUR6
RefSeq (mRNA) NM_000176 NM_008173
RefSeq (protein) NP_000167 NP_032199
Lokacija (UCSC) Chr 5:
142.66 - 142.82 Mb		 Chr 18:
39.41 - 39.49 Mb
PubMed pretraga [1] [2]

Glukokortikoidni receptor (GR, GCR, NR3C1, nuklearni receptor potfamilija 3, grupa C, član 1) receptor je za koji se vezuju kortizol i drugi glukokortikoidi.

GR je izražen u skoro svim ćelijma a telu i reguliše gene koji kontrolišu razviće, metabolizam, i imunski respons. Gen ovog receptora se izražava u nekoliko formi, te stoga GR ima mnoštvo različitih (pleiotropskih) dejstava u različitim delovima tela.

Kad se za GR vežu glukokortikoidi, njegov primarni mehanizam dejstva je regulacija trakripcija gena.[1][2] Nevezani receptor se nalazi u ćelijskom citosolu. Nakon vezivanja glukokortikoida za receptor, receptor-glukortikoidni kompleks može da povisi izražavanje antiinflamatornih proteina u jedru ili da suzbije izražavanje proinflamatornih proteina u citozolu (putem sprečavanja translokacije drugih transkripcionih faktora iz citozola u jedro).

Kod ljudi, GR protein je kodiran NR3C1 genom koji je lociran na hromozomu 5 (5q31).[3][4]

Strukture

Poput drugih steroidnih receptora,[5] glukokortikoidni receptor ima modularu strukturu[6] i sadrži sledeće domene (obležene sa A - F):

Vezivanje liganda i respons

U odsustvu hormona, glukokortikoidni receptor (GR) se nalazi u citosolu u kompleksu sa raznim proteinima uključujući protein toplotnog šoka 90 (hsp90), protein toplotnog šoka 70 (hsp70) i protein FKBP52 (FK506 vezujući protein 52).[7] Endogeni glukokortikoidni hormon kortizol difuzijom prolazi kroz ćelijsku membranu u citoplazmu i vezuje se za glukokortikoidni receptor (GR), što dovodi do oslobađanja proteina toplotnog šoka. Rezultirajuća aktivirana forma GR ima dva moguća mehanizma dejstva, transaktivacija i transrepresija.[8][9]

Transaktivacija

Direktni mehanizam dejstva obuhvata homodimerizaciju receptora, translokaciju putem aktivnog transporta u jedro, i vezivanje za specifiće DNK responsivne elemente, čime se aktivira transkripcija gena. Ovaj mehanizam dejstva se naziva transaktivacija. Biološki respons zavisi od tipa ćelije.

Transrepresija

U odsustvu aktiviranog GR, drugi transkripcini faktori kao što je NF-κB ili AP-1 mogu da transaktiviraju ciljne gene.[10] Aktivirani GR može da formira kompleks as tim drugim transkripcionim faktorima i da spreči njihovo vezivanje za ciljne gene i time suzbije izražavanje gena koje normalno kontrolišu NF-κB ili AP-1. Ovaj indirektni mehanizam dejstva se naziva transrepresija.

Klinički značaj

GR je abnormalan u sučajevima familialne glukokortikoidne otpornosti.[11]

U strukturama centralnog nervnog sistema, glukokortikoidni receptor učestvuje u neuroendokrinoj integraciji. On funkcioniše kao glavna komponenta endokrinog uticaja na mozak, posebno u responsu na stres. Ovaj receptor je impliciran u kratkotrajnu i dugotrajnu adaptaciju u responsu na stresore, i važan je za razumevanje psiholoških poremećaja, uključujući pojedine tipove depresije.[12][13]

Agonisti i antagonisti

Deksametazon je agonist, a RU486 i ciproteron su antagonisti GR. Isto tako, progesteron i DHEA deluju kao antagonisti na GR.

Interactions

Glukokortikoidni receptor može da formira interakcije sa:

Reference

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