TRHR

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Tirotropin-oslobađajući hormonski receptor
Identifikatori
SimboliTRHR; MGC141920
Vanjski IDOMIM: 188545 MGI: 98824 HomoloGene: 20707 IUPHAR: TRH1 GeneCards: TRHR Gene
Ontologija gena
Molekularna funkcija • aktivnost rodopsinu-sličnog receptor
• receptorska aktivnost
• aktivnost tirotropin-oslobađajućeg hormonskog receptora
Celularna komponenta • integralno sa ćelijskom membranom
• membrana
Biološki proces • prenos signala
• signalni put G-protein spregnutog receptora
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez720122045
EnsemblENSG00000174417ENSMUSG00000038760
UniProtP34981Q32MS1
RefSeq (mRNA)NM_003301NM_013696
RefSeq (protein)NP_003292NP_038724
Lokacija (UCSC)Chr 8:
110.17 - 110.2 Mb		Chr 15:
44.03 - 44.06 Mb
PubMed pretraga[1][2]

TRHR (tirotropin-oslobađajući hormonski receptor) je G protein-spregnuti receptor koji vezuje tripeptid tireotropin oslobađajući hormon.[1][2] TRHR je nađen u mozgu. Kad je ovaj receptor vezan za TRH dejstvuje kroz fosfolipazu C i povišava intracelularnu koncentraciju inozitol trifosfata.

Reference

  1. ↑ Yamada M, Monden T, Konaka S, Mori M (1993). „Assignment of human thyrotropin-releasing hormone (TRH) receptor gene to chromosome 8”. Somat. Cell Mol. Genet. 19 (6): 577–80. DOI:10.1007/BF01233384. PMID 8128317. 
  2. ↑ Gershengorn MC (1993). „Thyrotropin-releasing hormone receptor: cloning and regulation of its expression”. Recent Prog. Horm. Res. 48: 341–63. PMID 8382829. 

Literatura

  • Short RE, James LF, Panter KE, et al. (1993). „Effects of feeding ponderosa pine needles during pregnancy: comparative studies with bison, cattle, goats, and sheep.”. J. Anim. Sci. 70 (11): 3498–504. PMID 1459912. 
  • Yamada M, Iwasaki T, Satoh T, et al. (1996). „Activation of the thyrotropin-releasing hormone (TRH) receptor by a direct precursor of TRH, TRH-Gly.”. Neurosci. Lett. 196 (1-2): 109–12. DOI:10.1016/0304-3940(95)11861-P. PMID 7501234. 
  • Hinuma S, Hosoya M, Ogi K, et al. (1994). „Molecular cloning and functional expression of a human thyrotropin-releasing hormone (TRH) receptor gene.”. Biochim. Biophys. Acta 1219 (2): 251–9. PMID 7918619. 
  • Morrison N, Duthie SM, Boyd E, et al. (1994). „Assignment of the gene encoding the human thyrotropin-releasing hormone receptor to 8q23 by fluorescence in situ hybridization.”. Hum. Genet. 93 (6): 716–8. PMID 8005602. 
  • Yamada M, Monden T, Konaka S, Mori M (1994). „Assignment of human thyrotropin-releasing hormone (TRH) receptor gene to chromosome 8.”. Somat. Cell Mol. Genet. 19 (6): 577–80. DOI:10.1007/BF01233384. PMID 8128317. 
  • Duthie SM, Taylor PL, Anderson L, et al. (1994). „Cloning and functional characterisation of the human TRH receptor.”. Mol. Cell. Endocrinol. 95 (1-2): R11–5. DOI:10.1016/0303-7207(93)90043-J. PMID 8243797. 
  • Matre V, Karlsen HE, Wright MS, et al. (1993). „Molecular cloning of a functional human thyrotropin-releasing hormone receptor.”. Biochem. Biophys. Res. Commun. 195 (1): 179–85. DOI:10.1006/bbrc.1993.2027. PMID 8395824. 
  • Yamada M, Monden T, Satoh T, et al. (1993). „Pituitary adenomas of patients with acromegaly express thyrotropin-releasing hormone receptor messenger RNA: cloning and functional expression of the human thyrotropin-releasing hormone receptor gene.”. Biochem. Biophys. Res. Commun. 195 (2): 737–45. DOI:10.1006/bbrc.1993.2107. PMID 8396925. 
  • Iwasaki T, Yamada M, Satoh T, et al. (1996). „Genomic organization and promoter function of the human thyrotropin-releasing hormone receptor gene.”. J. Biol. Chem. 271 (36): 22183–8. DOI:10.1074/jbc.271.36.22183. PMID 8703031. 
  • Cook JV, McGregor A, Lee T, et al. (1996). „A disulfide bonding interaction role for cysteines in the extracellular domain of the thyrotropin-releasing hormone receptor.”. Endocrinology 137 (7): 2851–8. DOI:10.1210/en.137.7.2851. PMID 8770906. 
  • Collu R, Tang J, Castagné J, et al. (1997). „A novel mechanism for isolated central hypothyroidism: inactivating mutations in the thyrotropin-releasing hormone receptor gene.”. J. Clin. Endocrinol. Metab. 82 (5): 1561–5. DOI:10.1210/jc.82.5.1561. PMID 9141550. 
  • Petrou C, Tashjian AH (1999). „The thyrotropin-releasing hormone-receptor complex and G11alpha are both internalised into clathrin-coated vesicles.”. Cell. Signal. 10 (8): 553–9. DOI:10.1016/S0898-6568(97)00190-3. PMID 9794253. 
  • Matre V, Høvring PI, Orstavik S, et al. (1999). „Structural and functional organization of the gene encoding the human thyrotropin-releasing hormone receptor.”. J. Neurochem. 72 (1): 40–50. DOI:10.1046/j.1471-4159.1999.0720040.x. PMID 9886052. 
  • Kroeger KM, Hanyaloglu AC, Seeber RM, et al. (2001). „Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer.”. J. Biol. Chem. 276 (16): 12736–43. DOI:10.1074/jbc.M011311200. PMID 11278883. 
  • Zhu CC, Cook LB, Hinkle PM (2002). „Dimerization and phosphorylation of thyrotropin-releasing hormone receptors are modulated by agonist stimulation.”. J. Biol. Chem. 277 (31): 28228–37. DOI:10.1074/jbc.M204221200. PMID 12023974. 
  • Hanyaloglu AC, Seeber RM, Kohout TA, et al. (2003). „Homo- and hetero-oligomerization of thyrotropin-releasing hormone (TRH) receptor subtypes. Differential regulation of beta-arrestins 1 and 2.”. J. Biol. Chem. 277 (52): 50422–30. DOI:10.1074/jbc.M209340200. PMID 12393857. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). „Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. DOI:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
  • Cook LB, Zhu CC, Hinkle PM (2004). „Thyrotropin-releasing hormone receptor processing: role of ubiquitination and proteasomal degradation.”. Mol. Endocrinol. 17 (9): 1777–91. DOI:10.1210/me.2003-0073. PMID 12805411. 
  • Igarashi-Migitaka J, Yamada S, Hara M, et al. (2004). „Gene expression study of thyrotropin releasing hormone (TRH) receptor using RT-PCR: relationship to clinical and immunohistochemical phenotypes in a series of human pituitary adenomas.”. Endocr. J. 50 (4): 459–67. DOI:10.1507/endocrj.50.459. PMID 14599121. 
  • Cook LB, Hinkle PM (2004). „Fate of internalized thyrotropin-releasing hormone receptors monitored with a timer fusion protein.”. Endocrinology 145 (7): 3095–100. DOI:10.1210/en.2004-0304. PMID 15117874. 

Spoljašnje veze

  • „Thyrotropin-Releasing Hormone Receptors”. IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. Arhivirano iz originala na datum 2012-09-08. 
  • MeSH Receptors,+Thyrotropin-Releasing+Hormone
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Klasa A: Rodopsinu slični
α1 (A, B, D) • α2 (A, B, C) • β1 • β2 • β3
Adenozinski (A1, A2A, A2B, A3) • P2Y (1, 2, 4, 5, 6, 8, 9, 10, 11, 12, 13, 14)
(svi osim 5-HT3) 5-HT1 (A, B, D, E, F) • 5-HT2 (A, B, C) • 5-HT (4, 5A, 6, 7)
Drugi
Acetilholin (M1, M2, M3, M4, M5) • Dopamin (D1, D2, D3, D4, D5) • Histamin (H1, H2, H3, H4) • Melatonin (1A, 1B, 1C) • TAAR (1, 2, 3, 5, 6, 8, 9)
Metaboliti i
signalni molekuli
CysLT (1, 2) • LTB4 (1, 2) • FPRL1 • OXE • Prostaglandin (DP (1, 2), EP (1, 2, 3, 4), FP) • Prostaciklin • Tromboksan
Drugi
Žučna kiselina • Kanabinoidni (CB1, CB2, GPR (18, 55, 119)) • EBI2 • Estrogen • Slobodna masna kiselina (1, 2, 3, 4) • Laktat  • Lizofosfatidna kiselina (1, 2, 3, 4, 5, 6)  • Lizofosfolipid (1, 2, 3, 4, 5, 6, 7, 8) • Niacin (1, 2) • Oksoglutarat • PAF • Sfingozin-1-fosfat (1, 2, 3, 4, 5) • Sukcinat
Peptid
B/W (1, 2) • FF (1, 2) • S • Y (1, 2, 4, 5) • Neuromedin (B, U (1, 2)) • Neurotenzin (1, 2)
Drugi
Anafilatoksin (C3a, C5a) • Angiotenzin (1, 2) • Apelin • Bombezin (BRS3, GRPR, NMBR) • Bradikinin (B1, B2) • Hemokin • Holecistokinin (A, B) • Endotelin (A, B) • Formil peptid (1, 2, 3) • FSH • Galanin (1, 2, 3) • GHB receptor • Gonadotropin-oslobađajući hormon (1, 2) • Grelin • Kispeptin • Luteinizirajući hormon/horiogonadotropin • MAS (1, 1L, D, E, F, G, X1, X2, X3, X4) • Melanokortin (1, 2, 3, 4, 5) • MCHR (1, 2) • Motilin • Opioidni (δ, κ, μ, Nociceptin & ζ, ali ne σ) • Oreksin (1, 2) • Oksitocin • Prokineticin (1, 2) • Prolaktin-oslobađajući peptid • Relaksin (1, 2, 3, 4) • Somatostatin (1, 2, 3, 4, 5) • Tahikinin (1, 2, 3) • Tirotropin • Tirotropin-oslobađajući hormon • Urotenzin-II • Vazopresin (1A, 1B, 2)
Razno
GPR (1, 3, 4, 6, 12, 15, 17, 18, 19, 20, 21, 22, 23, 25, 26, 27, 31, 32, 33, 34, 35, 37, 39, 42, 44, 45, 50, 52, 55, 61, 62, 63, 65, 68, 75, 77, 78, 81, 82, 83, 84, 85, 87, 88, 92, 101, 103, 109A, 109B, 119, 120, 132, 135, 137B, 139, 141, 142, 146, 148, 149, 150, 151, 152, 153, 160, 161, 162, 171, 173, 174, 176, 177, 182, 183)
Drugi
Adrenomedulin • Mirisni • Opsin (3, 4, 5, 1LW, 1MW, 1SW, RGR, RRH) • Proteazom-aktivirani (1, 2, 3, 4) • SREB (1, 2, 3)
Klasa B: Sekretinu slični
GPR (56, 64, 97, 98, 110, 111, 112, 113, 114, 115, 116, 123, 124, 125, 126, 128, 133, 143, 144, 155, 157)
Drugi
Klasa C: Metabotropni
glutamat / feromon
TAS1R (1, 2, 3) • TAS2R (1, 3, 4, 5, 8, 9, 10, 12, 13, 14, 16, 19, 20, 30, 31, 38, 39, 40, 41, 42, 43, 45, 46, 50)
Drugi
Klasa F:
Frizzled / Zaglađeni
Uvojiti
Frizzled (1, 2, 3, 4, 5, 6, 7, 8, 9, 10)
Zaglađeni
B trdu: peptidi (nrpl/grfl/cytl/horl), receptori (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd, signalni putevi (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
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Hormoni
vidi hormoni
Opioidni peptidi
Drugi
Drugi neuropeptidi
Kinini
Neuromedini
B • N • S • U
Drugi
B trdu: peptidi (nrpl/grfl/cytl/horl), receptori (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd, signalni putevi (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)