Tirotropinski receptor

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Tirotropinski receptor
Identifikatori
SimboliTSHR; LGR3; MGC75129; hTSHR-I
Vanjski IDOMIM: 603372 MGI: 98849 HomoloGene: 315 IUPHAR: TSH GeneCards: TSHR Gene
Ontologija gena
Molekularna funkcija • receptorska aktivnost
• aktivnost tirotropinskog receptora
• vezivanje proteina
Celularna komponenta • ćelijska membrana
• integralno sa ćelijskom membranom
Biološki proces • prenos signala
• G-proteinska signalizacija, spregnuta sa cikličnim nukleotidnim sekundarnim glasnikom
• G-protein signalizacija, put aktiviranja adenilat ciklaze
• ćelija-ćelija signalizacija
• pozitivna regulacija ćelijske proliferacije
• lokomotorno ponašanje odraslih osoba
• regulacija lokomocije
• pozitivna regulacija veličine tela
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez725322095
EnsemblENSG00000165409ENSMUSG00000020963
UniProtP16473Q562E4
RefSeq (mRNA)NM_000369NM_011648
RefSeq (protein)NP_000360NP_035778
Lokacija (UCSC)Chr 14:
80.49 - 80.68 Mb		Chr 12:
91.81 - 91.95 Mb
PubMed pretraga[1][2]

Tirotropinski receptor (ili TSH receptor) je receptor koji odgovara na tireostimulišući hormon (takođe poznat kao "tirotropin", i stimuliše produkciju tiroksina (T4) i trijodotironina (T3). TSH receptor je član familij G protein-spregnutih receptora, integralnih membranskih proteina[1]. Ovaj receptor je spregnut sa Gs.[2]

One je prvenstveno nađen na površini tiroidnih epitelskih ćelija.

Vidi još

  • Gravesova bolest

Reference

  1. ↑ Farid NR, Szkudlinski MW (2004). „Minireview: structural and functional evolution of the thyrotropin receptor”. Endocrinology 145 (9): 4048–57. DOI:10.1210/en.2004-0437. PMID 15231707. 
  2. ↑ Calebiro D, Nikolaev VO, Lohse MJ (July 2010). „Imaging of persistent cAMP signaling by internalized G protein-coupled receptors”. J. Mol. Endocrinol. 45 (1): 1–8. DOI:10.1677/JME-10-0014. PMID 20378719. 

Literatura

  • Führer D, Wonerow P, Willgerodt H, Paschke R (1998). „Identification of a new thyrotropin receptor germline mutation (Leu629Phe) in a family with neonatal onset of autosomal dominant nonautoimmune hyperthyroidism.”. J. Clin. Endocrinol. Metab. 82 (12): 4234–8. DOI:10.1210/jc.82.12.4234. PMID 9398746. 
  • Farid NR, Kascur V, Balazs C (2000). „The human thyrotropin receptor is highly mutable: a review of gain-of-function mutations.”. Eur. J. Endocrinol. 143 (1): 25–30. DOI:10.1530/eje.0.1430025. PMID 10870027. 
  • Szkudlinski MW, Fremont V, Ronin C, Weintraub BD (2002). „Thyroid-stimulating hormone and thyroid-stimulating hormone receptor structure-function relationships.”. Physiol. Rev. 82 (2): 473–502. DOI:10.1152/physrev.00031.2001. PMID 11917095. 
  • Tonacchera M, Vitti P, De Servi M, et al. (2004). „Gain of function TSH receptor mutations and iodine deficiency: implications in iodine prophylaxis.”. J. Endocrinol. Invest. 26 (2 Suppl): 2–6. PMID 12762632. 
  • Arturi F, Scarpelli D, Coco A, et al. (2004). „Thyrotropin receptor mutations and thyroid hyperfunctioning adenomas ten years after their first discovery: unresolved questions.”. Thyroid 13 (4): 341–3. DOI:10.1089/105072503321669811. PMID 12804102. 
  • Vaidya B, Campbell V, Tripp JH, et al. (2004). „Premature birth and low birth weight associated with nonautoimmune hyperthyroidism due to an activating thyrotropin receptor gene mutation.”. Clin. Endocrinol. (Oxf) 60 (6): 711–8. DOI:10.1111/j.1365-2265.2004.02040.x. PMID 15163335. 
  • Takeshita A, Nagayama Y, Fujiyama K, et al. (1992). „Molecular cloning and sequencing of an alternatively spliced form of the human thyrotropin receptor transcript.”. Biochem. Biophys. Res. Commun. 188 (3): 1214–9. DOI:10.1016/0006-291X(92)91360-3. PMID 1445355. 
  • Graves PN, Tomer Y, Davies TF (1992). „Cloning and sequencing of a 1.3 KB variant of human thyrotropin receptor mRNA lacking the transmembrane domain.”. Biochem. Biophys. Res. Commun. 187 (2): 1135–43. DOI:10.1016/0006-291X(92)91315-H. PMID 1530609. 
  • Loosfelt H, Pichon C, Jolivet A, et al. (1992). „Two-subunit structure of the human thyrotropin receptor.”. Proc. Natl. Acad. Sci. U.S.A. 89 (9): 3765–9. DOI:10.1073/pnas.89.9.3765. PMC 525571. PMID 1570295. 
  • Nagayama Y, Russo D, Wadsworth HL, et al. (1991). „Eleven amino acids (Lys-201 to Lys-211) and 9 amino acids (Gly-222 to Leu-230) in the human thyrotropin receptor are involved in ligand binding.”. J. Biol. Chem. 266 (23): 14926–30. PMID 1651314. 
  • Murakami M, Mori M (1990). „Identification of immunogenic regions in human thyrotropin receptor for immunoglobulin G of patients with Graves' disease.”. Biochem. Biophys. Res. Commun. 171 (1): 512–8. DOI:10.1016/0006-291X(90)91423-P. PMID 1697467. 
  • Heldin NE, Gustavsson B, Westermark K, Westermark B (1992). „A somatic point mutation in a putative ligand binding domain of the TSH receptor in a patient with autoimmune hyperthyroidism.”. J. Clin. Endocrinol. Metab. 73 (6): 1374–6. DOI:10.1210/jcem-73-6-1374. PMID 1955520. 
  • Libert F, Passage E, Lefort A, et al. (1991). „Localization of human thyrotropin receptor gene to chromosome region 14q3 by in situ hybridization.”. Cytogenet. Cell Genet. 54 (1-2): 82–3. DOI:10.1159/000132964. PMID 2249482. 
  • Frazier AL, Robbins LS, Stork PJ, et al. (1991). „Isolation of TSH and LH/CG receptor cDNAs from human thyroid: regulation by tissue specific splicing.”. Mol. Endocrinol. 4 (8): 1264–76. DOI:10.1210/mend-4-8-1264. PMID 2293030. 
  • Misrahi M, Loosfelt H, Atger M, et al. (1990). „Cloning, sequencing and expression of human TSH receptor.”. Biochem. Biophys. Res. Commun. 166 (1): 394–403. DOI:10.1016/0006-291X(90)91958-U. PMID 2302212. 
  • Nagayama Y, Kaufman KD, Seto P, Rapoport B (1990). „Molecular cloning, sequence and functional expression of the cDNA for the human thyrotropin receptor.”. Biochem. Biophys. Res. Commun. 165 (3): 1184–90. DOI:10.1016/0006-291X(89)92727-7. PMID 2558651. 
  • Libert F, Lefort A, Gerard C, et al. (1990). „Cloning, sequencing and expression of the human thyrotropin (TSH) receptor: evidence for binding of autoantibodies.”. Biochem. Biophys. Res. Commun. 165 (3): 1250–5. DOI:10.1016/0006-291X(89)92736-8. PMID 2610690. 
  • Cuddihy RM, Bryant WP, Bahn RS (1996). „Normal function in vivo of a homozygotic polymorphism in the human thyrotropin receptor.”. Thyroid 5 (4): 255–7. DOI:10.1089/thy.1995.5.255. PMID 7488864. 
  • Bahn RS, Dutton CM, Heufelder AE, Sarkar G (1994). „A genomic point mutation in the extracellular domain of the thyrotropin receptor in patients with Graves' ophthalmopathy.”. J. Clin. Endocrinol. Metab. 78 (2): 256–60. DOI:10.1210/jc.78.2.256. PMID 7508946. 
  • Sunthornthepvarakui T, Gottschalk ME, Hayashi Y, Refetoff S (1995). „Brief report: resistance to thyrotropin caused by mutations in the thyrotropin-receptor gene.”. N. Engl. J. Med. 332 (3): 155–60. DOI:10.1056/NEJM199501193320305. PMID 7528344. 

Spoljašnje veze

  • „Glycoprotein Hormone Receptors: TSH”. IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. Arhivirano iz originala na datum 2013-11-01. 
  • MeSH Thyrotropin+Receptors
  • GRIS Arhivirano 2006-10-16 na Wayback Machine-u
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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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Neuropeptidni receptori
Hormonski receptori
Drugi
Opioidni receptori
Drugi neuropeptidni receptori
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)