메뉴 건너뛰기




Volumn 24, Issue 2, 2010, Pages 423-435

Plasma membrane expression of gonadotropin-releasing hormone receptors: Regulation by peptide and nonpeptide antagonists

Author keywords

[No Author keywords available]

Indexed keywords

[2 [5 [2 (2 AXABICYCLO[2.2.2]OCT 2 YL) 1,1 DIMETHYL 2 OXOETHYL] 2 (3,5 DIMETHYLPHENYL) 1H INDOL 3 YL] N (2 PYRIDIN 4 YLETHYL)PROPAN 1 AMINE]; BUSERELIN; CETRORELIX; G PROTEIN COUPLED RECEPTOR; GONADORELIN; GONADORELIN ANTAGONIST; GONADORELIN RECEPTOR; HEMAGGLUTININ; ITURELIX; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG;

EID: 75149152956     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2009-0343     Document Type: Article
Times cited : (17)

References (40)
  • 1
    • 0023065848 scopus 로고
    • The molecular mechanism of action of gonadotropin releasing hormone (GnRH) in the pituitary
    • Conn PM, Huckle WR, Andrews WV, McArdle CA 1987 The molecular mechanism of action of gonadotropin releasing hormone (GnRH) in the pituitary. Recent Prog Horm Res 43:29-68
    • (1987) Recent Prog Horm Res , vol.43 , pp. 29-68
    • Conn, P.M.1    Huckle, W.R.2    Andrews, W.V.3    McArdle, C.A.4
  • 2
    • 0029183393 scopus 로고
    • Expression and signal transduction pathways of gonadotropin-releasing hormone receptors
    • Stojilkovic SS, Catt KJ 1995 Expression and signal transduction pathways of gonadotropin-releasing hormone receptors. Recent Prog Horm Res 50:161-205
    • (1995) Recent Prog Horm Res , vol.50 , pp. 161-205
    • Stojilkovic, S.S.1    Catt, K.J.2
  • 4
    • 17044397637 scopus 로고    scopus 로고
    • Molecular biology of gonadotropin- releasing hormone (GnRH)-I, GnRH-II, and their receptors in humans
    • Cheng CK, Leung PC 2005 Molecular biology of gonadotropin- releasing hormone (GnRH)-I, GnRH-II, and their receptors in humans. Endocr Rev 26:283-306
    • (2005) Endocr Rev , vol.26 , pp. 283-306
    • Cheng, C.K.1    Leung, P.C.2
  • 5
    • 24044509155 scopus 로고    scopus 로고
    • Pituitary gonadotropin-releasing hormone receptor: Structure, distribution and regulation of expression
    • Rispoli LA, Nett TM 2005 Pituitary gonadotropin-releasing hormone receptor: structure, distribution and regulation of expression. Anim Reprod Sci 88:57-74
    • (2005) Anim Reprod Sci , vol.88 , pp. 57-74
    • Rispoli, L.A.1    Nett, T.M.2
  • 7
    • 0036473397 scopus 로고    scopus 로고
    • The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals
    • Luttrell LM, Lefkowitz RJ 2002 The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals. J Cell Sci 115:455-465
    • (2002) J Cell Sci , vol.115 , pp. 455-465
    • Luttrell, L.M.1    Lefkowitz, R.J.2
  • 8
    • 0028242680 scopus 로고
    • Absence of rapid desensitization of the mouse gonadotropin-releasing hormone receptor
    • Davidson JS, Wakefield IK, Millar RP 1994 Absence of rapid desensitization of the mouse gonadotropin-releasing hormone receptor. Biochem J 300:299-302
    • (1994) Biochem J , vol.300 , pp. 299-302
    • Davidson, J.S.1    Wakefield, I.K.2    Millar, R.P.3
  • 9
    • 0028862330 scopus 로고
    • Desensitization of gonadotropin-releasing hormone action in the gonadotrope-derived α T3-1 cell line
    • McArdle CA, Forrest-Owen W, Willars G, Davidson J, Poch A, Kratzmeier M 1995 Desensitization of gonadotropin-releasing hormone action in the gonadotrope-derived α T3-1 cell line. Endocrinology 136:4864-4871
    • (1995) Endocrinology , vol.136 , pp. 4864-4871
    • McArdle, C.A.1    Forrest-Owen, W.2    Willars, G.3    Davidson, J.4    Poch, A.5    Kratzmeier, M.6
  • 11
    • 0032496280 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone receptors with intracellular carboxyl-terminal tails undergo acute desensitization of total inositol phosphate production and exhibit accelerated internalization kinetics
    • Heding A, Vrecl M, Bogerd J, McGregor A, Sellar R, Taylor PL, Eidne KA 1998 Gonadotropin-releasing hormone receptors with intracellular carboxyl-terminal tails undergo acute desensitization of total inositol phosphate production and exhibit accelerated internalization kinetics. J Biol Chem 273:11472-11477
    • (1998) J Biol Chem , vol.273 , pp. 11472-11477
    • Heding, A.1    Vrecl, M.2    Bogerd, J.3    McGregor, A.4    Sellar, R.5    Taylor, P.L.6    Eidne, K.A.7
  • 12
    • 0036241442 scopus 로고    scopus 로고
    • Signaling, cycling and desensitization of gonadotrophin-releasing hormone receptors
    • McArdle CA, Franklin J, Green L, Hislop JN 2002 Signaling, cycling and desensitization of gonadotrophin-releasing hormone receptors. J Endocrinol 173:1-11
    • (2002) J Endocrinol , vol.173 , pp. 1-11
    • McArdle, C.A.1    Franklin, J.2    Green, L.3    Hislop, J.N.4
  • 13
    • 0035955742 scopus 로고    scopus 로고
    • Differential internalization of mammalian and non-mammalian gonadotropin-releasing hormone receptors. Uncoupling of dynamin-dependent internalization from mitogen-activated protein kinase signaling
    • Hislop JN, Everest HM, Flynn A, Harding T, Uney JB, Troskie BE, Millar RP, McArdle CA 2001 Differential internalization of mammalian and non-mammalian gonadotropin-releasing hormone receptors. Uncoupling of dynamin-dependent internalization from mitogen-activated protein kinase signaling. J Biol Chem 276:39685-39694
    • (2001) J Biol Chem , vol.276 , pp. 39685-39694
    • Hislop, J.N.1    Everest, H.M.2    Flynn, A.3    Harding, T.4    Uney, J.B.5    Troskie, B.E.6    Millar, R.P.7    McArdle, C.A.8
  • 14
    • 7244253015 scopus 로고    scopus 로고
    • Pharmacologic rescue of conformationally-defective proteins: Implications for the treatment of human disease
    • Ulloa-Aguirre A, Janovick JA, Brothers SP, Conn PM 2004 Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease. Traffic 5:821-837
    • (2004) Traffic , vol.5 , pp. 821-837
    • Ulloa-Aguirre, A.1    Janovick, J.A.2    Brothers, S.P.3    Conn, P.M.4
  • 15
    • 34748871331 scopus 로고    scopus 로고
    • G protein-coupled receptor trafficking in health and disease: Lessons learned to prepare for therapeutic mutant rescue in vivo
    • Conn PM, Ulloa-Aguirre A, Ito J, Janovick JA 2007 G protein-coupled receptor trafficking in health and disease: lessons learned to prepare for therapeutic mutant rescue in vivo. Pharmacol Rev 59:225-250
    • (2007) Pharmacol Rev , vol.59 , pp. 225-250
    • Conn, P.M.1    Ulloa-Aguirre, A.2    Ito, J.3    Janovick, J.A.4
  • 16
    • 0028832084 scopus 로고
    • Identification of N-glycosylation sites in the gonadotropin-releasing hormone receptor: Role in receptor expression but not ligand binding
    • Davidson JS, Flanagan CA, Zhou W, Becker II, Elario R, Emeran W, Sealfon SC, Millar RP 1995 Identification of N-glycosylation sites in the gonadotropin-releasing hormone receptor: role in receptor expression but not ligand binding. Mol Cell Endocrinol 107:241-245
    • (1995) Mol Cell Endocrinol , vol.107 , pp. 241-245
    • Davidson, J.S.1    Flanagan, C.A.2    Zhou, W.3    Becker, I.I.4    Elario, R.5    Emeran, W.6    Sealfon, S.C.7    Millar, R.P.8
  • 17
    • 0032230140 scopus 로고    scopus 로고
    • Addition of catfish gonadotropin-releasing hormone (GnRH) receptor intracellular carboxyl-terminal tail to rat GnRH receptor alters receptor expression and regulation
    • Lin X, Janovick JA, Brothers S, Blömenrohr M, Bogerd J, Conn PM 1998 Addition of catfish gonadotropin-releasing hormone (GnRH) receptor intracellular carboxyl-terminal tail to rat GnRH receptor alters receptor expression and regulation. Mol Endocrinol 12:161-171
    • (1998) Mol Endocrinol , vol.12 , pp. 161-171
    • Lin, X.1    Janovick, J.A.2    Brothers, S.3    Blömenrohr, M.4    Bogerd, J.5    Conn, P.M.6
  • 18
    • 0345045562 scopus 로고    scopus 로고
    • Pivotal role for the cytoplasmic carboxyl-terminal tail of a nonmammalian gonadotropin-releasing hormone receptor in cell surface expression, ligand binding, and receptor phosphorylation and internalization
    • Blomenröhr M, Heding A, Sellar R, Leurs R, Bogerd J, Eidne KA, Willars GB 1999 Pivotal role for the cytoplasmic carboxyl-terminal tail of a nonmammalian gonadotropin-releasing hormone receptor in cell surface expression, ligand binding, and receptor phosphorylation and internalization. Mol Pharmacol 56:1229-1237
    • (1999) Mol Pharmacol , vol.56 , pp. 1229-1237
    • Blomenröhr, M.1    Heding, A.2    Sellar, R.3    Leurs, R.4    Bogerd, J.5    Eidne, K.A.6    Willars, G.B.7
  • 19
    • 0031936827 scopus 로고    scopus 로고
    • Contrasting internalization kinetics of human and chicken gonadotropin-releasing hormone receptors mediated by C-terminal tail
    • Pawson AJ, Katz A, Sun YM, Lopes J, Illing N, Millar RP, Davidson JS 1998 Contrasting internalization kinetics of human and chicken gonadotropin-releasing hormone receptors mediated by C-terminal tail. J Endocrinol 156:R9-R12
    • (1998) J Endocrinol , vol.156
    • Pawson, A.J.1    Katz, A.2    Sun, Y.M.3    Lopes, J.4    Illing, N.5    Millar, R.P.6    Davidson, J.S.7
  • 21
    • 3042540232 scopus 로고    scopus 로고
    • Pharmacological chaperones: Potential treatment for conformational diseases
    • Bernier V, Lagacé M, Bichet DG, Bouvier M 2004 Pharmacological chaperones: potential treatment for conformational diseases. Trends Endocrinol Metab 15:222-228
    • (2004) Trends Endocrinol Metab , vol.15 , pp. 222-228
    • Bernier, V.1    Lagacé, M.2    Bichet, D.G.3    Bouvier, M.4
  • 22
    • 0034607918 scopus 로고    scopus 로고
    • Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human δ opioid receptor
    • Petaja-Repo UE, Hogue M, Laperriere A, Walker P, Bouvier M 2000 Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human δ opioid receptor. J Biol Chem 275:13727-13736
    • (2000) J Biol Chem , vol.275 , pp. 13727-13736
    • Petaja-Repo, U.E.1    Hogue, M.2    Laperriere, A.3    Walker, P.4    Bouvier, M.5
  • 23
    • 0037007201 scopus 로고    scopus 로고
    • Ligands act as pharmacological chaperones and increase the efficiency of δ opioid receptor maturation
    • Petäjä-Repo UE, Hogue M, Bhalla S, Laperrière A, Morello JP, Bouvier M 2002 Ligands act as pharmacological chaperones and increase the efficiency of δ opioid receptor maturation. EMBO J 21:1628-1637
    • (2002) EMBO J , vol.21 , pp. 1628-1637
    • Petäjä-Repo, U.E.1    Hogue, M.2    Bhalla, S.3    Laperrière, A.4    Morello, J.P.5    Bouvier, M.6
  • 25
    • 33750915929 scopus 로고    scopus 로고
    • Protein folding as posttranslational regulation: Evolution of a mechanism for controlled plasma membrane expression of a g protein-coupled receptor
    • Conn PM, Knollman PE, Brothers SP, Janovick JA 2006 Protein folding as posttranslational regulation: evolution of a mechanism for controlled plasma membrane expression of a g protein-coupled receptor. Mol Endocrinol 20:3035-3041
    • (2006) Mol Endocrinol , vol.20 , pp. 3035-3041
    • Conn, P.M.1    Knollman, P.E.2    Brothers, S.P.3    Janovick, J.A.4
  • 26
    • 33846785258 scopus 로고    scopus 로고
    • Intracellular gonadotropin-releasing hormone receptors in breast cancer and gonadotrope lineage cells
    • Sedgley KR, Finch AR, Caunt CJ, McArdle CA 2006 Intracellular gonadotropin-releasing hormone receptors in breast cancer and gonadotrope lineage cells. J Endocrinol 191:625-636
    • (2006) J Endocrinol , vol.191 , pp. 625-636
    • Sedgley, K.R.1    Finch, A.R.2    Caunt, C.J.3    McArdle, C.A.4
  • 27
    • 39749202910 scopus 로고    scopus 로고
    • Plasma membrane expression of GnRH receptors: Regulation by antagonists in breast, prostate, and gonadotrope cell lines
    • Finch AR, Sedgley KR, Caunt CJ, McArdle CA 2008 Plasma membrane expression of GnRH receptors: regulation by antagonists in breast, prostate, and gonadotrope cell lines. J Endocrinol 196:353-367
    • (2008) J Endocrinol , vol.196 , pp. 353-367
    • Finch, A.R.1    Sedgley, K.R.2    Caunt, C.J.3    McArdle, C.A.4
  • 28
    • 70349247756 scopus 로고    scopus 로고
    • Agonist-induced internalization and down-regulation of gonadotropin releasing hormone receptors
    • Finch AR, Caunt CJ, Armstrong SP, McArdle CA 2009 Agonist-induced internalization and down-regulation of gonadotropin releasing hormone receptors. Am J Physiol Cell Physiol 291:C591-C600
    • (2009) Am J Physiol Cell Physiol , vol.291
    • Finch, A.R.1    Caunt, C.J.2    Armstrong, S.P.3    McArdle, C.A.4
  • 29
    • 0032079392 scopus 로고    scopus 로고
    • Alanine-261 in intracellular loop III of the human gonadotropin-releasing hormone receptor is crucial for G-protein coupling and receptor internalization
    • Myburgh DB, Millar RP, Hapgood JP 1998 Alanine-261 in intracellular loop III of the human gonadotropin-releasing hormone receptor is crucial for G-protein coupling and receptor internalization. Biochem J 331:893-896
    • (1998) Biochem J , vol.331 , pp. 893-896
    • Myburgh, D.B.1    Millar, R.P.2    Hapgood, J.P.3
  • 30
    • 75149152791 scopus 로고    scopus 로고
    • NFAT proteins: Key regulators of T-cell development and function
    • Macian F 2005 NFAT proteins: key regulators of T-cell development and function. Nat Rev Immunol 84:488-499
    • (2005) Nat Rev Immunol , vol.84 , pp. 488-499
    • Macian, F.1
  • 31
    • 33746932103 scopus 로고    scopus 로고
    • Role of delivery and trafficking of δ-opioid peptide receptors in opioid analgesia and tolerance
    • Zhang X, Bao L, Guan JS 2006 Role of delivery and trafficking of δ-opioid peptide receptors in opioid analgesia and tolerance. Trends Pharmacol Sci 27:324-329
    • (2006) Trends Pharmacol Sci , vol.27 , pp. 324-329
    • Zhang, X.1    Bao, L.2    Guan, J.S.3
  • 32
    • 0032052309 scopus 로고    scopus 로고
    • Effects of LHRH analogues on mitogenic signal transduction in cancer cells
    • Emons G, Müller V, Ortmann O, Schulz KD 1998 Effects of LHRH analogues on mitogenic signal transduction in cancer cells. J Steroid Biochem Mol Biol 65:199-206
    • (1998) J Steroid Biochem Mol Biol , vol.65 , pp. 199-206
    • Emons, G.1    Müller, V.2    Ortmann, O.3    Schulz, K.D.4
  • 33
    • 0035182258 scopus 로고    scopus 로고
    • The actions of luteinizing hormone-releasing hormone agonists, antagonists and cytotoxic analogues on the luteinizing hormone-releasing hormone receptors on the pituitary and tumors
    • Schally AV, Halmos G, Rekasi Z, Arencibia-Jiminez JM 2001 The actions of luteinizing hormone-releasing hormone agonists, antagonists and cytotoxic analogues on the luteinizing hormone-releasing hormone receptors on the pituitary and tumors. Infertil Reprod Med Clin North Am 12:17-44
    • (2001) Infertil Reprod Med Clin North Am , vol.12 , pp. 17-44
    • Schally, A.V.1    Halmos, G.2    Rekasi, Z.3    Arencibia-Jiminez, J.M.4
  • 34
    • 0035430430 scopus 로고    scopus 로고
    • Applications for GnRH antagonists
    • Blithe DL 2001 Applications for GnRH antagonists. Trends Endocrinol Metab 12:238-240
    • (2001) Trends Endocrinol Metab , vol.12 , pp. 238-240
    • Blithe, D.L.1
  • 35
    • 44249086389 scopus 로고    scopus 로고
    • Amiloride derivatives and a nonpeptide antagonist bind at two distinct allosteric sites in the human gonadotropin-releasing hormone receptor
    • Heitman LH, Ye K, Oosterom J, Ijzerman AP 2008 Amiloride derivatives and a nonpeptide antagonist bind at two distinct allosteric sites in the human gonadotropin-releasing hormone receptor. Mol Pharmacol 73:1808-1815
    • (2008) Mol Pharmacol , vol.73 , pp. 1808-1815
    • Heitman, L.H.1    Ye, K.2    Oosterom, J.3    Ijzerman, A.P.4
  • 36
    • 45749121193 scopus 로고    scopus 로고
    • Non-peptide gonadotropin-releasing hormone receptor antagonists
    • Betz SF, Zhu YF, Chen C, Struthers RS 2008 Non-peptide gonadotropin-releasing hormone receptor antagonists. J Med Chem 26:3331-3348
    • (2008) J Med Chem , vol.26 , pp. 3331-3348
    • Betz, S.F.1    Zhu, Y.F.2    Chen, C.3    Struthers, R.S.4
  • 37
    • 34547176875 scopus 로고    scopus 로고
    • Trapping of a nonpeptide ligand by the extracellular domains of the gonadotropin-releasing hormone receptor results in insurmountable antagonism
    • Kohout TA, Xie Q, Reijmers S, Finn KJ, Guo Z, Zhu YF, Struthers RS 2007 Trapping of a nonpeptide ligand by the extracellular domains of the gonadotropin-releasing hormone receptor results in insurmountable antagonism. Mol Pharmacol 72:238-247
    • (2007) Mol Pharmacol , vol.72 , pp. 238-247
    • Kohout, T.A.1    Xie, Q.2    Reijmers, S.3    Finn, K.J.4    Guo, Z.5    Zhu, Y.F.6    Struthers, R.S.7
  • 38
    • 3843146128 scopus 로고    scopus 로고
    • Regulation of gonadotropin-releasing hormone receptors by protein kinase C: Inside out signaling and evidence for multiple active conformations
    • Caunt CJ, Hislop JN, Kelly E, Matharu AL, Green LD, Sedgley KR, Finch AR, McArdle CA 2004 Regulation of gonadotropin-releasing hormone receptors by protein kinase C: inside out signaling and evidence for multiple active conformations. Endocrinology 145:3594-3602
    • (2004) Endocrinology , vol.145 , pp. 3594-3602
    • Caunt, C.J.1    Hislop, J.N.2    Kelly, E.3    Matharu, A.L.4    Green, L.D.5    Sedgley, K.R.6    Finch, A.R.7    McArdle, C.A.8
  • 39
    • 5644247440 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone (GnRH) antagonists promote proapoptotic signaling in peripheral reproductive tumor cells by activating a Gαi-coupling state of the type I GnRH receptor
    • Maudsley S, Davidson L, Pawson AJ, Chan R, López de Maturana R, Millar RP 2004 Gonadotropin-releasing hormone (GnRH) antagonists promote proapoptotic signaling in peripheral reproductive tumor cells by activating a Gαi-coupling state of the type I GnRH receptor. Cancer Res 64:7533-7544
    • (2004) Cancer Res , vol.64 , pp. 7533-7544
    • Maudsley, S.1    Davidson, L.2    Pawson, A.J.3    Chan, R.4    López de Maturana, R.5    Millar, R.P.6
  • 40
    • 46349105039 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone analog structural determinants of selectivity for inhibition of cell growth: Support for the concept of ligand-induced selective signaling
    • López de Maturana R, Pawson AJ, Lu ZL, Davidson L, Maudsley S, Morgan K, Langdon SP, Millar RP 2008 Gonadotropin-releasing hormone analog structural determinants of selectivity for inhibition of cell growth: support for the concept of ligand-induced selective signaling. Mol Endocrinol 22:1711-1722
    • (2008) Mol Endocrinol , vol.22 , pp. 1711-1722
    • López de Maturana, R.1    Pawson, A.J.2    Lu, Z.L.3    Davidson, L.4    Maudsley, S.5    Morgan, K.6    Langdon, S.P.7    Millar, R.P.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.