메뉴 건너뛰기




Volumn 50, Issue 4, 1996, Pages 977-984

Radioligand-dependent discrepancy in agonist affinities enhanced by mutations in the κ-opioid receptor

Author keywords

[No Author keywords available]

Indexed keywords

DIPRENORPHINE; DYNORPHIN[1-8]; ENADOLINE; KAPPA OPIATE RECEPTOR; N METHYL N [7 (1 PYRROLIDINYL) 1 OXASPIRO[4.5]DEC 8 YL]BENZENEACETAMIDE; NORBINALTORPHIMINE; OPIATE AGONIST; OPIATE ANTAGONIST; RADIOLIGAND;

EID: 0029959123     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (32)

References (39)
  • 2
    • 0027052952 scopus 로고
    • The δ-opioid receptor: Isolation of a cDNA by expression cloning and pharmacological characterization
    • Kieffer, B. L., K. Befort, C. Gaveriaux-Ruff, and C. G. Hirth. The δ-opioid receptor: isolation of a cDNA by expression cloning and pharmacological characterization. Proc. Natl. Acad. Sci. USA 89:12048-12052 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 12048-12052
    • Kieffer, B.L.1    Befort, K.2    Gaveriaux-Ruff, C.3    Hirth, C.G.4
  • 4
    • 0027380497 scopus 로고
    • Molecular biology of opioid receptors
    • Reisine, T., and G. I. Bell. Molecular biology of opioid receptors. Trends Neurosci. 16:506-510 (1993).
    • (1993) Trends Neurosci. , vol.16 , pp. 506-510
    • Reisine, T.1    Bell, G.I.2
  • 5
    • 10244246769 scopus 로고
    • Opioids
    • (A. Herz, ed.). Springer-Verlag, NY
    • Archer, S. Opioids, in Handbook of Experimental Therapeutics (A. Herz, ed.). Vol. 104/I. Springer-Verlag, NY, 241-277 (1993).
    • (1993) Handbook of Experimental Therapeutics , vol.104 , Issue.1 , pp. 241-277
    • Archer, S.1
  • 6
    • 0028275934 scopus 로고
    • Structure-activity relationship of N17′-substituted norbinaltorphimine congeners: Role of the N17′ basic group in the interaction with aputative address subsite on the κ-opioid receptor
    • Portoghese, P. S., C.-E. Lin, F. Farouz-Grant, and A. E. Takemori. Structure-activity relationship of N17′-substituted norbinaltorphimine congeners: role of the N17′ basic group in the interaction with aputative address subsite on the κ-opioid receptor. J. Med. Chem. 37:1495-1500 (1994).
    • (1994) J. Med. Chem. , vol.37 , pp. 1495-1500
    • Portoghese, P.S.1    Lin, C.-E.2    Farouz-Grant, F.3    Takemori, A.E.4
  • 7
    • 0023812719 scopus 로고
    • Norbinaltorphimine, a highly selective kappa-opioid antagonist in analgesic and receptor binding assays
    • Takemori, A. E., B. Y. Ho, J. S. Naeseth, and P. S. Portoghese. Norbinaltorphimine, a highly selective kappa-opioid antagonist in analgesic and receptor binding assays. J. Pharmacol. Exp. Ther. 24:255-258 (1988).
    • (1988) J. Pharmacol. Exp. Ther. , vol.24 , pp. 255-258
    • Takemori, A.E.1    Ho, B.Y.2    Naeseth, J.S.3    Portoghese, P.S.4
  • 10
    • 0002726864 scopus 로고
    • 3H]-CI-977: A highly selective ligand for the κ-opioid receptor in both guinea-pig and rat forebrain
    • 3H]-CI-977: a highly selective ligand for the κ-opioid receptor in both guinea-pig and rat forebrain. Mol. Neuropharm. 1:23-29 (1990).
    • (1990) Mol. Neuropharm. , vol.1 , pp. 23-29
    • Boyle, S.J.1    Meecham, K.G.2    Hunter, J.C.3    Hughes, J.4
  • 12
    • 0028143479 scopus 로고
    • Human K opiate receptor second extracellular loop elevates dynorphins affinity for human μ/κ chimeras
    • Wang, J. B., P. S. Johnson, J. M. Wu, W. F. Wang, and G. R. UhI. Human K opiate receptor second extracellular loop elevates dynorphins affinity for human μ/κ chimeras. J. Biol. Chem. 269:25966-25969 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 25966-25969
    • Wang, J.B.1    Johnson, P.S.2    Wu, J.M.3    Wang, W.F.4    Uhi, G.R.5
  • 13
    • 0027932239 scopus 로고
    • Agonists and antagonists bind to different domains of the cloned κ-opioid receptor
    • Kong, H., K. Raynor, H. Yano, J. Takeda, G. I. Bell, and T. Reisine. Agonists and antagonists bind to different domains of the cloned κ-opioid receptor. Proc. Natl. Acad. Sci. USA 91:8042-8046 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8042-8046
    • Kong, H.1    Raynor, K.2    Yano, H.3    Takeda, J.4    Bell, G.I.5    Reisine, T.6
  • 14
    • 0028104682 scopus 로고
    • Differential binding domains of peptide and non-peptide ligands in the cloned rat κ opioid receptor
    • Xue, J.-C., C. Chen, J. Zhu, S. Kunapuli, J. K. DeRiel, L. Yu, and L.-Y. Liu-Chen. Differential binding domains of peptide and non-peptide ligands in the cloned rat κ opioid receptor. J. Biol. Chem. 269:30195-30199 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 30195-30199
    • Xue, J.-C.1    Chen, C.2    Zhu, J.3    Kunapuli, S.4    Deriel, J.K.5    Yu, L.6    Liu-Chen, L.-Y.7
  • 15
    • 0029013360 scopus 로고
    • Analysis of selective binding epitopes for the κ-opioid receptor antagonist norbinaltorphimine
    • Hjorth, S. A., K. Thirstrup, D. K. Grandy, and T. W. Schwartz. Analysis of selective binding epitopes for the κ-opioid receptor antagonist norbinaltorphimine. Mol. Pharmacol. 47:1089-1094 (1995).
    • (1995) Mol. Pharmacol. , vol.47 , pp. 1089-1094
    • Hjorth, S.A.1    Thirstrup, K.2    Grandy, D.K.3    Schwartz, T.W.4
  • 16
    • 0029045917 scopus 로고
    • The third extracellular loop of the μ opioid receptor is important for agonist selectivity
    • Xue, J.-C., C. Chen, J. Zhu, S. P. Kunapuli, K. Riel, L. Yu, and L.-Y. Liu-Chen. The third extracellular loop of the μ opioid receptor is important for agonist selectivity. J. Biol. Chem. 270:12977-12979 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 12977-12979
    • Xue, J.-C.1    Chen, C.2    Zhu, J.3    Kunapuli, S.P.4    Riel, K.5    Yu, L.6    Liu-Chen, L.-Y.7
  • 17
    • 0028934926 scopus 로고
    • Location of regions of the opioid receptor involved in selective agonist binding
    • Fukuda, K., S. Kato, and K. Mori. Location of regions of the opioid receptor involved in selective agonist binding. J. Biol. Chem. 270:6702-6709 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 6702-6709
    • Fukuda, K.1    Kato, S.2    Mori, K.3
  • 18
    • 0029017044 scopus 로고
    • A chimeric study of the molecular basis of affinity and selectivity of the K and the μ opioid receptors
    • Meng, F., M. T. Hoversten, R. C. Thompson, L. Taylor, S. J. Watson, and H. Akil. A chimeric study of the molecular basis of affinity and selectivity of the K and the μ opioid receptors. J. Biol. Chem. 270:12730-12736 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 12730-12736
    • Meng, F.1    Hoversten, M.T.2    Thompson, R.C.3    Taylor, L.4    Watson, S.J.5    Akil, H.6
  • 19
    • 0028978424 scopus 로고
    • DAMGO, a μ-opioid receptor selective agonist, distinguishes between μ- And δ-opioid receptors around their first extracellular loops
    • Onogi, T., M. Minami, Y. Katao, T. Nakagawa, Y. Aoki, T. Toya, S. Katsumata, and M. Satoh. DAMGO, a μ-opioid receptor selective agonist, distinguishes between μ- and δ-opioid receptors around their first extracellular loops. FEBS Lett. 357:93-97 (1995).
    • (1995) FEBS Lett. , vol.357 , pp. 93-97
    • Onogi, T.1    Minami, M.2    Katao, Y.3    Nakagawa, T.4    Aoki, Y.5    Toya, T.6    Katsumata, S.7    Satoh, M.8
  • 20
    • 11944268922 scopus 로고
    • Molecular mechanism of action of non-peptide ligands for peptide receptors
    • Schwartz, T. W., U. Gether, H. T. Shambye, and S. A. Hjorth. Molecular mechanism of action of non-peptide ligands for peptide receptors. Curr. Pharm. Design 1:325-342 (1995).
    • (1995) Curr. Pharm. Design , vol.1 , pp. 325-342
    • Schwartz, T.W.1    Gether, U.2    Shambye, H.T.3    Hjorth, S.A.4
  • 22
    • 0028076832 scopus 로고
    • Specific residues at the top pf transmembrane segments V and VI of the neurokinin-1 receptor involved in binding of the nonpeptide antagonist CP96,345
    • Gether, U, L. Nilsson, J. A. Lowe III, and T. W. Schwartz. Specific residues at the top pf transmembrane segments V and VI of the neurokinin-1 receptor involved in binding of the nonpeptide antagonist CP96,345. J. Biol. Chem. 269:23959-23964 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 23959-23964
    • Gether, U.1    Nilsson, L.2    Lowe III, J.A.3    Schwartz, T.W.4
  • 23
    • 0027988149 scopus 로고
    • Identification of peptide binding residues in the extracellular domains of the ATI receptor
    • Hjorth, S. A., H. T. Schambye, W. J. Greenlee, and T. W. Schwartz. Identification of peptide binding residues in the extracellular domains of the ATI receptor. J. Biol. Chem. 269:30953-30959 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 30953-30959
    • Hjorth, S.A.1    Schambye, H.T.2    Greenlee, W.J.3    Schwartz, T.W.4
  • 24
    • 0028235782 scopus 로고
    • Differentiation between binding sites for angiotensin II and nonpeptide antagonists on the angiotensin type 1 receptors. Proc
    • Schambye, H. T., S. A. Hjorth, D. J. Bergsma, G. Sathe, and T. W. Schwartz. Differentiation between binding sites for angiotensin II and nonpeptide antagonists on the angiotensin type 1 receptors. Proc. Natl. Acad. Sci. USA 91:7046-7050 (1994).
    • (1994) Natl. Acad. Sci. USA , vol.91 , pp. 7046-7050
    • Schambye, H.T.1    Hjorth, S.A.2    Bergsma, D.J.3    Sathe, G.4    Schwartz, T.W.5
  • 25
    • 0028043957 scopus 로고
    • Mutations along transmembrane segment II of the NK-1 receptor affect substance P competition with non-peptide antagonists but not substance P binding
    • Rosenkilde, M. M., M. Cahir, U. Gether, S. A. Hjorth, and T. W. Schwartz. Mutations along transmembrane segment II of the NK-1 receptor affect substance P competition with non-peptide antagonists but not substance P binding. J. Biol. Chem. 269:28160-28164 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 28160-28164
    • Rosenkilde, M.M.1    Cahir, M.2    Gether, U.3    Hjorth, S.A.4    Schwartz, T.W.5
  • 26
    • 0028293626 scopus 로고
    • Interaction of substance P with the second and seventh transmembrane domains of the neurokinin-1 receptor
    • Huang R. C., H. Yu, C. D. Strader, and T. M. Fong. Interaction of substance P with the second and seventh transmembrane domains of the neurokinin-1 receptor. Biochemistry 33:3007-3013 (1994).
    • (1994) Biochemistry , vol.33 , pp. 3007-3013
    • Huang, R.C.1    Yu, H.2    Strader, C.D.3    Fong, T.M.4
  • 27
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton, R. M., H. D. Hunt, S. N. Ho, J. K. Pullen, and L. R. Pease. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene (Amst.) 77:51-59 (1989).
    • (1989) Gene (Amst.) , vol.77 , pp. 51-59
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 28
    • 0027340010 scopus 로고
    • Chimeric NK1 (substance P)/NK3 (neurokinin B) receptors
    • Gether, U., T. E. Johansen, and T. W. Schwartz. Chimeric NK1 (substance P)/NK3 (neurokinin B) receptors. J. Biol. Chem. 268:7893-7898 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 7893-7898
    • Gether, U.1    Johansen, T.E.2    Schwartz, T.W.3
  • 29
    • 0027297275 scopus 로고
    • Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins
    • Lefkowitz, R. J., S. Cotecchia, P. Samama, and T. Costa. Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins. Trends Pharmacol. Sci. 14:303-307 (1993).
    • (1993) Trends Pharmacol. Sci. , vol.14 , pp. 303-307
    • Lefkowitz, R.J.1    Cotecchia, S.2    Samama, P.3    Costa, T.4
  • 30
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the β2-adrenergic receptor
    • Samama, P., S. Cotecchia, T. Costa, and R. J. Lefkowitz. A mutation-induced activated state of the β2-adrenergic receptor. J. Biol. Chem. 268: 4625-4636 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 31
    • 0029061611 scopus 로고
    • Agonist-receptor efficacy. I. Mechanisms of efficacy and receptor promiscuity
    • Kenakin, T. Agonist-receptor efficacy. I. Mechanisms of efficacy and receptor promiscuity. Trends Pharmacol. Sci. 16:188-192 (1995).
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 188-192
    • Kenakin, T.1
  • 33
  • 34
    • 0344584211 scopus 로고
    • Reciprocal modulation of agonist and antagonist binding to muscarinic cholinergic receptor by guanine nucleotides
    • Burgisser, E., A. De Lean, and R. J. Lefkowitz. Reciprocal modulation of agonist and antagonist binding to muscarinic cholinergic receptor by guanine nucleotides. Proc. Natl. Acad. Sci. USA 79:1732-1736 (1982).
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 1732-1736
    • Burgisser, E.1    De Lean, A.2    Lefkowitz, R.J.3
  • 35
    • 0019940309 scopus 로고
    • Dopamine receptor of the porcine anterior pituitary gland: Evidence for two affinity states discriminated by both agonists and antagonists
    • De Lean, A., B. F. Kilpatrick, and M. G. Caron. Dopamine receptor of the porcine anterior pituitary gland: evidence for two affinity states discriminated by both agonists and antagonists. Mol. Pharmacol. 22:290-297 (1982).
    • (1982) Mol. Pharmacol. , vol.22 , pp. 290-297
    • De Lean, A.1    Kilpatrick, B.F.2    Caron, M.G.3
  • 38
    • 0020321751 scopus 로고
    • Differential regulation of the μ-, δ-, and κ-opiate receptor subtypes by guanyl nucleotides and metal ions
    • Pfeiffer, A., W. Sadée, and A. Herz. Differential regulation of the μ-, δ-, and κ-opiate receptor subtypes by guanyl nucleotides and metal ions. J. Neurosci. 2:912-917 (1982).
    • (1982) J. Neurosci. , vol.2 , pp. 912-917
    • Pfeiffer, A.1    Sadée, W.2    Herz, A.3
  • 39
    • 0026498187 scopus 로고
    • Guanine nucleotide-binding protein-coupled and -uncoupled states of opioid receptors and their relevance to the determination of subtypes
    • Richardson, A., C. Demoliou-Mason, and E. A. Barnard. Guanine nucleotide-binding protein-coupled and -uncoupled states of opioid receptors and their relevance to the determination of subtypes. Proc. Natl. Acad. Sci. USA 89:10198-10202 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10198-10202
    • Richardson, A.1    Demoliou-Mason, C.2    Barnard, E.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.