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Volumn 24, Issue 1, 1999, Pages 37-42

Inactivation of the purified bovine μ opioid receptor by sulfhydryl reagents

Author keywords

Cysteine; Purified opioid receptor; Sulfhydryl reagent

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); BREMAZOCINE; ENKEPHALIN[2 DEXTRO ALANINE 4 METHYLPHENYLALANINE 5 GLYCINE]; METHYLAMINE; MU OPIATE RECEPTOR; NALOXONE; THIOL REAGENT;

EID: 0032926537     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020923928936     Document Type: Article
Times cited : (3)

References (29)
  • 1
    • 0029102878 scopus 로고
    • Molecular biology of the opioid receptors: Structure, functions, and distributions
    • Minami, M. and Satoh, M. 1995. Molecular biology of the opioid receptors: structure, functions, and distributions. Neuroscience Research 23:121-45.
    • (1995) Neuroscience Research , vol.23 , pp. 121-145
    • Minami, M.1    Satoh, M.2
  • 3
    • 0029017044 scopus 로고
    • A chimeric study of the molecular basis of affinity and selectivity of the κ and δ opioid receptors potential role of extracellular domains
    • Meng, F., Hoversten, M. T., Thompson, R. C., Taylor, L., Watson, S. J., and Akil, H. 1995. A chimeric study of the molecular basis of affinity and selectivity of the κ and δ opioid receptors potential role of extracellular domains. J. Biol. Chem. 270:12730-2736.
    • (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
  • 4
    • 0028170438 scopus 로고
    • Mu opiate receptor: Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity
    • Surratt, C. K., Johnson, P. S., Moriwaki, A., Seidleck, B. K., Blaschak, C. J., Wang, J. B., and Uhl, G. R. 1994. Mu opiate receptor: charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity. J. Biol. Chem. 269: 20548-0553.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20548-20553
    • Surratt, C.K.1    Johnson, P.S.2    Moriwaki, A.3    Seidleck, B.K.4    Blaschak, C.J.5    Wang, J.B.6    Uhl, G.R.7
  • 5
    • 0030040907 scopus 로고    scopus 로고
    • The conserved aspartate residue in the third putative transmembrane domain of the 6 opioid receptor is not the anionic counterpart for cationic opiate binding but is a constituent of the receptor binding site
    • Befort, K., Tabbara, L., Bausch, S., Chavkin, C., Evans, C. J., and Kieffer, B. L. 1996. The conserved aspartate residue in the third putative transmembrane domain of the 6 opioid receptor is not the anionic counterpart for cationic opiate binding but is a constituent of the receptor binding site. Mol. Pharmacol. 49:216-23.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 216-223
    • Befort, K.1    Tabbara, L.2    Bausch, S.3    Chavkin, C.4    Evans, C.J.5    Kieffer, B.L.6
  • 6
    • 0029586680 scopus 로고
    • Studies on μ and δ opioid receptor selectivity utilizing chimeric and site-mutagenized receptors
    • Wang, W. W., Shahrestanifar, Jin, J., and Howells, R. D. 1995. Studies on μ and δ opioid receptor selectivity utilizing chimeric and site-mutagenized receptors. Proc. Natl. Acad. Sci. 92:12436-12440.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 12436-12440
    • Wang, W.W.1    Shahrestanifar2    Jin, J.3    Howells, R.D.4
  • 7
    • 0027444691 scopus 로고
    • A single residue, aspartic acid 95, in the delta opioid receptor specifies selective high affinity agonist binding
    • Kong, H., Raynor, K., Yasuda, K., Moe, S. T., Portoghese, P. S., Bell, G. I., and Reisine, T. 1993. A single residue, aspartic acid 95, in the delta opioid receptor specifies selective high affinity agonist binding. J. Biol. Chem. 268:23055-3058.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23055-23058
    • Kong, H.1    Raynor, K.2    Yasuda, K.3    Moe, S.T.4    Portoghese, P.S.5    Bell, G.I.6    Reisine, T.7
  • 10
    • 0016822591 scopus 로고
    • Differential effects of protein-modifying reagents on receptor binding of opiate agonists and antagonists
    • Pasternak, G. W., Wilson, H. A., and Snyder, S. H. 1975. Differential effects of protein-modifying reagents on receptor binding of opiate agonists and antagonists. Mol. Pharmacol. 11:340-51.
    • (1975) Mol. Pharmacol. , vol.11 , pp. 340-351
    • Pasternak, G.W.1    Wilson, H.A.2    Snyder, S.H.3
  • 11
    • 0005507696 scopus 로고
    • Kinetics of opiate receptor inactivation by sulfhydryl reagents: Evidence for conformational change in presence of sodium ions
    • Simon, E. J., and Groth, J. 1975 Kinetics of opiate receptor inactivation by sulfhydryl reagents: evidence for conformational change in presence of sodium ions. Proc. Natl. Acad. Sci. USA 72:2404-407.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 2404-2407
    • Simon, E.J.1    Groth, J.2
  • 12
    • 0026878758 scopus 로고
    • Sulfhydryl groups on opioid receptors revisited: Evidence for two sulfhydryl groups at or near the active site of the mu opioid receptor
    • Ofri, D. and Simon, E. J. 1992. Sulfhydryl groups on opioid receptors revisited: Evidence for two sulfhydryl groups at or near the active site of the mu opioid receptor. Receptor 2:109-19.
    • (1992) Receptor , vol.2 , pp. 109-119
    • Ofri, D.1    Simon, E.J.2
  • 14
    • 0020663379 scopus 로고
    • Protection of opiate receptors in NG108-15 cells against modification by N-ethylmaleimide
    • Mulliken-Kilpatrick, D., Larsen, N. E., and Blume, J. J. 1983. Protection of opiate receptors in NG108-15 cells against modification by N-ethylmaleimide. J. Neurosci. 3:145-52.
    • (1983) J. Neurosci. , vol.3 , pp. 145-152
    • Mulliken-Kilpatrick, D.1    Larsen, N.E.2    Blume, J.J.3
  • 16
    • 0022366557 scopus 로고
    • Purification of an active opioid binding protein from bovine striatum
    • Gioannini, T. L., Howard, A. D., Hiller, J. M., and Simon, E. J. 1985. Purification of an active opioid binding protein from bovine striatum. J. Biol. Chem. 260:15117-15121.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15117-15121
    • Gioannini, T.L.1    Howard, A.D.2    Hiller, J.M.3    Simon, E.J.4
  • 17
    • 0028810707 scopus 로고
    • Functional reconstitution of a highly purified μ-opioid binding protein with purified G-proteins in liposomes
    • Fan, L.-Q., Gioannini, T. L., Wolinski, T., and Simon, E. J. 1995. Functional reconstitution of a highly purified μ-opioid binding protein with purified G-proteins in liposomes. J of Neurochem. 65:2537-542.
    • (1995) J of Neurochem. , vol.65 , pp. 2537-2542
    • Fan, L.-Q.1    Gioannini, T.L.2    Wolinski, T.3    Simon, E.J.4
  • 18
    • 0027218190 scopus 로고
    • Reconstitution of a purified mu-opioid binding protein in liposomes: Selective, high affinity, GTPγS-sensitive mu-opioid agonist binding is restored
    • Gioannini, T. L., Fan, L.-Q., Hyde, L., Ofri, D., Yao, Y. -H., Hiller, J. M., and Simon, E. J. 1993. Reconstitution of a purified mu-opioid binding protein in liposomes: Selective, high affinity, GTPγS-sensitive mu-opioid agonist binding is restored. Biochem. Biophys. Res. Comm. 194:901-908.
    • (1993) Biochem. Biophys. Res. Comm. , vol.194 , pp. 901-908
    • Gioannini, T.L.1    Fan, L.-Q.2    Hyde, L.3    Ofri, D.4    Yao, Y.H.5    Hiller, J.M.6    Simon, E.J.7
  • 19
    • 0344212122 scopus 로고
    • The modification of cysteine
    • CRC Press, Boca Raton, F1
    • Lundblad, R. L. 1995. The modification of cysteine. Pages 63-89, in Techniques in Protein Modification. CRC Press, Boca Raton, F1.
    • (1995) Techniques in Protein Modification , pp. 63-89
    • Lundblad, R.L.1
  • 20
    • 0026527094 scopus 로고
    • Characterization of CHAPS-solubilized opioid receptors: Reconstitution and uncoupling of guanine nucleotide-sensitive agonist binding
    • Ofri, D., Ritter, A. M., Liu, Y., Gioannini, T. L., Hiller, J. M., and Simon, E. J. 1992. Characterization of CHAPS-solubilized opioid receptors: Reconstitution and uncoupling of guanine nucleotide-sensitive agonist binding. J. Neurochem. 58:628-635.
    • (1992) J. Neurochem. , vol.58 , pp. 628-635
    • Ofri, D.1    Ritter, A.M.2    Liu, Y.3    Gioannini, T.L.4    Hiller, J.M.5    Simon, E.J.6
  • 21
    • 0029908852 scopus 로고    scopus 로고
    • Sensitivity of opioid receptor binding to N-substituted maleimides and methanethiosulfonate derivatives
    • Shahrestanifar, M. S. and Howells, R. D. 1996. Sensitivity of opioid receptor binding to N-substituted maleimides and methanethiosulfonate derivatives. Neurochem. Res. 21:1295-1299.
    • (1996) Neurochem. Res. , vol.21 , pp. 1295-1299
    • Shahrestanifar, M.S.1    Howells, R.D.2
  • 22
    • 0345074384 scopus 로고    scopus 로고
    • Cysteine residues in transmembrane domains of mu opiate receptor are involved in receptor binding
    • Abs
    • Deng, H. B. and Weng, J. B. 1996. Cysteine residues in transmembrane domains of mu opiate receptor are involved in receptor binding. Society for Neuroscience 22:1766 (Abs).
    • (1996) Society for Neuroscience , vol.22 , pp. 1766
    • Deng, H.B.1    Weng, J.B.2
  • 24
    • 0028355745 scopus 로고
    • The electrostatic potential of the acetylcholine binding sites in the nicotinic receptor probed by reactions of binding-site cysteines with charged methanethiosulfonates
    • Stauffer, D. A., and Karlin, A. 1994 The electrostatic potential of the acetylcholine binding sites in the nicotinic receptor probed by reactions of binding-site cysteines with charged methanethiosulfonates. Biochem. 33, 6840-6849.
    • (1994) Biochem. , vol.33 , pp. 6840-6849
    • Stauffer, D.A.1    Karlin, A.2
  • 25
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cyteine-substitution mutants
    • Akabas, M. H. Stauffer, D. A., Xu, M and Karlin, A. 1992. Acetylcholine receptor channel structure probed in cyteine-substitution mutants. Science 258:307-310.
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 26
    • 0027501362 scopus 로고
    • Amino acids lining the channel of the γ-aminobutyric acid type a receptor identified by cysteine substitution
    • Xu, M. and Akabas, M. H. 1993. Amino acids lining the channel of the γ-aminobutyric acid type A receptor identified by cysteine substitution. J. Biol. Chem. 268:21505-21508.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21505-21508
    • Xu, M.1    Akabas, M.H.2
  • 27
    • 0028264188 scopus 로고
    • Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator
    • Akabas, M. H., Kaufmann, C., Cook, T. A., and Archdeacon, P. 1994. Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 269: 14865-14868.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14865-14868
    • Akabas, M.H.1    Kaufmann, C.2    Cook, T.A.3    Archdeacon, P.4
  • 28
    • 0029863220 scopus 로고    scopus 로고
    • Studies on inhibition of μ and δ opioid receptor binding by dithiothreitol and N-ethyhnaleimide
    • Shahrestanifar, M., Wang, W. W. and Howells, R. D. 1996. Studies on inhibition of μ and δ opioid receptor binding by dithiothreitol and N-ethyhnaleimide. J. Biol. Chem. 271:5505-5512.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5505-5512
    • Shahrestanifar, M.1    Wang, W.W.2    Howells, R.D.3
  • 29
    • 0031009612 scopus 로고    scopus 로고
    • Identification in the μ-opioid receptor of cysteine residues responsible for inactivation of ligand binding by thiol alkylating and reducing agents
    • Giabelet, G., Capeyrou, R., Dietrich, G., and Emorine, L. J. 1997. Identification in the μ-opioid receptor of cysteine residues responsible for inactivation of ligand binding by thiol alkylating and reducing agents. FEBS Lett. 408:135-140.
    • (1997) FEBS Lett. , vol.408 , pp. 135-140
    • Giabelet, G.1    Capeyrou, R.2    Dietrich, G.3    Emorine, L.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.