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Volumn 75, Issue 1, 2000, Pages 164-173

Association of a lower molecular weight protein to the μ-opioid receptor demonstrated by 125I-β-endorphin cross-linking studies

Author keywords

Opioid receptor; 125I Endorphin; Cross linking

Indexed keywords

BETA ENDORPHIN; IODINE 125; MU OPIATE RECEPTOR;

EID: 0034045823     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2000.0750164.x     Document Type: Article
Times cited : (5)

References (47)
  • 4
    • 0032545499 scopus 로고    scopus 로고
    • Identification of serine 356 and serine 363 as the amino acids involved in etorphine-induced down-regulation of the μ-opioid receptor
    • Burd A. L., El-Kouhen R., Erickson L. J., Loh H. H., and Law P. Y. (1998) Identification of serine 356 and serine 363 as the amino acids involved in etorphine-induced down-regulation of the μ-opioid receptor. J. Biol. Chem. 273, 34488-34495.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34488-34495
    • Burd, A.L.1    El-Kouhen, R.2    Erickson, L.J.3    Loh, H.H.4    Law, P.Y.5
  • 5
    • 0033575916 scopus 로고    scopus 로고
    • A kinase-regulated PDZ-domain interaction controls endocytic sorting of the β2-adrenergic receptor
    • Cao T. T., Deacon H. W., Reczek D., Bretscher A., and von Zastrow M. (1999) A kinase-regulated PDZ-domain interaction controls endocytic sorting of the β2-adrenergic receptor. Nature 401, 286-290.
    • (1999) Nature , vol.401 , pp. 286-290
    • Cao, T.T.1    Deacon, H.W.2    Reczek, D.3    Bretscher, A.4    Von Zastrow, M.5
  • 6
    • 0028989522 scopus 로고
    • 2A cells stably expressing a cloned μ-opioid receptor: A specific cellular model to study acute and chronic effects of morphine
    • 2A cells stably expressing a cloned μ-opioid receptor: a specific cellular model to study acute and chronic effects of morphine. Mol. Brain Res. 30, 269-278.
    • (1995) Mol. Brain Res. , vol.30 , pp. 269-278
    • Chakrabarti, S.1    Law, P.Y.2    Loh, H.H.3
  • 8
    • 0023711798 scopus 로고
    • Calcium phosphate-mediated gene transfer: A highly efficient transfection system for stably transforming cells with plasmid DNA
    • Chen C. A. and Okayama H. (1988) Calcium phosphate-mediated gene transfer: a highly efficient transfection system for stably transforming cells with plasmid DNA. Biotechniques 6, 632-638.
    • (1988) Biotechniques , vol.6 , pp. 632-638
    • Chen, C.A.1    Okayama, H.2
  • 9
    • 0027503898 scopus 로고
    • Molecular cloning of a rat κ opioid receptor reveals sequence similarities to the μ and δ opioid receptors
    • Chen Y., Mestek A., Liu J., and Yu L. (1993) Molecular cloning of a rat κ opioid receptor reveals sequence similarities to the μ and δ opioid receptors. Biochem. J. 295, 625-628.
    • (1993) Biochem. J. , vol.295 , pp. 625-628
    • Chen, Y.1    Mestek, A.2    Liu, J.3    Yu, L.4
  • 11
    • 0030760634 scopus 로고    scopus 로고
    • Dimerization of the δ-opioid receptor: Implication for a role in receptor internalization
    • Cvejic S. and Devi L. A. (1997) Dimerization of the δ-opioid receptor: implication for a role in receptor internalization. J. Biol. Chem. 272, 26959-26964.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26959-26964
    • Cvejic, S.1    Devi, L.A.2
  • 12
    • 0033546146 scopus 로고    scopus 로고
    • Cloning and characterization of ATRAP, a novel protein that interacts with the angiotensin II type 1 receptor
    • Daviet L., Lehtonen J. Y. A., Tamura K., Griese D. P., Horiuchi M., and Dzau V. J. (1999) Cloning and characterization of ATRAP, a novel protein that interacts with the angiotensin II type 1 receptor. J. Biol. Chem. 274, 17058-17062.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17058-17062
    • Daviet, L.1    Lehtonen, J.Y.A.2    Tamura, K.3    Griese, D.P.4    Horiuchi, M.5    Dzau, V.J.6
  • 13
    • 0030593035 scopus 로고    scopus 로고
    • Role of β-arrestin in mediating agonist-promoted G protein-coupled receptor internalization
    • Ferguson S. S. G., Downey W. E. I., Colapietro A. M., Barak L. S., Ménard L., and Caron M. G. (1996) Role of β-arrestin in mediating agonist-promoted G protein-coupled receptor internalization. Science 271, 363-366.
    • (1996) Science , vol.271 , pp. 363-366
    • Ferguson, S.S.G.1    Downey, W.E.I.2    Colapietro, A.M.3    Barak, L.S.4    Ménard, L.5    Caron, M.G.6
  • 14
    • 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
  • 15
    • 0025084434 scopus 로고
    • Purification, cloning and tissue distribution of a 23 kDa rat protein isolated by morphine affinity chromatography
    • Grandy D. K., Hanneman E., Bunzow J., Shih M., Machida C. A., Bidlack J. M., and Civelli O. (1990) Purification, cloning and tissue distribution of a 23 kDa rat protein isolated by morphine affinity chromatography. Mol. Endocrinol. 4, 1370-1376.
    • (1990) Mol. Endocrinol. , vol.4 , pp. 1370-1376
    • Grandy, D.K.1    Hanneman, E.2    Bunzow, J.3    Shih, M.4    Machida, C.A.5    Bidlack, J.M.6    Civelli, O.7
  • 16
    • 0026793174 scopus 로고
    • Affinity cross-linked δ-opioid receptor in NG10815 cells is low molecular weight (22 kDa) and coupled to GTP-binding proteins
    • Harada J., Ueda H., Iso Y., and Satoh M. (1992) Affinity cross-linked δ-opioid receptor in NG10815 cells is low molecular weight (22 kDa) and coupled to GTP-binding proteins. Eur. J. Pharmacol. 227, 301-307.
    • (1992) Eur. J. Pharmacol. , vol.227 , pp. 301-307
    • Harada, J.1    Ueda, H.2    Iso, Y.3    Satoh, M.4
  • 17
    • 0022745441 scopus 로고
    • h-endorphin and its use for crosslinking of opioid binding sites in human striatum and NG108-15 neuroblastoma-glioma cells
    • h-endorphin and its use for crosslinking of opioid binding sites in human striatum and NG108-15 neuroblastoma-glioma cells. Proc. Natl. Acad. Sci. USA 83, 4622-4625.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4622-4625
    • Helmeste, D.M.1    Hammonds, R.G.J.2    Li, C.H.3
  • 18
    • 0026471991 scopus 로고
    • The 22 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS
    • Hess D. T., Slater T. M., Wilson M. C., and Skene J. H. P. (1992) The 22 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS. J. Neurosci. 12, 4634-4641.
    • (1992) J. Neurosci. , vol.12 , pp. 4634-4641
    • Hess, D.T.1    Slater, T.M.2    Wilson, M.C.3    Skene, J.H.P.4
  • 19
    • 0026833428 scopus 로고
    • Nicotinic receptor-associated 43 K protein and progressive stabilization of the postsynaptic membrane
    • Hill J. A. Jr. (1992) Nicotinic receptor-associated 43 K protein and progressive stabilization of the postsynaptic membrane. Mol. Neurobiol. 6, 1-17.
    • (1992) Mol. Neurobiol. , vol.6 , pp. 1-17
    • Hill J.A., Jr.1
  • 20
    • 0022195414 scopus 로고
    • Covalent labeling of opioid receptors with radioiodinated human β-endorphin
    • Howard A. D., de La Baume S., Gioannini T. L., Hiller J. M., and Simon E. J. (1985) Covalent labeling of opioid receptors with radioiodinated human β-endorphin. J. Biol. Chem. 260, 10833-10839.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10833-10839
    • Howard, A.D.1    De La Baume, S.2    Gioannini, T.L.3    Hiller, J.M.4    Simon, E.J.5
  • 22
    • 0021133317 scopus 로고
    • Solubilization and characterization of μ, δ, κ opioid binding sites from guinea pig brain: Physical separation of κ receptors
    • Itzhak Y., Hiller J. M., and Simon E. J. (1984) Solubilization and characterization of μ, δ, κ opioid binding sites from guinea pig brain: physical separation of κ receptors. Proc. Natl. Acad. Sci. USA 81, 4217-4221.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4217-4221
    • Itzhak, Y.1    Hiller, J.M.2    Simon, E.J.3
  • 23
    • 0029073041 scopus 로고
    • Histidine tagging both allows convenient single-step purification of bovine rhodopsin and exerts ionic strength-dependent effects on its photochemistry
    • Janssen J. J. M., Bovee-Geurts P. H. M., Merkx M., and DeGrip W. J. (1995) Histidine tagging both allows convenient single-step purification of bovine rhodopsin and exerts ionic strength-dependent effects on its photochemistry. J. Biol. Chem. 270, 11222-11229.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11222-11229
    • Janssen, J.J.M.1    Bovee-Geurts, P.H.M.2    Merkx, M.3    Degrip, W.J.4
  • 24
    • 0033578005 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimerization modulates receptor function
    • Jordan B. A. and Devi L. A. (1999) G-protein-coupled receptor heterodimerization modulates receptor function. Nature 399, 697-700.
    • (1999) Nature , vol.399 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 25
    • 0023819524 scopus 로고
    • 125l-labeled human β-endorphin to cell lines possessing either μ-or δ-type opioid binding sites
    • 125l-labeled human β-endorphin to cell lines possessing either μ-or δ-type opioid binding sites. Brain Res. 440, 280-284.
    • (1988) Brain Res. , vol.440 , pp. 280-284
    • Keren, O.1    Gioannini, T.L.2    Hiller, J.M.3    Simon, E.J.4
  • 26
    • 0029417155 scopus 로고
    • Recent advances in molecular recognition and signal transaction of active peptides: Receptors for opioid peptides
    • Kieffer B. L. (1995) Recent advances in molecular recognition and signal transaction of active peptides: receptors for opioid peptides. Cell. Mol. Neurobiol. 15, 615-635.
    • (1995) Cell. Mol. Neurobiol. , vol.15 , pp. 615-635
    • Kieffer, B.L.1
  • 27
    • 0028117163 scopus 로고
    • Cytokine signal transduction
    • Kishimoto T., Taga T., and Akira S. (1994) Cytokine signal transduction. Cell 76, 253-262.
    • (1994) Cell , vol.76 , pp. 253-262
    • Kishimoto, T.1    Taga, T.2    Akira, S.3
  • 28
    • 0026612529 scopus 로고
    • 125I-endorphin cross-linked proteins in NG108-15 cell membranes
    • 125I-endorphin cross-linked proteins in NG108-15 cell membranes. J. Biol. Chem. 267, 12722-12727.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12722-12727
    • Ko, J.L.1    Lee, N.M.2    Loh, H.H.3
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0020694935 scopus 로고
    • Opioid regulation of adenosine 3′:5′-cyclic monophosphate level in neuroblastoma × glioma NG108-15 hybrid cells
    • Law P. Y., Hom D. S., and Loh H. H. (1982) Opioid regulation of adenosine 3′:5′-cyclic monophosphate level in neuroblastoma × glioma NG108-15 hybrid cells. Mol. Pharmacol. 23, 26-35.
    • (1982) Mol. Pharmacol. , vol.23 , pp. 26-35
    • Law, P.Y.1    Hom, D.S.2    Loh, H.H.3
  • 31
    • 0031023556 scopus 로고    scopus 로고
    • Agonist activation of δ-opioid receptor but not μ-opioid receptor potentiates fetal calf serum or tyrosine kinase receptor-mediated cell proliferation in a cell-line specific manner
    • Law P. Y., McGinn T. M., Campbell K. M., Erickson L. E., and Loh H. H. (1997) Agonist activation of δ-opioid receptor but not μ-opioid receptor potentiates fetal calf serum or tyrosine kinase receptor-mediated cell proliferation in a cell-line specific manner. Mol. Pharmacol. 51, 152-160.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 152-160
    • Law, P.Y.1    McGinn, T.M.2    Campbell, K.M.3    Erickson, L.E.4    Loh, H.H.5
  • 32
    • 0025352299 scopus 로고
    • Arrestin: A protein that regulates β-adrenergic receptor function
    • Lohse M. J., Benovic J. L., Codina J., Caron M. G., and Lefkowitz R. J. (1990) Arrestin: a protein that regulates β-adrenergic receptor function. Science 248, 1547-1550.
    • (1990) Science , vol.248 , pp. 1547-1550
    • Lohse, M.J.1    Benovic, J.L.2    Codina, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 35
    • 0020609355 scopus 로고
    • Molecular size of opiate receptors in neuroblastoma-glioma hybrid cells as determined by radiation inactivation analysis
    • McLawhon R. W., Ellory J. C., and Dawson G. (1983) Molecular size of opiate receptors in neuroblastoma-glioma hybrid cells as determined by radiation inactivation analysis. J. Biol. Chem. 258, 2101-2105.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2101-2105
    • McLawhon, R.W.1    Ellory, J.C.2    Dawson, G.3
  • 36
    • 0029102878 scopus 로고
    • Molecular biology of the opioid receptors: Structures, functions and distributions
    • Minami M. and Satoh M. (1995) Molecular biology of the opioid receptors: structures, functions and distributions. Neurosci. Res. 23, 121-145.
    • (1995) Neurosci. Res. , vol.23 , pp. 121-145
    • Minami, M.1    Satoh, M.2
  • 37
    • 0019061918 scopus 로고
    • LIGAND: A versatile computerized approach for characterization of ligand-binding systems
    • Munson P. J. and Rodbard D. (1980) LIGAND: a versatile computerized approach for characterization of ligand-binding systems. Anal. Biochem. 107, 220-239.
    • (1980) Anal. Biochem. , vol.107 , pp. 220-239
    • Munson, P.J.1    Rodbard, D.2
  • 39
    • 0028169458 scopus 로고
    • Ability of δ-opioid receptors to interact with multiple G-proteins is independent of receptor density
    • Prather P. L., McGinn T. M., Erickson L. J., Evans C. J., Loh H. H., and Law P. Y. (1994) Ability of δ-opioid receptors to interact with multiple G-proteins is independent of receptor density. J. Biol. Chem. 269, 21293-21302.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21293-21302
    • Prather, P.L.1    McGinn, T.M.2    Erickson, L.J.3    Evans, C.J.4    Loh, H.H.5    Law, P.Y.6
  • 40
    • 0029867023 scopus 로고    scopus 로고
    • Regulating G protein signaling
    • Roush W. (1996) Regulating G protein signaling. Science 271, 1056-1058.
    • (1996) Science , vol.271 , pp. 1056-1058
    • Roush, W.1
  • 41
    • 0029123401 scopus 로고
    • From structure to function: Possible biological roles of a new widespread protein family binding hydrophobic ligands and displaying a nucleotide binding site
    • Schoentgen F. and Jollés P. (1995) From structure to function: possible biological roles of a new widespread protein family binding hydrophobic ligands and displaying a nucleotide binding site. FEBS Lett. 369, 22-26.
    • (1995) FEBS Lett. , vol.369 , pp. 22-26
    • Schoentgen, F.1    Jollés, P.2
  • 42
    • 0033538487 scopus 로고    scopus 로고
    • Association of the D2 dopamine receptor third cytoplasmic loop with spinophilin, a protein phosphatase-1-interacting protein
    • Smith F. D., Oxford G. S., and Milgram S. L. (1999) Association of the D2 dopamine receptor third cytoplasmic loop with spinophilin, a protein phosphatase-1-interacting protein. J. Biol. Chem. 274, 19894-19900.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19894-19900
    • Smith, F.D.1    Oxford, G.S.2    Milgram, S.L.3
  • 43
    • 0027293023 scopus 로고
    • Chronic opioid treatment may uncouple opioid receptors and G proteins: Evidence from radiation inactivalion analysis
    • Tao P. L., Chang L. R., Chou Y. P., Law P. Y., and Loh H. H. (1993) Chronic opioid treatment may uncouple opioid receptors and G proteins: evidence from radiation inactivalion analysis. Eur. J. Pharmacol. 246, 233-238.
    • (1993) Eur. J. Pharmacol. , vol.246 , pp. 233-238
    • Tao, P.L.1    Chang, L.R.2    Chou, Y.P.3    Law, P.Y.4    Loh, H.H.5
  • 44
    • 0033618426 scopus 로고    scopus 로고
    • Calmodulin binding to G protein-coupling domain of opioid receptors
    • Wang D., Sadee W., and Quillian J. M. (1999) Calmodulin binding to G protein-coupling domain of opioid receptors. J. Biol. Chem. 274, 22081-22088.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22081-22088
    • Wang, D.1    Sadee, W.2    Quillian, J.M.3
  • 45
    • 0032402450 scopus 로고    scopus 로고
    • Molecular basis of receptor/G protein-coupling selectivity
    • Wess J. (1998) Molecular basis of receptor/G protein-coupling selectivity. Pharmacol Ther. 80, 231-264.
    • (1998) Pharmacol Ther. , vol.80 , pp. 231-264
    • Wess, J.1


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