메뉴 건너뛰기




Volumn 112, Issue 4, 2010, Pages 1026-1034

Differential modulation of mu-opioid receptor signaling to adenylyl cyclase by regulators of G protein signaling proteins 4 or 8 and 7 in permeabilised C6 cells is Gα subtype dependent

Author keywords

Adenylyl cyclase; G proteins; Mu opioid; Permeabilization; Regulators of G protein signaling proteins

Indexed keywords

ADENYLATE CYCLASE; DIGITONIN; ENKEPHALIN[2 DEXTRO ALANINE 4 METHYLPHENYLALANINE 5 GLYCINE]; FORSKOLIN; MU OPIATE RECEPTOR; REGULATOR OF G PROTEIN SIGNALING 7; REGULATOR OF G PROTEIN SIGNALING 8; RGS PROTEIN; RGS4 PROTEIN; UNCLASSIFIED DRUG;

EID: 75149115424     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2009.06519.x     Document Type: Article
Times cited : (28)

References (37)
  • 1
    • 0034967910 scopus 로고    scopus 로고
    • Stimulation of guanosine-5′-O-(3-[35S]thio)triphosphate binding in digitonin-permeabilized C6 rat glioma cells: Evidence for an organized association of mu-opioid receptors and G protein
    • Alt A., McFadyen I. J., Fan C. D., Woods J. H. Traynor J. R. (2001) Stimulation of guanosine-5′-O-(3-[35S]thio)triphosphate binding in digitonin-permeabilized C6 rat glioma cells: evidence for an organized association of mu-opioid receptors and G protein. J. Pharmacol. Exp. Ther. 298, 116 121.
    • (2001) J. Pharmacol. Exp. Ther. , vol.298 , pp. 116-121
    • Alt, A.1    McFadyen, I.J.2    Fan, C.D.3    Woods, J.H.4    Traynor, J.R.5
  • 2
    • 0022556401 scopus 로고
    • Maintenance of whole cell isoproterenol and forskolin responsiveness in adenylate cyclase of permeabilized cells
    • Brooker G. Pedone C. (1986) Maintenance of whole cell isoproterenol and forskolin responsiveness in adenylate cyclase of permeabilized cells. J. Cyclic Nucleotide Protein Phosphor. Res. 11, 113 121.
    • (1986) J. Cyclic Nucleotide Protein Phosphor. Res. , vol.11 , pp. 113-121
    • Brooker, G.1    Pedone, C.2
  • 3
    • 1542358989 scopus 로고    scopus 로고
    • Molecular neurobiology of drug addiction
    • Chao J. Nestler E. J. (2004) Molecular neurobiology of drug addiction. Annu. Rev. Med. 55, 113 132.
    • (2004) Annu. Rev. Med. , vol.55 , pp. 113-132
    • Chao, J.1    Nestler, E.J.2
  • 5
    • 4344691146 scopus 로고    scopus 로고
    • Assays for G-protein-coupled receptor signaling using RGS-insensitive Galpha subunits
    • Clark M. J. Traynor J. R. (2004) Assays for G-protein-coupled receptor signaling using RGS-insensitive Galpha subunits. Methods Enzymol. 389, 155 169.
    • (2004) Methods Enzymol. , vol.389 , pp. 155-169
    • Clark, M.J.1    Traynor, J.R.2
  • 6
    • 0037984338 scopus 로고    scopus 로고
    • o. Effects on adenylyl cyclase, extracellular signal-regulated kinases, and intracellular calcium pathways
    • o. Effects on adenylyl cyclase, extracellular signal-regulated kinases, and intracellular calcium pathways. J. Biol. Chem. 278, 9418 9425.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9418-9425
    • Clark, M.J.1    Harrison, C.2    Zhong, H.3    Neubig, R.R.4    Traynor, J.R.5
  • 7
    • 33645846309 scopus 로고    scopus 로고
    • Comparison of the relative efficacy and potency of mu-opioid agonists to activate Galpha(i/o) proteins containing a pertussis toxin-insensitive mutation
    • Clark M. J., Furman C. A., Gilson T. D. Traynor J. R. (2006) Comparison of the relative efficacy and potency of mu-opioid agonists to activate Galpha(i/o) proteins containing a pertussis toxin-insensitive mutation. J. Pharmacol. Exp. Ther. 317, 858 864.
    • (2006) J. Pharmacol. Exp. Ther. , vol.317 , pp. 858-864
    • Clark, M.J.1    Furman, C.A.2    Gilson, T.D.3    Traynor, J.R.4
  • 8
    • 42449104407 scopus 로고    scopus 로고
    • Endogenous regulators of G protein signaling differentially modulate full and partial mu-opioid agonists at adenylyl cyclase as predicted by a collision coupling model
    • Clark M. J., Linderman J. J. Traynor J. R. (2008) Endogenous regulators of G protein signaling differentially modulate full and partial mu-opioid agonists at adenylyl cyclase as predicted by a collision coupling model. Mol. Pharmacol. 73, 1538 1548.
    • (2008) Mol. Pharmacol. , vol.73 , pp. 1538-1548
    • Clark, M.J.1    Linderman, J.J.2    Traynor, J.R.3
  • 9
    • 19244367478 scopus 로고    scopus 로고
    • The R7 subfamily of RGS proteins assists tachyphylaxis and acute tolerance at mu-opioid receptors
    • Garzon J., Lopez-Fando A. Sanchez-Blazquez P. (2003) The R7 subfamily of RGS proteins assists tachyphylaxis and acute tolerance at mu-opioid receptors. Neuropsychopharmacology 28, 1983 1990.
    • (2003) Neuropsychopharmacology , vol.28 , pp. 1983-1990
    • Garzon, J.1    Lopez-Fando, A.2    Sanchez-Blazquez, P.3
  • 10
    • 0030764226 scopus 로고    scopus 로고
    • Regulators of G-protein signaling (RGS) proteins: Region-specific expression of nine subtypes in rat brain
    • Gold S. J., Ni Y. G., Dohlman H. G. Nestler E. J. (1997) Regulators of G-protein signaling (RGS) proteins: region-specific expression of nine subtypes in rat brain. J. Neurosci. 17, 8024 8037.
    • (1997) J. Neurosci. , vol.17 , pp. 8024-8037
    • Gold, S.J.1    Ni, Y.G.2    Dohlman, H.G.3    Nestler, E.J.4
  • 12
    • 0031017573 scopus 로고    scopus 로고
    • RGS4 and GAIP are GTPase-activating proteins for Gq alpha and block activation of phospholipase C beta by gamma-thio-GTP-Gq alpha
    • Hepler J. R., Berman D. M., Gilman A. G. Kozasa T. (1997) RGS4 and GAIP are GTPase-activating proteins for Gq alpha and block activation of phospholipase C beta by gamma-thio-GTP-Gq alpha. Proc. Natl Acad. Sci. USA 94, 428 432.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 428-432
    • Hepler, J.R.1    Berman, D.M.2    Gilman, A.G.3    Kozasa, T.4
  • 13
    • 0036733358 scopus 로고    scopus 로고
    • Cellular regulation of RGS proteins: Modulators and integrators of G protein signaling
    • Hollinger S. Hepler J. R. (2002) Cellular regulation of RGS proteins: modulators and integrators of G protein signaling. Pharmacol. Rev. 54, 527 559.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 527-559
    • Hollinger, S.1    Hepler, J.R.2
  • 14
    • 0038193543 scopus 로고    scopus 로고
    • RGS6, RGS7, RGS9, and RGS11 stimulate GTPase activity of Gi family G-proteins with differential selectivity and maximal activity
    • Hooks S. B., Waldo G. L., Corbitt J., Bodor E. T., Krumins A. M. Harden T. K. (2003) RGS6, RGS7, RGS9, and RGS11 stimulate GTPase activity of Gi family G-proteins with differential selectivity and maximal activity. J. Biol. Chem. 278, 10087 10093.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10087-10093
    • Hooks, S.B.1    Waldo, G.L.2    Corbitt, J.3    Bodor, E.T.4    Krumins, A.M.5    Harden, T.K.6
  • 15
    • 0036781281 scopus 로고    scopus 로고
    • Molecular mechanisms of analgesia induced by opioids and ethanol: Is the GIRK channel one of the keys?
    • Ikeda K., Kobayashi T., Kumanishi T., Yano R., Sora I. Niki H. (2002) Molecular mechanisms of analgesia induced by opioids and ethanol: is the GIRK channel one of the keys? Neurosci. Res. 44, 121 131.
    • (2002) Neurosci. Res. , vol.44 , pp. 121-131
    • Ikeda, K.1    Kobayashi, T.2    Kumanishi, T.3    Yano, R.4    Sora, I.5    Niki, H.6
  • 16
    • 0036456158 scopus 로고    scopus 로고
    • Expression of RGS2, RGS4 and RGS7 in the developing postnatal brain
    • Ingi T. Aoki Y. (2002) Expression of RGS2, RGS4 and RGS7 in the developing postnatal brain. Eur. J. Neurosci. 15, 929 936.
    • (2002) Eur. J. Neurosci. , vol.15 , pp. 929-936
    • Ingi, T.1    Aoki, Y.2
  • 18
  • 19
    • 0034721832 scopus 로고    scopus 로고
    • Rapid kinetics of regulator of G-protein signaling (RGS)-mediated Galphai and Galphao deactivation. Galpha specificity of RGS4 and RGS7
    • Lan K. L., Zhong H., Nanamori M. Neubig R. R. (2000) Rapid kinetics of regulator of G-protein signaling (RGS)-mediated Galphai and Galphao deactivation. Galpha specificity of RGS4 and RGS7. J. Biol. Chem. 275, 33497 33503.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33497-33503
    • Lan, K.L.1    Zhong, H.2    Nanamori, M.3    Neubig, R.R.4
  • 20
    • 0032791257 scopus 로고    scopus 로고
    • Differential binding properties of oripavines at cloned mu- and delta-opioid receptors
    • Lee K. O., Akil H., Woods J. H. Traynor J. R. (1999) Differential binding properties of oripavines at cloned mu- and delta-opioid receptors. Eur. J. Pharmacol. 378, 323 330.
    • (1999) Eur. J. Pharmacol. , vol.378 , pp. 323-330
    • Lee, K.O.1    Akil, H.2    Woods, J.H.3    Traynor, J.R.4
  • 21
    • 0025921771 scopus 로고
    • Purification of recombinant Gi alpha and Go alpha proteins from Escherichia coli
    • Linder M. E. Gilman A. G. (1991) Purification of recombinant Gi alpha and Go alpha proteins from Escherichia coli. Methods Enzymol. 195, 202 215.
    • (1991) Methods Enzymol. , vol.195 , pp. 202-215
    • Linder, M.E.1    Gilman, A.G.2
  • 22
    • 0035104122 scopus 로고    scopus 로고
    • The human delta opioid receptor activates G(i1)alpha more efficiently than G(o1)alpha
    • Moon H. E., Cavalli A., Bahia D. S., Hoffmann M., Massotte D. Milligan G. (2001) The human delta opioid receptor activates G(i1)alpha more efficiently than G(o1)alpha. J. Neurochem. 76, 1805 1813.
    • (2001) J. Neurochem. , vol.76 , pp. 1805-1813
    • Moon, H.E.1    Cavalli, A.2    Bahia, D.S.3    Hoffmann, M.4    Massotte, D.5    Milligan, G.6
  • 23
    • 0032695796 scopus 로고    scopus 로고
    • Regulators of G protein signaling 6 and 7. Purification of complexes with Gbeta5 and assessment of their effects on G protein-mediated signaling pathways
    • Posner B. A., Gilman A. G. Harris B. A. (1999) Regulators of G protein signaling 6 and 7. Purification of complexes with Gbeta5 and assessment of their effects on G protein-mediated signaling pathways. J. Biol. Chem. 274, 31087 31093.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31087-31093
    • Posner, B.A.1    Gilman, A.G.2    Harris, B.A.3
  • 24
    • 0028052299 scopus 로고
    • G-protein antisense oligodeoxyribonucleotides and mu-opioid supraspinal antinociception
    • Raffa R. B., Martinez R. P. Connelly C. D. (1994) G-protein antisense oligodeoxyribonucleotides and mu-opioid supraspinal antinociception. Eur. J. Pharmacol. 258, R5 R7.
    • (1994) Eur. J. Pharmacol. , vol.258
    • Raffa, R.B.1    Martinez, R.P.2    Connelly, C.D.3
  • 25
    • 33845301393 scopus 로고    scopus 로고
    • Identification of small-molecule inhibitors of RGS4 using a high-throughput flow cytometry protein interaction assay
    • Roman D. L., Talbot J. N., Roof R. A., Sunahara R. K., Traynor J. R. Neubig R. R. (2007) Identification of small-molecule inhibitors of RGS4 using a high-throughput flow cytometry protein interaction assay. Mol. Pharmacol. 71, 169 175.
    • (2007) Mol. Pharmacol. , vol.71 , pp. 169-175
    • Roman, D.L.1    Talbot, J.N.2    Roof, R.A.3    Sunahara, R.K.4    Traynor, J.R.5    Neubig, R.R.6
  • 27
    • 0033783132 scopus 로고    scopus 로고
    • GTPase-activating proteins for heterotrimeric G proteins: Regulators of G protein signaling (RGS) and RGS-like proteins
    • Ross E. M. Wilkie T. M. (2000) GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins. Annu. Rev. Biochem. 69, 795 827.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 795-827
    • Ross, E.M.1    Wilkie, T.M.2
  • 29
    • 0029552394 scopus 로고
    • In vivo injection of antisense oligodeoxynucleotides to G alpha subunits and supraspinal analgesia evoked by mu and delta opioid agonists
    • Sanchez-Blazquez P., Garcia-Espana A. Garzon J. (1995) In vivo injection of antisense oligodeoxynucleotides to G alpha subunits and supraspinal analgesia evoked by mu and delta opioid agonists. J. Pharmacol. Exp. Ther. 275, 1590 1596.
    • (1995) J. Pharmacol. Exp. Ther. , vol.275 , pp. 1590-1596
    • Sanchez-Blazquez, P.1    Garcia-Espana, A.2    Garzon, J.3
  • 30
    • 0025644869 scopus 로고
    • Permeabilizing cells: Some methods and applications for the study of intracellular processes
    • Schulz I. (1990) Permeabilizing cells: some methods and applications for the study of intracellular processes. Methods Enzymol. 192, 280 300.
    • (1990) Methods Enzymol. , vol.192 , pp. 280-300
    • Schulz, I.1
  • 31
    • 25444528729 scopus 로고    scopus 로고
    • The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits
    • Siderovski D. P. Willard F. S. (2005) The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits. Int. J. Biol. Sci. 1, 51 66.
    • (2005) Int. J. Biol. Sci. , vol.1 , pp. 51-66
    • Siderovski, D.P.1    Willard, F.S.2
  • 32
    • 0035931919 scopus 로고    scopus 로고
    • Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A
    • Slep K. C., Kercher M. A., He W., Cowan C. W., Wensel T. G. Sigler P. B. (2001) Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A. Nature 409, 1071 1077.
    • (2001) Nature , vol.409 , pp. 1071-1077
    • Slep, K.C.1    Kercher, M.A.2    He, W.3    Cowan, C.W.4    Wensel, T.G.5    Sigler, P.B.6
  • 33
    • 44049098168 scopus 로고    scopus 로고
    • Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits
    • Soundararajan M., Willard F. S., Kimple A. J. et al. (2008) Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits. Proc. Natl Acad. Sci. USA 105, 6457 6462.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 6457-6462
    • Soundararajan, M.1    Willard, F.S.2    Kimple, A.J.3
  • 34
    • 0030982264 scopus 로고    scopus 로고
    • Structure of RGS4 bound to AlF4 - Activated G(i alpha1): Stabilization of the transition state for GTP hydrolysis
    • Tesmer J. J., Berman D. M., Gilman A. G. Sprang S. R. (1997) Structure of RGS4 bound to AlF4 - activated G(i alpha1): stabilization of the transition state for GTP hydrolysis. Cell 89, 251 261.
    • (1997) Cell , vol.89 , pp. 251-261
    • Tesmer, J.J.1    Berman, D.M.2    Gilman, A.G.3    Sprang, S.R.4
  • 35
    • 0028986870 scopus 로고
    • 35S]thio)triphosphate binding to membranes from human neuroblastoma SH-SY5Y cells
    • 35S]thio)triphosphate binding to membranes from human neuroblastoma SH-SY5Y cells. Mol. Pharmacol. 47, 848 854.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 848-854
    • Traynor, J.R.1    Nahorski, S.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.