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Volumn 77, Issue 2, 2009, Pages 216-227

Concomitant activation of adenylyl cyclase suppresses the opposite influences of CB1 cannabinoid receptor agonists on tyrosine hydroxylase expression

Author keywords

Cell signalling; Forskolin; Functional selectivity; Gene reporter; Tyrosine hydroxylase

Indexed keywords

4 (1,1 DIMETHYLHEPTYL) 1',2',3',4',5',6' HEXAHYDRO 2,3' DIHYDROXY 6' (3 HYDROXYPROPYL)BIPHENYL; ADENYLATE CYCLASE; CANNABINOID 1 RECEPTOR AGONIST; CRE RECOMBINASE; DEXANABINOL; FORSKOLIN; LUCIFERASE; PERTUSSIS TOXIN; PROTEIN KINASE C; TRANSCRIPTION FACTOR AP 1; TYROSINE 3 MONOOXYGENASE;

EID: 57249103358     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2008.10.010     Document Type: Article
Times cited : (9)

References (56)
  • 1
    • 0027516837 scopus 로고
    • A dual role for the cAMP-dependent protein kinase in tyrosine hydroxylase gene expression
    • Kim K.S., Park D.H., Wessel T.C., Song B., Wagner J.A., and Joh T.H. A dual role for the cAMP-dependent protein kinase in tyrosine hydroxylase gene expression. Proc Natl Acad Sci USA 90 (1993) 3471-3475
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3471-3475
    • Kim, K.S.1    Park, D.H.2    Wessel, T.C.3    Song, B.4    Wagner, J.A.5    Joh, T.H.6
  • 2
    • 0027291181 scopus 로고
    • Both the basal and inducible transcription of the tyrosine hydroxylase gene are dependent upon a cAMP response element
    • Kim K.S., Lee M.K., Carroll J., and Joh T.H. Both the basal and inducible transcription of the tyrosine hydroxylase gene are dependent upon a cAMP response element. J Biol Chem 268 (1993) 15689-15695
    • (1993) J Biol Chem , vol.268 , pp. 15689-15695
    • Kim, K.S.1    Lee, M.K.2    Carroll, J.3    Joh, T.H.4
  • 3
    • 0024421363 scopus 로고
    • 5′ flanking DNA sequences direct cell-specific expression of rat tyrosine hydroxylase
    • Cambi F., Fung B., and Chikaraishi D. 5′ flanking DNA sequences direct cell-specific expression of rat tyrosine hydroxylase. J Neurochem 53 (1989) 1656-1659
    • (1989) J Neurochem , vol.53 , pp. 1656-1659
    • Cambi, F.1    Fung, B.2    Chikaraishi, D.3
  • 4
    • 0030023053 scopus 로고    scopus 로고
    • AP1-mediated transcriptional enhancement of the rat tyrosine hydroxylase gene by muscarinic stimulation
    • Chae H.D., Suh B.C., Joh T.H., and Kim K.T. AP1-mediated transcriptional enhancement of the rat tyrosine hydroxylase gene by muscarinic stimulation. J Neurochem 66 (1996) 1264-1272
    • (1996) J Neurochem , vol.66 , pp. 1264-1272
    • Chae, H.D.1    Suh, B.C.2    Joh, T.H.3    Kim, K.T.4
  • 5
    • 0036765563 scopus 로고    scopus 로고
    • Neurotensin induces tyrosine hydroxylase gene activation through nitric oxide and protein kinase C signaling pathways
    • Najimi M., Robert J.J., Mallet J., Rostene W., and Forgez P. Neurotensin induces tyrosine hydroxylase gene activation through nitric oxide and protein kinase C signaling pathways. Mol Pharmacol 62 (2002) 647-653
    • (2002) Mol Pharmacol , vol.62 , pp. 647-653
    • Najimi, M.1    Robert, J.J.2    Mallet, J.3    Rostene, W.4    Forgez, P.5
  • 6
    • 0033777248 scopus 로고    scopus 로고
    • Regulation of tyrosine hydroxylase gene transcription by the cAMP-signaling pathway: involvement of multiple transcription factors
    • Lim J., Yang C., Hong S.J., and Kim K.S. Regulation of tyrosine hydroxylase gene transcription by the cAMP-signaling pathway: involvement of multiple transcription factors. Mol Cell Biochem 212 (2000) 51-60
    • (2000) Mol Cell Biochem , vol.212 , pp. 51-60
    • Lim, J.1    Yang, C.2    Hong, S.J.3    Kim, K.S.4
  • 7
    • 0032981668 scopus 로고    scopus 로고
    • CREB mediates the cAMP-responsiveness of the tyrosine hydroxylase gene: use of an antisense RNA strategy to produce CREB-deficient PC12 cell lines
    • Piech-Dumas K.M., and Tank A.W. CREB mediates the cAMP-responsiveness of the tyrosine hydroxylase gene: use of an antisense RNA strategy to produce CREB-deficient PC12 cell lines. Brain Res Mol Brain Res 70 (1999) 219-230
    • (1999) Brain Res Mol Brain Res , vol.70 , pp. 219-230
    • Piech-Dumas, K.M.1    Tank, A.W.2
  • 8
    • 13244262876 scopus 로고    scopus 로고
    • Role of basic region leucine zipper transcription factors cyclic AMP response element binding protein (CREB), CREB2, activating transcription factor 2 and CAAT/enhancer binding protein alpha in cyclic AMP response element-mediated transcription
    • Thiel G., Al Sarraj J., Vinson C., Stefano L., and Bach K. Role of basic region leucine zipper transcription factors cyclic AMP response element binding protein (CREB), CREB2, activating transcription factor 2 and CAAT/enhancer binding protein alpha in cyclic AMP response element-mediated transcription. J Neurochem 92 (2005) 321-336
    • (2005) J Neurochem , vol.92 , pp. 321-336
    • Thiel, G.1    Al Sarraj, J.2    Vinson, C.3    Stefano, L.4    Bach, K.5
  • 9
    • 0030814764 scopus 로고    scopus 로고
    • Structure/function relationship of the cAMP response element in tyrosine hydroxylase gene transcription
    • Tinti C., Yang C., Seo H., Conti B., Kim C., Joh T.H., et al. Structure/function relationship of the cAMP response element in tyrosine hydroxylase gene transcription. J Biol Chem 272 (1997) 19158-19164
    • (1997) J Biol Chem , vol.272 , pp. 19158-19164
    • Tinti, C.1    Yang, C.2    Seo, H.3    Conti, B.4    Kim, C.5    Joh, T.H.6
  • 10
    • 16244411322 scopus 로고    scopus 로고
    • Differential effects of forskolin on tyrosine hydroxylase gene transcription in identified brainstem catecholaminergic neuronal subtypes in organotypic culture
    • Rusnak M., and Gainer H. Differential effects of forskolin on tyrosine hydroxylase gene transcription in identified brainstem catecholaminergic neuronal subtypes in organotypic culture. Eur J Neurosci 21 (2005) 889-898
    • (2005) Eur J Neurosci , vol.21 , pp. 889-898
    • Rusnak, M.1    Gainer, H.2
  • 12
    • 0038472490 scopus 로고    scopus 로고
    • c-Fos is essential for the response of the tyrosine hydroxylase gene to depolarization or phorbol ester
    • Sun B., and Tank A.W. c-Fos is essential for the response of the tyrosine hydroxylase gene to depolarization or phorbol ester. J Neurochem 85 (2003) 1421-1430
    • (2003) J Neurochem , vol.85 , pp. 1421-1430
    • Sun, B.1    Tank, A.W.2
  • 15
    • 34447619258 scopus 로고    scopus 로고
    • Agonist selective modulation of tyrosine hydroxylase expression by cannabinoid ligands in a murine neuroblastoma cell line
    • Bosier B., Tilleux S., Najimi M., Lambert D.M., and Hermans E. Agonist selective modulation of tyrosine hydroxylase expression by cannabinoid ligands in a murine neuroblastoma cell line. J Neurochem 102 (2007) 1996-2007
    • (2007) J Neurochem , vol.102 , pp. 1996-2007
    • Bosier, B.1    Tilleux, S.2    Najimi, M.3    Lambert, D.M.4    Hermans, E.5
  • 16
    • 34447650979 scopus 로고    scopus 로고
    • Versatility of GPCR recognition by drugs: from biological implications to therapeutic relevance
    • Bosier B., and Hermans E. Versatility of GPCR recognition by drugs: from biological implications to therapeutic relevance. Trends Pharmacol Sci 28 (2007) 438-446
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 438-446
    • Bosier, B.1    Hermans, E.2
  • 17
    • 50249177582 scopus 로고    scopus 로고
    • Differential modulation of AP-1- and CRE-driven transcription by cannabinoid agonists emphasizes functional selectivity at the CB1 receptor
    • Bosier B., Hermans E., and Lambert D. Differential modulation of AP-1- and CRE-driven transcription by cannabinoid agonists emphasizes functional selectivity at the CB1 receptor. Br J Pharmacol 155 (2008) 24-33
    • (2008) Br J Pharmacol , vol.155 , pp. 24-33
    • Bosier, B.1    Hermans, E.2    Lambert, D.3
  • 18
    • 0032159213 scopus 로고    scopus 로고
    • Inhibition by insulin of glucocorticoid-induced gene transcription: involvement of the ligand-binding domain of the glucocorticoid receptor and independence from the phosphatidylinositol 3-kinase and mitogen-activated protein kinase pathways
    • Pierreux C.E., Urso B., De Meyts P., Rousseau G.G., and Lemaigre F.P. Inhibition by insulin of glucocorticoid-induced gene transcription: involvement of the ligand-binding domain of the glucocorticoid receptor and independence from the phosphatidylinositol 3-kinase and mitogen-activated protein kinase pathways. Mol Endocrinol 12 (1998) 1343-1354
    • (1998) Mol Endocrinol , vol.12 , pp. 1343-1354
    • Pierreux, C.E.1    Urso, B.2    De Meyts, P.3    Rousseau, G.G.4    Lemaigre, F.P.5
  • 19
    • 0242583853 scopus 로고    scopus 로고
    • The endocannabinoid system in the basal ganglia and in the mesolimbic reward system: implications for neurological and psychiatric disorders
    • van der Stelt M., and Di Marzo V. The endocannabinoid system in the basal ganglia and in the mesolimbic reward system: implications for neurological and psychiatric disorders. Eur J Pharmacol 480 (2003) 133-150
    • (2003) Eur J Pharmacol , vol.480 , pp. 133-150
    • van der Stelt, M.1    Di Marzo, V.2
  • 20
    • 1642323631 scopus 로고    scopus 로고
    • Tyrosine hydroxylase transcription depends primarily on cAMP response element activity, regardless of the type of inducing stimulus
    • Lewis-Tuffin L.J., Quinn P.G., and Chikaraishi D.M. Tyrosine hydroxylase transcription depends primarily on cAMP response element activity, regardless of the type of inducing stimulus. Mol Cell Neurosci 25 (2004) 536-547
    • (2004) Mol Cell Neurosci , vol.25 , pp. 536-547
    • Lewis-Tuffin, L.J.1    Quinn, P.G.2    Chikaraishi, D.M.3
  • 21
    • 0037430846 scopus 로고    scopus 로고
    • Interactions between Egr1 and AP1 factors in regulation of tyrosine hydroxylase transcription
    • Nakashima A., Ota A., and Sabban E.L. Interactions between Egr1 and AP1 factors in regulation of tyrosine hydroxylase transcription. Brain Res Mol Brain Res 112 (2003) 61-69
    • (2003) Brain Res Mol Brain Res , vol.112 , pp. 61-69
    • Nakashima, A.1    Ota, A.2    Sabban, E.L.3
  • 22
    • 0034282856 scopus 로고    scopus 로고
    • Ability of Egr1 to activate tyrosine hydroxylase transcription in PC12 cells Cross-talk with AP-1 factors
    • Papanikolaou N.A., and Sabban E.L. Ability of Egr1 to activate tyrosine hydroxylase transcription in PC12 cells Cross-talk with AP-1 factors. J Biol Chem 275 (2000) 26683-26689
    • (2000) J Biol Chem , vol.275 , pp. 26683-26689
    • Papanikolaou, N.A.1    Sabban, E.L.2
  • 23
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • Shaulian E., and Karin M. AP-1 as a regulator of cell life and death. Nat Cell Biol 4 (2002) E131-E136
    • (2002) Nat Cell Biol , vol.4
    • Shaulian, E.1    Karin, M.2
  • 24
    • 22844435649 scopus 로고    scopus 로고
    • 2-Arachidonoylglycerol stimulates activator protein-1-dependent transcriptional activity and enhances epidermal growth factor-induced cell transformation in JB6 P + cells
    • Zhao Q., He Z., Chen N., Cho Y.Y., Zhu F., Lu C., et al. 2-Arachidonoylglycerol stimulates activator protein-1-dependent transcriptional activity and enhances epidermal growth factor-induced cell transformation in JB6 P + cells. J Biol Chem 280 (2005) 26735-26742
    • (2005) J Biol Chem , vol.280 , pp. 26735-26742
    • Zhao, Q.1    He, Z.2    Chen, N.3    Cho, Y.Y.4    Zhu, F.5    Lu, C.6
  • 25
    • 0141668883 scopus 로고    scopus 로고
    • The endocannabinoid system in human keratinocytes. Evidence that anandamide inhibits epidermal differentiation through CB1 receptor-dependent inhibition of protein kinase C, activation protein-1, and transglutaminase
    • Maccarrone M., Di Rienzo M., Battista N., Gasperi V., Guerrieri P., Rossi A., et al. The endocannabinoid system in human keratinocytes. Evidence that anandamide inhibits epidermal differentiation through CB1 receptor-dependent inhibition of protein kinase C, activation protein-1, and transglutaminase. J Biol Chem 278 (2003) 33896-33903
    • (2003) J Biol Chem , vol.278 , pp. 33896-33903
    • Maccarrone, M.1    Di Rienzo, M.2    Battista, N.3    Gasperi, V.4    Guerrieri, P.5    Rossi, A.6
  • 26
    • 0142184968 scopus 로고    scopus 로고
    • Neurons on cannabinoids: dead or alive?
    • Guzman M. Neurons on cannabinoids: dead or alive?. Br J Pharmacol 140 (2003) 439-440
    • (2003) Br J Pharmacol , vol.140 , pp. 439-440
    • Guzman, M.1
  • 27
    • 84855339807 scopus 로고    scopus 로고
    • Effects on cell viability
    • Guzman M. Effects on cell viability. Handb Exp Pharmacol (2005) 627-642
    • (2005) Handb Exp Pharmacol , pp. 627-642
    • Guzman, M.1
  • 28
    • 0025942516 scopus 로고
    • The bisindolylmaleimide GF 109203X is a potent and selective inhibitor of protein kinase C
    • Toullec D., Pianetti P., Coste H., Bellevergue P., Grand-Perret T., Ajakane M., et al. The bisindolylmaleimide GF 109203X is a potent and selective inhibitor of protein kinase C. J Biol Chem 266 (1991) 15771-15781
    • (1991) J Biol Chem , vol.266 , pp. 15771-15781
    • Toullec, D.1    Pianetti, P.2    Coste, H.3    Bellevergue, P.4    Grand-Perret, T.5    Ajakane, M.6
  • 31
    • 0023155966 scopus 로고
    • K-252 compounds, novel and potent inhibitors of protein kinase C and cyclic nucleotide-dependent protein kinases
    • Kase H., Iwahashi K., Nakanishi S., Matsuda Y., Yamada K., Takahashi M., et al. K-252 compounds, novel and potent inhibitors of protein kinase C and cyclic nucleotide-dependent protein kinases. Biochem Biophys Res Commun 142 (1987) 436-440
    • (1987) Biochem Biophys Res Commun , vol.142 , pp. 436-440
    • Kase, H.1    Iwahashi, K.2    Nakanishi, S.3    Matsuda, Y.4    Yamada, K.5    Takahashi, M.6
  • 32
    • 0025248571 scopus 로고
    • Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells
    • Chijiwa T., Mishima A., Hagiwara M., Sano M., Hayashi K., Inoue T., et al. Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells. J Biol Chem 265 (1990) 5267-5272
    • (1990) J Biol Chem , vol.265 , pp. 5267-5272
    • Chijiwa, T.1    Mishima, A.2    Hagiwara, M.3    Sano, M.4    Hayashi, K.5    Inoue, T.6
  • 35
    • 0038777265 scopus 로고    scopus 로고
    • The stimulatory effect of cannabinoids on calcium uptake is mediated by Gs GTP-binding proteins and cAMP formation
    • Bash R., Rubovitch V., Gafni M., and Sarne Y. The stimulatory effect of cannabinoids on calcium uptake is mediated by Gs GTP-binding proteins and cAMP formation. Neurosignals 12 (2003) 39-44
    • (2003) Neurosignals , vol.12 , pp. 39-44
    • Bash, R.1    Rubovitch, V.2    Gafni, M.3    Sarne, Y.4
  • 36
    • 36448970925 scopus 로고    scopus 로고
    • Agonist-dependent cannabinoid receptor signalling in human trabecular meshwork cells
    • McIntosh B.T., Hudson B., Yegorova S., Jollimore C.A., and Kelly M.E. Agonist-dependent cannabinoid receptor signalling in human trabecular meshwork cells. Br J Pharmacol 152 (2007) 1111-1120
    • (2007) Br J Pharmacol , vol.152 , pp. 1111-1120
    • McIntosh, B.T.1    Hudson, B.2    Yegorova, S.3    Jollimore, C.A.4    Kelly, M.E.5
  • 37
    • 38549130695 scopus 로고    scopus 로고
    • Unique agonist-bound cannabinoid CB1 receptor conformations indicate agonist specificity in signaling
    • Georgieva T., Devanathan S., Stropova D., Park C.K., Salamon Z., Tollin G., et al. Unique agonist-bound cannabinoid CB1 receptor conformations indicate agonist specificity in signaling. Eur J Pharmacol 581 (2008) 19-29
    • (2008) Eur J Pharmacol , vol.581 , pp. 19-29
    • Georgieva, T.1    Devanathan, S.2    Stropova, D.3    Park, C.K.4    Salamon, Z.5    Tollin, G.6
  • 38
    • 0032756226 scopus 로고    scopus 로고
    • Agonist selective regulation of G proteins by cannabinoid CB(1) and CB(2) receptors
    • Glass M., and Northup J.K. Agonist selective regulation of G proteins by cannabinoid CB(1) and CB(2) receptors. Mol Pharmacol 56 (1999) 1362-1369
    • (1999) Mol Pharmacol , vol.56 , pp. 1362-1369
    • Glass, M.1    Northup, J.K.2
  • 39
    • 21744437960 scopus 로고    scopus 로고
    • Chemically distinct ligands promote differential CB1 cannabinoid receptor-Gi protein interactions
    • Mukhopadhyay S., and Howlett A.C. Chemically distinct ligands promote differential CB1 cannabinoid receptor-Gi protein interactions. Mol Pharmacol 67 (2005) 2016-2024
    • (2005) Mol Pharmacol , vol.67 , pp. 2016-2024
    • Mukhopadhyay, S.1    Howlett, A.C.2
  • 40
    • 0030857066 scopus 로고    scopus 로고
    • Concurrent stimulation of cannabinoid CB1 and dopamine D2 receptors augments cAMP accumulation in striatal neurons: evidence for a Gs linkage to the CB1 receptor
    • Glass M., and Felder C.C. Concurrent stimulation of cannabinoid CB1 and dopamine D2 receptors augments cAMP accumulation in striatal neurons: evidence for a Gs linkage to the CB1 receptor. J Neurosci 17 (1997) 5327-5333
    • (1997) J Neurosci , vol.17 , pp. 5327-5333
    • Glass, M.1    Felder, C.C.2
  • 41
    • 0032968566 scopus 로고    scopus 로고
    • Dual intracellular signaling pathways mediated by the human cannabinoid CB1 receptor
    • Calandra B., Portier M., Kerneis A., Delpech M., Carillon C., Le Fur G., et al. Dual intracellular signaling pathways mediated by the human cannabinoid CB1 receptor. Eur J Pharmacol 374 (1999) 445-455
    • (1999) Eur J Pharmacol , vol.374 , pp. 445-455
    • Calandra, B.1    Portier, M.2    Kerneis, A.3    Delpech, M.4    Carillon, C.5    Le Fur, G.6
  • 42
    • 0032246648 scopus 로고    scopus 로고
    • Dual activation and inhibition of adenylyl cyclase by cannabinoid receptor agonists: evidence for agonist-specific trafficking of intracellular responses
    • Bonhaus D.W., Chang L.K., Kwan J., and Martin G.R. Dual activation and inhibition of adenylyl cyclase by cannabinoid receptor agonists: evidence for agonist-specific trafficking of intracellular responses. J Pharmacol Exp Ther 287 (1998) 884-888
    • (1998) J Pharmacol Exp Ther , vol.287 , pp. 884-888
    • Bonhaus, D.W.1    Chang, L.K.2    Kwan, J.3    Martin, G.R.4
  • 43
    • 22944487986 scopus 로고    scopus 로고
    • Multiple signaling states of G-protein-coupled receptors
    • Perez D.M., and Karnik S.S. Multiple signaling states of G-protein-coupled receptors. Pharmacol Rev 57 (2005) 147-161
    • (2005) Pharmacol Rev , vol.57 , pp. 147-161
    • Perez, D.M.1    Karnik, S.S.2
  • 44
    • 33748490903 scopus 로고    scopus 로고
    • In vitro pharmacological characterization of AM1241: a protean agonist at the cannabinoid CB2 receptor?
    • Yao B.B., Mukherjee S., Fan Y., Garrison T.R., Daza A.V., Grayson G.K., et al. In vitro pharmacological characterization of AM1241: a protean agonist at the cannabinoid CB2 receptor?. Br J Pharmacol 149 (2006) 145-154
    • (2006) Br J Pharmacol , vol.149 , pp. 145-154
    • Yao, B.B.1    Mukherjee, S.2    Fan, Y.3    Garrison, T.R.4    Daza, A.V.5    Grayson, G.K.6
  • 45
    • 0032502590 scopus 로고    scopus 로고
    • Repeated exposure to delta 9-tetrahydrocannabinol reduces prefrontal cortical dopamine metabolism in the rat
    • Jentsch J.D., Verrico C.D., Le D., and Roth R.H. Repeated exposure to delta 9-tetrahydrocannabinol reduces prefrontal cortical dopamine metabolism in the rat. Neurosci Lett 246 (1998) 169-172
    • (1998) Neurosci Lett , vol.246 , pp. 169-172
    • Jentsch, J.D.1    Verrico, C.D.2    Le, D.3    Roth, R.H.4
  • 46
    • 2442682719 scopus 로고    scopus 로고
    • Differential effects of acute cannabinoid drug treatment, mediated by CB1 receptors, on the in vivo activity of tyrosine and tryptophan hydroxylase in the rat brain
    • Moranta D., Esteban S., and Garcia-Sevilla J.A. Differential effects of acute cannabinoid drug treatment, mediated by CB1 receptors, on the in vivo activity of tyrosine and tryptophan hydroxylase in the rat brain. Naunyn Schmiedebergs Arch Pharmacol 369 (2004) 516-524
    • (2004) Naunyn Schmiedebergs Arch Pharmacol , vol.369 , pp. 516-524
    • Moranta, D.1    Esteban, S.2    Garcia-Sevilla, J.A.3
  • 47
    • 0023941878 scopus 로고
    • Activation of adenylate cyclase and inhibition of glucose transport in rat adipocytes by forskolin analogues: structural determinants for distinct sites of action
    • Joost H.G., Habberfield A.D., Simpson I.A., Laurenza A., and Seamon K.B. Activation of adenylate cyclase and inhibition of glucose transport in rat adipocytes by forskolin analogues: structural determinants for distinct sites of action. Mol Pharmacol 33 (1988) 449-453
    • (1988) Mol Pharmacol , vol.33 , pp. 449-453
    • Joost, H.G.1    Habberfield, A.D.2    Simpson, I.A.3    Laurenza, A.4    Seamon, K.B.5
  • 48
    • 0023764549 scopus 로고
    • Effect of forskolin on voltage-gated K + channels is independent of adenylate cyclase activation
    • Hoshi T., Garber S.S., and Aldrich R.W. Effect of forskolin on voltage-gated K + channels is independent of adenylate cyclase activation. Science 240 (1988) 1652-1655
    • (1988) Science , vol.240 , pp. 1652-1655
    • Hoshi, T.1    Garber, S.S.2    Aldrich, R.W.3
  • 49
    • 0023753033 scopus 로고
    • Modulation of acetylcholine receptor desensitization by forskolin is independent of cAMP
    • Wagoner P.K., and Pallotta B.S. Modulation of acetylcholine receptor desensitization by forskolin is independent of cAMP. Science 240 (1988) 1655-1657
    • (1988) Science , vol.240 , pp. 1655-1657
    • Wagoner, P.K.1    Pallotta, B.S.2
  • 50
    • 0003259456 scopus 로고
    • cAMP and forskolin decrease gamma-aminobutyric acid-gated chloride flux in rat brain synaptoneurosomes
    • Heuschneider G., and Schwartz R.D. cAMP and forskolin decrease gamma-aminobutyric acid-gated chloride flux in rat brain synaptoneurosomes. Proc Natl Acad Sci USA 86 (1989) 2938-2942
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2938-2942
    • Heuschneider, G.1    Schwartz, R.D.2
  • 51
    • 0028029718 scopus 로고
    • Regulation of forskolin interactions with type I, II, V, and VI adenylyl cyclases by Gs alpha
    • Sutkowski E.M., Tang W.J., Broome C.W., Robbins J.D., and Seamon K.B. Regulation of forskolin interactions with type I, II, V, and VI adenylyl cyclases by Gs alpha. Biochemistry 33 (1994) 12852-12859
    • (1994) Biochemistry , vol.33 , pp. 12852-12859
    • Sutkowski, E.M.1    Tang, W.J.2    Broome, C.W.3    Robbins, J.D.4    Seamon, K.B.5
  • 52
    • 0031660109 scopus 로고    scopus 로고
    • Cannabinoid receptor activation differentially regulates the various adenylyl cyclase isozymes
    • Rhee M.H., Bayewitch M., Avidor-Reiss T., Levy R., and Vogel Z. Cannabinoid receptor activation differentially regulates the various adenylyl cyclase isozymes. J Neurochem 71 (1998) 1525-1534
    • (1998) J Neurochem , vol.71 , pp. 1525-1534
    • Rhee, M.H.1    Bayewitch, M.2    Avidor-Reiss, T.3    Levy, R.4    Vogel, Z.5
  • 53
    • 0034106410 scopus 로고    scopus 로고
    • Differential superactivation of adenylyl cyclase isozymes after chronic activation of the CB(1) cannabinoid receptor
    • Rhee M.H., Nevo I., Avidor-Reiss T., Levy R., and Vogel Z. Differential superactivation of adenylyl cyclase isozymes after chronic activation of the CB(1) cannabinoid receptor. Mol Pharmacol 57 (2000) 746-752
    • (2000) Mol Pharmacol , vol.57 , pp. 746-752
    • Rhee, M.H.1    Nevo, I.2    Avidor-Reiss, T.3    Levy, R.4    Vogel, Z.5
  • 54
    • 0036191893 scopus 로고    scopus 로고
    • G protein specificity: traffic direction required
    • Albert P.R., and Robillard L. G protein specificity: traffic direction required. Cell Signal 14 (2002) 407-418
    • (2002) Cell Signal , vol.14 , pp. 407-418
    • Albert, P.R.1    Robillard, L.2
  • 55
    • 0033515116 scopus 로고    scopus 로고
    • Distinct roles for Galphai2, Galphai3, and Gbeta gamma in modulation offorskolin- or Gs-mediated cAMP accumulation and calcium mobilization by dopamine D2S receptors
    • Ghahremani M.H., Cheng P., Lembo P.M., and Albert P.R. Distinct roles for Galphai2, Galphai3, and Gbeta gamma in modulation offorskolin- or Gs-mediated cAMP accumulation and calcium mobilization by dopamine D2S receptors. J Biol Chem 274 (1999) 9238-9245
    • (1999) J Biol Chem , vol.274 , pp. 9238-9245
    • Ghahremani, M.H.1    Cheng, P.2    Lembo, P.M.3    Albert, P.R.4
  • 56
    • 33644879238 scopus 로고    scopus 로고
    • 8-OH-DPAT attenuates isoproterenol- but not forskolin-stimulated accumulation of cAMP in mediobasal hypothalamus
    • Majumdar D., Peterson-Ford A., and Uphouse L. 8-OH-DPAT attenuates isoproterenol- but not forskolin-stimulated accumulation of cAMP in mediobasal hypothalamus. Brain Res 1075 (2006) 93-99
    • (2006) Brain Res , vol.1075 , pp. 93-99
    • Majumdar, D.1    Peterson-Ford, A.2    Uphouse, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.