메뉴 건너뛰기




Volumn 16, Issue 42006, 1996, Pages 1-23

Anomalous behavior of CGP 12177A on β2-adrenergic receptors

Author keywords

[No Author keywords available]

Indexed keywords

4 (3 TERT BUTYLAMINO 2 HYDROXYPROPOXY) 2 BENZIMIDAZOLONE; BETA 1 ADRENERGIC RECEPTOR; CELL SURFACE RECEPTOR;

EID: 0029945009     PISSN: 10799893     EISSN: None     Source Type: Journal    
DOI: 10.3109/10799899609039938     Document Type: Article
Times cited : (75)

References (44)
  • 1
    • 0020523811 scopus 로고
    • CGP12177: a hydrophilic β-adrenergic receptor radioligand reveals high affinity binding of agonists to intact cells
    • Staehelin M., Simons P., Jaeggi K., Wigger N. CGP12177: a hydrophilic β-adrenergic receptor radioligand reveals high affinity binding of agonists to intact cells. J. Biol. Chem. 1983; 258: 3496 – 3502
    • (1983) J. Biol. Chem. , vol.258 , pp. 3496-3502
    • Staehelin, M.1    Simons, P.2    Jaeggi, K.3    Wigger, N.4
  • 2
    • 0020339975 scopus 로고
    • Rapid and reversible disappearence of β-adrenergic cell surface receptors
    • Staehelin M., Simons P. Rapid and reversible disappearence of β-adrenergic cell surface receptors. EMBO J. 1982; 1: 187 – 190
    • (1982) EMBO J. , vol.1 , pp. 187-190
    • Staehelin, M.1    Simons, P.2
  • 3
    • 0021088173 scopus 로고
    • Determination of the desensitization of β-adrenergic receptors by [3H]CCP-12177
    • Hertel C., Müller P., Portenier M., Staehelin M. Determination of the desensitization of β-adrenergic receptors by [3H]CCP-12177. Biochem. J. 1983; 216: 669 – 674
    • (1983) Biochem. J. , vol.216 , pp. 669-674
    • Hertel, C.1    Müller, P.2    Portenier, M.3    Staehelin, M.4
  • 4
    • 0022975277 scopus 로고
    • Desensitization of the β-adrenergic receptor-coupled adenylate cyclase in cultured mammalian cells: receptor sequestration versus receptor function
    • Kassis S., Olasmaa M., Sullivan M., Fishman P. H. Desensitization of the β-adrenergic receptor-coupled adenylate cyclase in cultured mammalian cells: receptor sequestration versus receptor function. J. Biol. Chem. 1986; 261: 12233 – 12237
    • (1986) J. Biol. Chem. , vol.261 , pp. 12233-12237
    • Kassis, S.1    Olasmaa, M.2    Sullivan, M.3    Fishman, P.H.4
  • 6
    • 0024405758 scopus 로고
    • The β-adrenergic radioligand [3H] CGP-12177, generally classified as an antagonist, is a thermogenic agonist in brown adipose tissue
    • Mohell N., Dicker A. The β-adrenergic radioligand [3H] CGP-12177, generally classified as an antagonist, is a thermogenic agonist in brown adipose tissue. Biochem. J. 1989; 261: 401 – 405
    • (1989) Biochem. J. , vol.261 , pp. 401-405
    • Mohell, N.1    Dicker, A.2
  • 7
    • 0025969595 scopus 로고
    • Adenylate cyclase agonist properties of CGP-12177A in brown fat: evidence for atypical β-adrenergic receptors
    • Scarpace P. J., Matheny M. Adenylate cyclase agonist properties of CGP-12177A in brown fat: evidence for atypical β-adrenergic receptors. Am. J. Physiol. 1991; 260: E226 – E231
    • (1991) Am. J. Physiol. , vol.260 , pp. E226-E231
    • Scarpace, P.J.1    Matheny, M.2
  • 8
    • 0026090708 scopus 로고
    • CGP 12177A modulates brown fat adenylate cyclase activity by interacting with two distinct receptor sites
    • Granneman J. G., Whitty C. J. CGP 12177A modulates brown fat adenylate cyclase activity by interacting with two distinct receptor sites. J. Pharmacol. Exp. Ther. 1991; 256: 421 – 425
    • (1991) J. Pharmacol. Exp. Ther. , vol.256 , pp. 421-425
    • Granneman, J.G.1    Whitty, C.J.2
  • 9
    • 0025827764 scopus 로고
    • Coexistence of three β-adrenoceptor subtypes in white fat cells of various mammalian species
    • Langin D., Portillo M. P., Saulnier-Blache J.-S., Lafontan M. Coexistence of three β-adrenoceptor subtypes in white fat cells of various mammalian species. Eur. J. Pharmacol. 1991; 199: 291 – 301
    • (1991) Eur. J. Pharmacol. , vol.199 , pp. 291-301
    • Langin, D.1    Portillo, M.P.2    Saulnier-Blache, J.-S.3    Lafontan, M.4
  • 10
    • 0025876222 scopus 로고
    • Atypical β-adrenergic receptor in 3T3-F442A adipocytes. Pharmacological and molecular relationship with the human β3-adrenergic receptor
    • Feve B., Emorine L. J., Lasnier F., Blin N., Baude B., Nahmias C., Strosberg A. D., Pairault J. Atypical β-adrenergic receptor in 3T3-F442A adipocytes. Pharmacological and molecular relationship with the human β3-adrenergic receptor. J. Biol. Chem. 1991; 266: 20329 – 20336
    • (1991) J. Biol. Chem. , vol.266 , pp. 20329-20336
    • Feve, B.1    Emorine, L.J.2    Lasnier, F.3    Blin, N.4    Baude, B.5    Nahmias, C.6    Strosberg, A.D.7    Pairault, J.8
  • 13
    • 0026325126 scopus 로고
    • Molecular cloning and expression of the rat β3-adrenergic receptor
    • Granneman J. G., Lahners K. N., Chaudhry A. Molecular cloning and expression of the rat β3-adrenergic receptor. Mol. Pharmacol. 1991; 40: 895 – 899
    • (1991) Mol. Pharmacol. , vol.40 , pp. 895-899
    • Granneman, J.G.1    Lahners, K.N.2    Chaudhry, A.3
  • 15
    • 0026530611 scopus 로고
    • Radioligand binding studies of the atypical β3-adrenergic receptor in rat brown adipose tissue using [3H]CGP 12177
    • Muzzin P., Revelli J.-P., Fraser C. M., Giacobino J.-P. Radioligand binding studies of the atypical β3-adrenergic receptor in rat brown adipose tissue using [3H]CGP 12177. FEBS Lett. 1992; 298: 162 – 164
    • (1992) FEBS Lett. , vol.298 , pp. 162-164
    • Muzzin, P.1    Revelli, J.-P.2    Fraser, C.M.3    Giacobino, J.-P.4
  • 17
    • 0027761394 scopus 로고
    • Structural, and conformational features determining selective signal transduction in the β3-adrenergic receptor
    • Blin N., Camoin L., Maigret B., Strosberg A. D. Structural, and conformational features determining selective signal transduction in the β3-adrenergic receptor. Mol. Pharmacol. 1993; 44: 1094 – 1104
    • (1993) Mol. Pharmacol. , vol.44 , pp. 1094-1104
    • Blin, N.1    Camoin, L.2    Maigret, B.3    Strosberg, A.D.4
  • 20
    • 0003083826 scopus 로고
    • cDNA for the human β2-adrenergic receptor: a protein with multiple membrane-spaning domains and encoded by a gene whose chromosomal location is shared with that of the receptor for platlet-derived growth factor
    • Kobilka B. K., Dixon R. A. F., Frielle T., Dohlman H. G., Bolanowski M. A., Sigal I. S., Yang-Feng T. L., Francke U., Caron M. G., Lefkowitz R. J. cDNA for the human β2-adrenergic receptor: a protein with multiple membrane-spaning domains and encoded by a gene whose chromosomal location is shared with that of the receptor for platlet-derived growth factor. Proc. Natl. Acad. Sci. USA 1987; 84: 46 – 50
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 46-50
    • Kobilka, B.K.1    Dixon, R.A.F.2    Frielle, T.3    Dohlman, H.G.4    Bolanowski, M.A.5    Sigal, I.S.6    Yang-Feng, T.L.7    Francke, U.8    Caron, M.G.9    Lefkowitz, R.J.10
  • 23
    • 0029056440 scopus 로고
    • Differences in desensitization between human β1- and β2-adrenergic receptors stably expressed in transfected hamster cells. Cellular
    • Zhou X.-M., Pak M., Wang Z., Fishman P. H. Differences in desensitization between human β1- and β2-adrenergic receptors stably expressed in transfected hamster cells. Cellular. Signalling 1995; 7: 207 – 217
    • (1995) Signalling , vol.7 , pp. 207-217
    • Zhou, X.-M.1    Pak, M.2    Wang, Z.3    Fishman, P.H.4
  • 24
    • 0025883303 scopus 로고
    • Desensitization of the human β1-adrenergic receptor: involvement of the cyclic AMP-dependent but not a receptor-specific protein kinase
    • Zhou X.-M., Fishman P. H. Desensitization of the human β1-adrenergic receptor: involvement of the cyclic AMP-dependent but not a receptor-specific protein kinase. J. Biol. Chem. 1991; 266: 7462 – 7468
    • (1991) J. Biol. Chem. , vol.266 , pp. 7462-7468
    • Zhou, X.-M.1    Fishman, P.H.2
  • 25
    • 0026021807 scopus 로고
    • Characterization and regulation of β1-adrenergic receptors in a human neuro-epithelioma cell line
    • Fishman P. H., Nussbaum E., Duman R. S. Characterization and regulation of β1-adrenergic receptors in a human neuro-epithelioma cell line. J. Neurochem. 1991; 56: 596 – 602
    • (1991) J. Neurochem. , vol.56 , pp. 596-602
    • Fishman, P.H.1    Nussbaum, E.2    Duman, R.S.3
  • 26
    • 0028068432 scopus 로고
    • Independent and coordinate regulation of β1- and β2-adrenergic receptors in rat C6 glioma cells
    • Fishman P. H., Miller T., Curran P. K., Feussner G. K. Independent and coordinate regulation of β1- and β2-adrenergic receptors in rat C6 glioma cells. J. Receptor Res. 1994; 14: 281 – 296
    • (1994) J. Receptor Res. , vol.14 , pp. 281-296
    • Fishman, P.H.1    Miller, T.2    Curran, P.K.3    Feussner, G.K.4
  • 27
    • 0021737396 scopus 로고
    • Desensitization of catechol-amine-stimulated adenylate cyclase and down-regulation of beta-adrenergic receptors in rat glioma C6 cells: role of cyclic AMP and protein synthesis
    • Zaremba T. G., Fishman P. H. Desensitization of catechol-amine-stimulated adenylate cyclase and down-regulation of beta-adrenergic receptors in rat glioma C6 cells: role of cyclic AMP and protein synthesis. Mol. Pharmacol. 1984; 26: 206 – 213
    • (1984) Mol. Pharmacol. , vol.26 , pp. 206-213
    • Zaremba, T.G.1    Fishman, P.H.2
  • 28
    • 0023637429 scopus 로고
    • The role of a low β1-adrenoceptor selectivity of [3H]CGP-12177 for resolving subtype-selectivity of competitive ligands
    • Nanoff C., Freissmuth M., Schβtz W. The role of a low β1-adrenoceptor selectivity of [3H]CGP-12177 for resolving subtype-selectivity of competitive ligands. Naunyn Schmiedeberg's Arch. Pharmacol. 1987; 336: 519 – 525
    • (1987) Naunyn Schmiedeberg's Arch. Pharmacol. , vol.336 , pp. 519-525
    • Nanoff, C.1    Freissmuth, M.2    Schβtz, W.3
  • 29
    • 0022017322 scopus 로고
    • (-)-S-[3H]CGP-12177 and its use to determine the rate constants of unlabeled β-adrenergic antagonists
    • Affolter H., Hertel C., Jaeggi K., Portenier M., Staehlin M. (-)-S-[3H]CGP-12177 and its use to determine the rate constants of unlabeled β-adrenergic antagonists. Proc. Natl. Acad. Sci. USA 1985; 83: 925 – 929
    • (1985) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 925-929
    • Affolter, H.1    Hertel, C.2    Jaeggi, K.3    Portenier, M.4    Staehlin, M.5
  • 30
    • 0027283546 scopus 로고
    • Partial agonist, full agonist, antagonists: dilemmas of definition
    • Hoyer D., Boddeke H. W.G. M. Partial agonist, full agonist, antagonists: dilemmas of definition. Trends Pharmacol. Sci. 1993; 14: 270 – 275
    • (1993) Trends Pharmacol. Sci. , vol.14 , pp. 270-275
    • Hoyer, D.1    Boddeke, H.W.G.M.2
  • 31
    • 0028030774 scopus 로고
    • Dual signaling potential is common among Gs-coupled receptors and dependent on receptor density
    • Zhu X., Gilbert S., Birnbaumer M., Birmbaumer L. Dual signaling potential is common among Gs-coupled receptors and dependent on receptor density. Mol. Pharmacol. 1994; 46: 460 – 469
    • (1994) Mol. Pharmacol. , vol.46 , pp. 460-469
    • Zhu, X.1    Gilbert, S.2    Birnbaumer, M.3    Birmbaumer, L.4
  • 32
    • 0029061611 scopus 로고
    • Agonist-receptor efficacy I: mechanisms of efficacy and receptor promiscuity
    • Kenakin T. P. Agonist-receptor efficacy I: mechanisms of efficacy and receptor promiscuity. Trends Pharmacol. Sci. 1995; 16: 188 – 192
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 188-192
    • Kenakin, T.P.1
  • 33
    • 0029054965 scopus 로고
    • Agonist-receptor efficacy I: agonist trafficking of receptor signals
    • Kenakin T. P. Agonist-receptor efficacy I: agonist trafficking of receptor signals. Trends Pharmacol. Sci. 1995; 16: 232 – 238
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 232-238
    • Kenakin, T.P.1
  • 34
    • 0027732228 scopus 로고
    • Close reciprocal regulation of β1- and β2-adrenergic receptors by dexamethasone in C6glioma cells: effects on catecholamine responsiveness
    • Zhong H., Minneman K. P. Close reciprocal regulation of β1- and β2-adrenergic receptors by dexamethasone in C6glioma cells: effects on catecholamine responsiveness. Mol. Pharmacol. 1993; 44: 1085 – 1093
    • (1993) Mol. Pharmacol. , vol.44 , pp. 1085-1093
    • Zhong, H.1    Minneman, K.P.2
  • 35
    • 0025174187 scopus 로고
    • Amplification of cyclic AMP generation reveals agonistic effects of certain β-adrenergic antagonists
    • Jasper J. R., Michel M. C., Insel P. A. Amplification of cyclic AMP generation reveals agonistic effects of certain β-adrenergic antagonists. Mol. Pharmacol. 1990; 37: 44 – 49
    • (1990) Mol. Pharmacol. , vol.37 , pp. 44-49
    • Jasper, J.R.1    Michel, M.C.2    Insel, P.A.3
  • 36
    • 0023906198 scopus 로고
    • The β2-adrenergic receptors of human epidermoid carcinoma cells bear two different types of oligosaccharides which influence expression on the cell surface
    • Cervantes-Olivier P., Delavier-Klutchko C., Durieu-Trautmann O., Kaveri S., Desmandril M., Strosberg A. D. The β2-adrenergic receptors of human epidermoid carcinoma cells bear two different types of oligosaccharides which influence expression on the cell surface. Biochem. J. 1988; 250: 133 – 143
    • (1988) Biochem. J. , vol.250 , pp. 133-143
    • Cervantes-Olivier, P.1    Delavier-Klutchko, C.2    Durieu-Trautmann, O.3    Kaveri, S.4    Desmandril, M.5    Strosberg, A.D.6
  • 37
    • 0023930678 scopus 로고
    • Role of glycosylation for β2-adrenoceptor function in A431 cells
    • Boege F., Ward M., Jβrss R., Hekman M., Helmreich E. J. M. Role of glycosylation for β2-adrenoceptor function in A431 cells. J. Biol. Chem. 1988; 263: 9040 – 9049
    • (1988) J. Biol. Chem. , vol.263 , pp. 9040-9049
    • Boege, F.1    Ward, M.2    Jβrss, R.3    Hekman, M.4    Helmreich, E.J.M.5
  • 38
    • 0024544232 scopus 로고
    • Palmitoylation of the human β2-adrenergic receptor. Mutation of Cys341in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor
    • O'Dowd B. F., Hnatowich M., Caron M. G., Lefkowitz R. J., Bouvier M. Palmitoylation of the human β2-adrenergic receptor. Mutation of Cys341in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor. J. Biol. Chem. 1989; 264: 7564 – 7569
    • (1989) J. Biol. Chem. , vol.264 , pp. 7564-7569
    • O'Dowd, B.F.1    Hnatowich, M.2    Caron, M.G.3    Lefkowitz, R.J.4    Bouvier, M.5
  • 39
    • 0021194782 scopus 로고
    • Activation of the inhibitory GTP-binding protein of adenylate cyclase, G1by β-adrenergic receptors in reconstituted phsopholipids vesicles
    • Asano T., Katada T., Gilman A. G., Ross E. M. Activation of the inhibitory GTP-binding protein of adenylate cyclase, G1by β-adrenergic receptors in reconstituted phsopholipids vesicles. J. Biol. Chem. 1984; 259: 9351 – 9354
    • (1984) J. Biol. Chem. , vol.259 , pp. 9351-9354
    • Asano, T.1    Katada, T.2    Gilman, A.G.3    Ross, E.M.4
  • 41
    • 0019137579 scopus 로고
    • A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-adrenergic receptor
    • DeLean A., Stadel J. M., Lefkowitz R. J. A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-adrenergic receptor. J. Biol. Chem. 1980; 255: 7108 – 7117
    • (1980) J. Biol. Chem. , vol.255 , pp. 7108-7117
    • DeLean, A.1    Stadel, J.M.2    Lefkowitz, R.J.3
  • 42
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the β2-adrenergic receptor. Extending the ternary complex model
    • Samama P., Cotecchia S., Costa T., Lefkowitz R. J. A mutation-induced activated state of the β2-adrenergic receptor. Extending the ternary complex model. J. Biol. Chem. 1993; 268: 4625 – 4636
    • (1993) J. Biol. Chem. , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 44
    • 0027936892 scopus 로고
    • Membrane organization in G-protein mechanisms
    • Neubig R. R. Membrane organization in G-protein mechanisms. FASEB J. 1994; 8: 939 – 946
    • (1994) FASEB J. , vol.8 , pp. 939-946
    • Neubig, R.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.