Desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline
Summary Rats pretreated with 1-acetyl-2-phenylhydrazide, to induce reticulocytosis, were treated with (±)isoprenaline (4×30 mg/kg in 6 h intervals within 24 h before blood sampling) in order to desensitize the β-adrenoceptor-adenylate cyclase-system of circulating red cells. 1. In membrane preparati...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1981 |
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| Umfang: |
8 |
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| Reproduktion: |
Springer Online Journal Archives 1860-2002 |
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| Übergeordnetes Werk: |
in: Naunyn-Schmiedeberg's archives of pharmacology - 1873, 317(1981) vom: Apr., Seite 294-301 |
| Übergeordnetes Werk: |
volume:317 ; year:1981 ; month:04 ; pages:294-301 ; extent:8 |
| Links: |
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NLEJ200609351 |
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| 245 | 1 | 0 | |a Desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline |
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| 520 | |a Summary Rats pretreated with 1-acetyl-2-phenylhydrazide, to induce reticulocytosis, were treated with (±)isoprenaline (4×30 mg/kg in 6 h intervals within 24 h before blood sampling) in order to desensitize the β-adrenoceptor-adenylate cyclase-system of circulating red cells. 1. In membrane preparations Vmax-values of (-)isoprenaline-sensitive adenylate cyclase activity declined by about 50% without significant alterations of the apparent K m-values. Basal activity, as well as enzyme activity stimulated maximally by guanylyl-imidodiphosphate and by fluoride were also decreased to the same extent. 2. In intact cells, maximal synthesis of cAMP stimulated by 10−5 M (-)isoprenaline was decreased by about 50% compared to cell suspensions from control animals in the presence of Ro 20-1724 or papaverine, inhibitors of phosphodiesterase. Without inhibition of phosphodiesterase, (-)isoprenaline stimulated cAMP synthesis in cell suspensions from desensitized animals exceeded that from control animals more than 10-fold. A 20–30% decrease of phosphodiesterase activity, measured in membrane and cytoplasmic fractions explains this unexpected result. 3. In membrane preparations from untreated animals, Bmax-values for the antagonist ligand [3H] dihydroalprenolol ([3H] DHA) were (0.98±0.16 pmoles/mg protein (n=7). For the agonist-ligand [3H] hydroxybenzylisoprenaline ([3H]-HBI) only 0.23±0.024 pmoles/mg protein (n=12) were obtained. After pretreatment of the animals with (±)isoprenaline, the Bmax-value for [3H] HBI was decreased by about 50%; whereas, that for [3H] DHA was decreased only by about 10%. No change in K D-values for both ligands occurred. 4. It is proposed that β-adrenergic desensitization in immature red cells, i.e. the decrease of (-)isoprenalinesensitive adenylate cyclase activity, results from loss of high affinity β-adrenoceptor sites. This might be induced by uncoupling the adrenoceptors from the nucleotide binding protein. A functional impairment or loss of this regulatory protein may be responsible for the apparent loss of adenylate cyclase activity. Since [3H] HBI, in contrast to [3H] DHA, labels predominantly β-adrenoceptors in the high affinity state it is a more sensitive marker to detect alterations at the adrenoceptor level following desensitization. | ||
| 533 | |f Springer Online Journal Archives 1860-2002 | ||
| 700 | 1 | |a Wiemer, G. |4 oth | |
| 700 | 1 | |a Kaiser, G. |4 oth | |
| 700 | 1 | |a Dietz, J. |4 oth | |
| 700 | 1 | |a Reinhardt, M. |4 oth | |
| 700 | 1 | |a Wellstein, A. |4 oth | |
| 700 | 1 | |a Palm, D. |4 oth | |
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(DE-627)NLEJ200609351 DE-627 ger DE-627 rakwb eng Desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline 1981 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Rats pretreated with 1-acetyl-2-phenylhydrazide, to induce reticulocytosis, were treated with (±)isoprenaline (4×30 mg/kg in 6 h intervals within 24 h before blood sampling) in order to desensitize the β-adrenoceptor-adenylate cyclase-system of circulating red cells. 1. In membrane preparations Vmax-values of (-)isoprenaline-sensitive adenylate cyclase activity declined by about 50% without significant alterations of the apparent K m-values. Basal activity, as well as enzyme activity stimulated maximally by guanylyl-imidodiphosphate and by fluoride were also decreased to the same extent. 2. In intact cells, maximal synthesis of cAMP stimulated by 10−5 M (-)isoprenaline was decreased by about 50% compared to cell suspensions from control animals in the presence of Ro 20-1724 or papaverine, inhibitors of phosphodiesterase. Without inhibition of phosphodiesterase, (-)isoprenaline stimulated cAMP synthesis in cell suspensions from desensitized animals exceeded that from control animals more than 10-fold. A 20–30% decrease of phosphodiesterase activity, measured in membrane and cytoplasmic fractions explains this unexpected result. 3. In membrane preparations from untreated animals, Bmax-values for the antagonist ligand [3H] dihydroalprenolol ([3H] DHA) were (0.98±0.16 pmoles/mg protein (n=7). For the agonist-ligand [3H] hydroxybenzylisoprenaline ([3H]-HBI) only 0.23±0.024 pmoles/mg protein (n=12) were obtained. After pretreatment of the animals with (±)isoprenaline, the Bmax-value for [3H] HBI was decreased by about 50%; whereas, that for [3H] DHA was decreased only by about 10%. No change in K D-values for both ligands occurred. 4. It is proposed that β-adrenergic desensitization in immature red cells, i.e. the decrease of (-)isoprenalinesensitive adenylate cyclase activity, results from loss of high affinity β-adrenoceptor sites. This might be induced by uncoupling the adrenoceptors from the nucleotide binding protein. A functional impairment or loss of this regulatory protein may be responsible for the apparent loss of adenylate cyclase activity. Since [3H] HBI, in contrast to [3H] DHA, labels predominantly β-adrenoceptors in the high affinity state it is a more sensitive marker to detect alterations at the adrenoceptor level following desensitization. Springer Online Journal Archives 1860-2002 Wiemer, G. oth Kaiser, G. oth Dietz, J. oth Reinhardt, M. oth Wellstein, A. oth Palm, D. oth in Naunyn-Schmiedeberg's archives of pharmacology 1873 317(1981) vom: Apr., Seite 294-301 (DE-627)NLEJ188984607 (DE-600)1462940-9 1432-1912 nnns volume:317 year:1981 month:04 pages:294-301 extent:8 http://dx.doi.org/10.1007/BF00501309 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 317 1981 4 294-301 8 |
| spelling |
(DE-627)NLEJ200609351 DE-627 ger DE-627 rakwb eng Desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline 1981 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Rats pretreated with 1-acetyl-2-phenylhydrazide, to induce reticulocytosis, were treated with (±)isoprenaline (4×30 mg/kg in 6 h intervals within 24 h before blood sampling) in order to desensitize the β-adrenoceptor-adenylate cyclase-system of circulating red cells. 1. In membrane preparations Vmax-values of (-)isoprenaline-sensitive adenylate cyclase activity declined by about 50% without significant alterations of the apparent K m-values. Basal activity, as well as enzyme activity stimulated maximally by guanylyl-imidodiphosphate and by fluoride were also decreased to the same extent. 2. In intact cells, maximal synthesis of cAMP stimulated by 10−5 M (-)isoprenaline was decreased by about 50% compared to cell suspensions from control animals in the presence of Ro 20-1724 or papaverine, inhibitors of phosphodiesterase. Without inhibition of phosphodiesterase, (-)isoprenaline stimulated cAMP synthesis in cell suspensions from desensitized animals exceeded that from control animals more than 10-fold. A 20–30% decrease of phosphodiesterase activity, measured in membrane and cytoplasmic fractions explains this unexpected result. 3. In membrane preparations from untreated animals, Bmax-values for the antagonist ligand [3H] dihydroalprenolol ([3H] DHA) were (0.98±0.16 pmoles/mg protein (n=7). For the agonist-ligand [3H] hydroxybenzylisoprenaline ([3H]-HBI) only 0.23±0.024 pmoles/mg protein (n=12) were obtained. After pretreatment of the animals with (±)isoprenaline, the Bmax-value for [3H] HBI was decreased by about 50%; whereas, that for [3H] DHA was decreased only by about 10%. No change in K D-values for both ligands occurred. 4. It is proposed that β-adrenergic desensitization in immature red cells, i.e. the decrease of (-)isoprenalinesensitive adenylate cyclase activity, results from loss of high affinity β-adrenoceptor sites. This might be induced by uncoupling the adrenoceptors from the nucleotide binding protein. A functional impairment or loss of this regulatory protein may be responsible for the apparent loss of adenylate cyclase activity. Since [3H] HBI, in contrast to [3H] DHA, labels predominantly β-adrenoceptors in the high affinity state it is a more sensitive marker to detect alterations at the adrenoceptor level following desensitization. Springer Online Journal Archives 1860-2002 Wiemer, G. oth Kaiser, G. oth Dietz, J. oth Reinhardt, M. oth Wellstein, A. oth Palm, D. oth in Naunyn-Schmiedeberg's archives of pharmacology 1873 317(1981) vom: Apr., Seite 294-301 (DE-627)NLEJ188984607 (DE-600)1462940-9 1432-1912 nnns volume:317 year:1981 month:04 pages:294-301 extent:8 http://dx.doi.org/10.1007/BF00501309 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 317 1981 4 294-301 8 |
| allfields_unstemmed |
(DE-627)NLEJ200609351 DE-627 ger DE-627 rakwb eng Desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline 1981 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Rats pretreated with 1-acetyl-2-phenylhydrazide, to induce reticulocytosis, were treated with (±)isoprenaline (4×30 mg/kg in 6 h intervals within 24 h before blood sampling) in order to desensitize the β-adrenoceptor-adenylate cyclase-system of circulating red cells. 1. In membrane preparations Vmax-values of (-)isoprenaline-sensitive adenylate cyclase activity declined by about 50% without significant alterations of the apparent K m-values. Basal activity, as well as enzyme activity stimulated maximally by guanylyl-imidodiphosphate and by fluoride were also decreased to the same extent. 2. In intact cells, maximal synthesis of cAMP stimulated by 10−5 M (-)isoprenaline was decreased by about 50% compared to cell suspensions from control animals in the presence of Ro 20-1724 or papaverine, inhibitors of phosphodiesterase. Without inhibition of phosphodiesterase, (-)isoprenaline stimulated cAMP synthesis in cell suspensions from desensitized animals exceeded that from control animals more than 10-fold. A 20–30% decrease of phosphodiesterase activity, measured in membrane and cytoplasmic fractions explains this unexpected result. 3. In membrane preparations from untreated animals, Bmax-values for the antagonist ligand [3H] dihydroalprenolol ([3H] DHA) were (0.98±0.16 pmoles/mg protein (n=7). For the agonist-ligand [3H] hydroxybenzylisoprenaline ([3H]-HBI) only 0.23±0.024 pmoles/mg protein (n=12) were obtained. After pretreatment of the animals with (±)isoprenaline, the Bmax-value for [3H] HBI was decreased by about 50%; whereas, that for [3H] DHA was decreased only by about 10%. No change in K D-values for both ligands occurred. 4. It is proposed that β-adrenergic desensitization in immature red cells, i.e. the decrease of (-)isoprenalinesensitive adenylate cyclase activity, results from loss of high affinity β-adrenoceptor sites. This might be induced by uncoupling the adrenoceptors from the nucleotide binding protein. A functional impairment or loss of this regulatory protein may be responsible for the apparent loss of adenylate cyclase activity. Since [3H] HBI, in contrast to [3H] DHA, labels predominantly β-adrenoceptors in the high affinity state it is a more sensitive marker to detect alterations at the adrenoceptor level following desensitization. Springer Online Journal Archives 1860-2002 Wiemer, G. oth Kaiser, G. oth Dietz, J. oth Reinhardt, M. oth Wellstein, A. oth Palm, D. oth in Naunyn-Schmiedeberg's archives of pharmacology 1873 317(1981) vom: Apr., Seite 294-301 (DE-627)NLEJ188984607 (DE-600)1462940-9 1432-1912 nnns volume:317 year:1981 month:04 pages:294-301 extent:8 http://dx.doi.org/10.1007/BF00501309 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 317 1981 4 294-301 8 |
| allfieldsGer |
(DE-627)NLEJ200609351 DE-627 ger DE-627 rakwb eng Desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline 1981 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Rats pretreated with 1-acetyl-2-phenylhydrazide, to induce reticulocytosis, were treated with (±)isoprenaline (4×30 mg/kg in 6 h intervals within 24 h before blood sampling) in order to desensitize the β-adrenoceptor-adenylate cyclase-system of circulating red cells. 1. In membrane preparations Vmax-values of (-)isoprenaline-sensitive adenylate cyclase activity declined by about 50% without significant alterations of the apparent K m-values. Basal activity, as well as enzyme activity stimulated maximally by guanylyl-imidodiphosphate and by fluoride were also decreased to the same extent. 2. In intact cells, maximal synthesis of cAMP stimulated by 10−5 M (-)isoprenaline was decreased by about 50% compared to cell suspensions from control animals in the presence of Ro 20-1724 or papaverine, inhibitors of phosphodiesterase. Without inhibition of phosphodiesterase, (-)isoprenaline stimulated cAMP synthesis in cell suspensions from desensitized animals exceeded that from control animals more than 10-fold. A 20–30% decrease of phosphodiesterase activity, measured in membrane and cytoplasmic fractions explains this unexpected result. 3. In membrane preparations from untreated animals, Bmax-values for the antagonist ligand [3H] dihydroalprenolol ([3H] DHA) were (0.98±0.16 pmoles/mg protein (n=7). For the agonist-ligand [3H] hydroxybenzylisoprenaline ([3H]-HBI) only 0.23±0.024 pmoles/mg protein (n=12) were obtained. After pretreatment of the animals with (±)isoprenaline, the Bmax-value for [3H] HBI was decreased by about 50%; whereas, that for [3H] DHA was decreased only by about 10%. No change in K D-values for both ligands occurred. 4. It is proposed that β-adrenergic desensitization in immature red cells, i.e. the decrease of (-)isoprenalinesensitive adenylate cyclase activity, results from loss of high affinity β-adrenoceptor sites. This might be induced by uncoupling the adrenoceptors from the nucleotide binding protein. A functional impairment or loss of this regulatory protein may be responsible for the apparent loss of adenylate cyclase activity. Since [3H] HBI, in contrast to [3H] DHA, labels predominantly β-adrenoceptors in the high affinity state it is a more sensitive marker to detect alterations at the adrenoceptor level following desensitization. Springer Online Journal Archives 1860-2002 Wiemer, G. oth Kaiser, G. oth Dietz, J. oth Reinhardt, M. oth Wellstein, A. oth Palm, D. oth in Naunyn-Schmiedeberg's archives of pharmacology 1873 317(1981) vom: Apr., Seite 294-301 (DE-627)NLEJ188984607 (DE-600)1462940-9 1432-1912 nnns volume:317 year:1981 month:04 pages:294-301 extent:8 http://dx.doi.org/10.1007/BF00501309 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 317 1981 4 294-301 8 |
| allfieldsSound |
(DE-627)NLEJ200609351 DE-627 ger DE-627 rakwb eng Desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline 1981 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Rats pretreated with 1-acetyl-2-phenylhydrazide, to induce reticulocytosis, were treated with (±)isoprenaline (4×30 mg/kg in 6 h intervals within 24 h before blood sampling) in order to desensitize the β-adrenoceptor-adenylate cyclase-system of circulating red cells. 1. In membrane preparations Vmax-values of (-)isoprenaline-sensitive adenylate cyclase activity declined by about 50% without significant alterations of the apparent K m-values. Basal activity, as well as enzyme activity stimulated maximally by guanylyl-imidodiphosphate and by fluoride were also decreased to the same extent. 2. In intact cells, maximal synthesis of cAMP stimulated by 10−5 M (-)isoprenaline was decreased by about 50% compared to cell suspensions from control animals in the presence of Ro 20-1724 or papaverine, inhibitors of phosphodiesterase. Without inhibition of phosphodiesterase, (-)isoprenaline stimulated cAMP synthesis in cell suspensions from desensitized animals exceeded that from control animals more than 10-fold. A 20–30% decrease of phosphodiesterase activity, measured in membrane and cytoplasmic fractions explains this unexpected result. 3. In membrane preparations from untreated animals, Bmax-values for the antagonist ligand [3H] dihydroalprenolol ([3H] DHA) were (0.98±0.16 pmoles/mg protein (n=7). For the agonist-ligand [3H] hydroxybenzylisoprenaline ([3H]-HBI) only 0.23±0.024 pmoles/mg protein (n=12) were obtained. After pretreatment of the animals with (±)isoprenaline, the Bmax-value for [3H] HBI was decreased by about 50%; whereas, that for [3H] DHA was decreased only by about 10%. No change in K D-values for both ligands occurred. 4. It is proposed that β-adrenergic desensitization in immature red cells, i.e. the decrease of (-)isoprenalinesensitive adenylate cyclase activity, results from loss of high affinity β-adrenoceptor sites. This might be induced by uncoupling the adrenoceptors from the nucleotide binding protein. A functional impairment or loss of this regulatory protein may be responsible for the apparent loss of adenylate cyclase activity. Since [3H] HBI, in contrast to [3H] DHA, labels predominantly β-adrenoceptors in the high affinity state it is a more sensitive marker to detect alterations at the adrenoceptor level following desensitization. Springer Online Journal Archives 1860-2002 Wiemer, G. oth Kaiser, G. oth Dietz, J. oth Reinhardt, M. oth Wellstein, A. oth Palm, D. oth in Naunyn-Schmiedeberg's archives of pharmacology 1873 317(1981) vom: Apr., Seite 294-301 (DE-627)NLEJ188984607 (DE-600)1462940-9 1432-1912 nnns volume:317 year:1981 month:04 pages:294-301 extent:8 http://dx.doi.org/10.1007/BF00501309 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 317 1981 4 294-301 8 |
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In membrane preparations Vmax-values of (-)isoprenaline-sensitive adenylate cyclase activity declined by about 50% without significant alterations of the apparent K m-values. Basal activity, as well as enzyme activity stimulated maximally by guanylyl-imidodiphosphate and by fluoride were also decreased to the same extent. 2. In intact cells, maximal synthesis of cAMP stimulated by 10−5 M (-)isoprenaline was decreased by about 50% compared to cell suspensions from control animals in the presence of Ro 20-1724 or papaverine, inhibitors of phosphodiesterase. Without inhibition of phosphodiesterase, (-)isoprenaline stimulated cAMP synthesis in cell suspensions from desensitized animals exceeded that from control animals more than 10-fold. A 20–30% decrease of phosphodiesterase activity, measured in membrane and cytoplasmic fractions explains this unexpected result. 3. 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Desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline |
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Desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline |
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Desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline |
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(DE-627)NLEJ200609351 |
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Desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline |
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1981 |
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Elektronische Aufsätze |
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desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline |
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Desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline |
| abstract |
Summary Rats pretreated with 1-acetyl-2-phenylhydrazide, to induce reticulocytosis, were treated with (±)isoprenaline (4×30 mg/kg in 6 h intervals within 24 h before blood sampling) in order to desensitize the β-adrenoceptor-adenylate cyclase-system of circulating red cells. 1. In membrane preparations Vmax-values of (-)isoprenaline-sensitive adenylate cyclase activity declined by about 50% without significant alterations of the apparent K m-values. Basal activity, as well as enzyme activity stimulated maximally by guanylyl-imidodiphosphate and by fluoride were also decreased to the same extent. 2. In intact cells, maximal synthesis of cAMP stimulated by 10−5 M (-)isoprenaline was decreased by about 50% compared to cell suspensions from control animals in the presence of Ro 20-1724 or papaverine, inhibitors of phosphodiesterase. Without inhibition of phosphodiesterase, (-)isoprenaline stimulated cAMP synthesis in cell suspensions from desensitized animals exceeded that from control animals more than 10-fold. A 20–30% decrease of phosphodiesterase activity, measured in membrane and cytoplasmic fractions explains this unexpected result. 3. In membrane preparations from untreated animals, Bmax-values for the antagonist ligand [3H] dihydroalprenolol ([3H] DHA) were (0.98±0.16 pmoles/mg protein (n=7). For the agonist-ligand [3H] hydroxybenzylisoprenaline ([3H]-HBI) only 0.23±0.024 pmoles/mg protein (n=12) were obtained. After pretreatment of the animals with (±)isoprenaline, the Bmax-value for [3H] HBI was decreased by about 50%; whereas, that for [3H] DHA was decreased only by about 10%. No change in K D-values for both ligands occurred. 4. It is proposed that β-adrenergic desensitization in immature red cells, i.e. the decrease of (-)isoprenalinesensitive adenylate cyclase activity, results from loss of high affinity β-adrenoceptor sites. This might be induced by uncoupling the adrenoceptors from the nucleotide binding protein. A functional impairment or loss of this regulatory protein may be responsible for the apparent loss of adenylate cyclase activity. Since [3H] HBI, in contrast to [3H] DHA, labels predominantly β-adrenoceptors in the high affinity state it is a more sensitive marker to detect alterations at the adrenoceptor level following desensitization. |
| abstractGer |
Summary Rats pretreated with 1-acetyl-2-phenylhydrazide, to induce reticulocytosis, were treated with (±)isoprenaline (4×30 mg/kg in 6 h intervals within 24 h before blood sampling) in order to desensitize the β-adrenoceptor-adenylate cyclase-system of circulating red cells. 1. In membrane preparations Vmax-values of (-)isoprenaline-sensitive adenylate cyclase activity declined by about 50% without significant alterations of the apparent K m-values. Basal activity, as well as enzyme activity stimulated maximally by guanylyl-imidodiphosphate and by fluoride were also decreased to the same extent. 2. In intact cells, maximal synthesis of cAMP stimulated by 10−5 M (-)isoprenaline was decreased by about 50% compared to cell suspensions from control animals in the presence of Ro 20-1724 or papaverine, inhibitors of phosphodiesterase. Without inhibition of phosphodiesterase, (-)isoprenaline stimulated cAMP synthesis in cell suspensions from desensitized animals exceeded that from control animals more than 10-fold. A 20–30% decrease of phosphodiesterase activity, measured in membrane and cytoplasmic fractions explains this unexpected result. 3. In membrane preparations from untreated animals, Bmax-values for the antagonist ligand [3H] dihydroalprenolol ([3H] DHA) were (0.98±0.16 pmoles/mg protein (n=7). For the agonist-ligand [3H] hydroxybenzylisoprenaline ([3H]-HBI) only 0.23±0.024 pmoles/mg protein (n=12) were obtained. After pretreatment of the animals with (±)isoprenaline, the Bmax-value for [3H] HBI was decreased by about 50%; whereas, that for [3H] DHA was decreased only by about 10%. No change in K D-values for both ligands occurred. 4. It is proposed that β-adrenergic desensitization in immature red cells, i.e. the decrease of (-)isoprenalinesensitive adenylate cyclase activity, results from loss of high affinity β-adrenoceptor sites. This might be induced by uncoupling the adrenoceptors from the nucleotide binding protein. A functional impairment or loss of this regulatory protein may be responsible for the apparent loss of adenylate cyclase activity. Since [3H] HBI, in contrast to [3H] DHA, labels predominantly β-adrenoceptors in the high affinity state it is a more sensitive marker to detect alterations at the adrenoceptor level following desensitization. |
| abstract_unstemmed |
Summary Rats pretreated with 1-acetyl-2-phenylhydrazide, to induce reticulocytosis, were treated with (±)isoprenaline (4×30 mg/kg in 6 h intervals within 24 h before blood sampling) in order to desensitize the β-adrenoceptor-adenylate cyclase-system of circulating red cells. 1. In membrane preparations Vmax-values of (-)isoprenaline-sensitive adenylate cyclase activity declined by about 50% without significant alterations of the apparent K m-values. Basal activity, as well as enzyme activity stimulated maximally by guanylyl-imidodiphosphate and by fluoride were also decreased to the same extent. 2. In intact cells, maximal synthesis of cAMP stimulated by 10−5 M (-)isoprenaline was decreased by about 50% compared to cell suspensions from control animals in the presence of Ro 20-1724 or papaverine, inhibitors of phosphodiesterase. Without inhibition of phosphodiesterase, (-)isoprenaline stimulated cAMP synthesis in cell suspensions from desensitized animals exceeded that from control animals more than 10-fold. A 20–30% decrease of phosphodiesterase activity, measured in membrane and cytoplasmic fractions explains this unexpected result. 3. In membrane preparations from untreated animals, Bmax-values for the antagonist ligand [3H] dihydroalprenolol ([3H] DHA) were (0.98±0.16 pmoles/mg protein (n=7). For the agonist-ligand [3H] hydroxybenzylisoprenaline ([3H]-HBI) only 0.23±0.024 pmoles/mg protein (n=12) were obtained. After pretreatment of the animals with (±)isoprenaline, the Bmax-value for [3H] HBI was decreased by about 50%; whereas, that for [3H] DHA was decreased only by about 10%. No change in K D-values for both ligands occurred. 4. It is proposed that β-adrenergic desensitization in immature red cells, i.e. the decrease of (-)isoprenalinesensitive adenylate cyclase activity, results from loss of high affinity β-adrenoceptor sites. This might be induced by uncoupling the adrenoceptors from the nucleotide binding protein. A functional impairment or loss of this regulatory protein may be responsible for the apparent loss of adenylate cyclase activity. Since [3H] HBI, in contrast to [3H] DHA, labels predominantly β-adrenoceptors in the high affinity state it is a more sensitive marker to detect alterations at the adrenoceptor level following desensitization. |
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Desensitization of the β-adrenoceptor-adenylate cyclase system of immature erythrocytes by in-vivo treatment of rats with isoprenaline |
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Wiemer, G. Kaiser, G. Dietz, J. Reinhardt, M. Wellstein, A. Palm, D. |
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