No Role for Phospholipase A2 and Protein Kinase C in the Potentiation by α-Adrenoceptors of β-Adrenoceptor-Mediated Cyclic AMP Formation in Rat Brain
Abstract: This study was undertaken to examine the role of phospholipase A2 and protein kinase C in the potentiation of β-adrenoceptor-mediated cyclic AMP formation by α-ad-renoceptors in rat cerebral cortical slices. Inhibition of ara-chidonic acid metabolism by a range of cyclooxygenase and lipoxy...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Robinson, Jean P. [verfasserIn] Kendall, David A. [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1989 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 53(1989), 2, Seite 0 |
| Übergeordnetes Werk: |
volume:53 ; year:1989 ; number:2 ; pages:0 |
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| DOI / URN: |
10.1111/j.1471-4159.1989.tb07367.x |
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| 520 | |a Abstract: This study was undertaken to examine the role of phospholipase A2 and protein kinase C in the potentiation of β-adrenoceptor-mediated cyclic AMP formation by α-ad-renoceptors in rat cerebral cortical slices. Inhibition of ara-chidonic acid metabolism by a range of cyclooxygenase and lipoxygenase inhibitors had no effect on the potentiation of isoprenaline-stimulated cyclic AMP. Conversely, stimulation of leukotriene formation had no effect on the response to isoprenaline. The phospholipase A2 activator, melittin, stimulated cyclic AMP and potentiated the effect of isoprenaline, but these responses were not influenced by cyclooxygenase or lipoxygenase inhibitors. Indomethacin was also ineffective against the potentiation of vasoactive intestinal peptide-stimulated cyclic AMP by noradrenaline. Phorbol ester potentiated the cyclic AMP response to isoprenaline, and this potentiation was antagonized by three different putative protein kinase C inhibitors. However, the same inhibitors did not affect the α-adrenoceptor-stimulated enhancement of the response to isoprenaline. We have found no evidence, therefore, to support the suggestion that arachidonic acid and its metabolites and/or protein kinase C mediate the α-adreno-ceptor modulation of β-adrenoceptor function. | ||
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10.1111/j.1471-4159.1989.tb07367.x doi (DE-627)NLEJ240274466 DE-627 ger DE-627 rakwb Robinson, Jean P. verfasserin aut No Role for Phospholipase A2 and Protein Kinase C in the Potentiation by α-Adrenoceptors of β-Adrenoceptor-Mediated Cyclic AMP Formation in Rat Brain Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: This study was undertaken to examine the role of phospholipase A2 and protein kinase C in the potentiation of β-adrenoceptor-mediated cyclic AMP formation by α-ad-renoceptors in rat cerebral cortical slices. Inhibition of ara-chidonic acid metabolism by a range of cyclooxygenase and lipoxygenase inhibitors had no effect on the potentiation of isoprenaline-stimulated cyclic AMP. Conversely, stimulation of leukotriene formation had no effect on the response to isoprenaline. The phospholipase A2 activator, melittin, stimulated cyclic AMP and potentiated the effect of isoprenaline, but these responses were not influenced by cyclooxygenase or lipoxygenase inhibitors. Indomethacin was also ineffective against the potentiation of vasoactive intestinal peptide-stimulated cyclic AMP by noradrenaline. Phorbol ester potentiated the cyclic AMP response to isoprenaline, and this potentiation was antagonized by three different putative protein kinase C inhibitors. However, the same inhibitors did not affect the α-adrenoceptor-stimulated enhancement of the response to isoprenaline. We have found no evidence, therefore, to support the suggestion that arachidonic acid and its metabolites and/or protein kinase C mediate the α-adreno-ceptor modulation of β-adrenoceptor function. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| α-Adrenoceptors Kendall, David A. verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 53(1989), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:53 year:1989 number:2 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1989.tb07367.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 53 1989 2 0 |
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10.1111/j.1471-4159.1989.tb07367.x doi (DE-627)NLEJ240274466 DE-627 ger DE-627 rakwb Robinson, Jean P. verfasserin aut No Role for Phospholipase A2 and Protein Kinase C in the Potentiation by α-Adrenoceptors of β-Adrenoceptor-Mediated Cyclic AMP Formation in Rat Brain Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: This study was undertaken to examine the role of phospholipase A2 and protein kinase C in the potentiation of β-adrenoceptor-mediated cyclic AMP formation by α-ad-renoceptors in rat cerebral cortical slices. Inhibition of ara-chidonic acid metabolism by a range of cyclooxygenase and lipoxygenase inhibitors had no effect on the potentiation of isoprenaline-stimulated cyclic AMP. Conversely, stimulation of leukotriene formation had no effect on the response to isoprenaline. The phospholipase A2 activator, melittin, stimulated cyclic AMP and potentiated the effect of isoprenaline, but these responses were not influenced by cyclooxygenase or lipoxygenase inhibitors. Indomethacin was also ineffective against the potentiation of vasoactive intestinal peptide-stimulated cyclic AMP by noradrenaline. Phorbol ester potentiated the cyclic AMP response to isoprenaline, and this potentiation was antagonized by three different putative protein kinase C inhibitors. However, the same inhibitors did not affect the α-adrenoceptor-stimulated enhancement of the response to isoprenaline. We have found no evidence, therefore, to support the suggestion that arachidonic acid and its metabolites and/or protein kinase C mediate the α-adreno-ceptor modulation of β-adrenoceptor function. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| α-Adrenoceptors Kendall, David A. verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 53(1989), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:53 year:1989 number:2 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1989.tb07367.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 53 1989 2 0 |
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10.1111/j.1471-4159.1989.tb07367.x doi (DE-627)NLEJ240274466 DE-627 ger DE-627 rakwb Robinson, Jean P. verfasserin aut No Role for Phospholipase A2 and Protein Kinase C in the Potentiation by α-Adrenoceptors of β-Adrenoceptor-Mediated Cyclic AMP Formation in Rat Brain Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: This study was undertaken to examine the role of phospholipase A2 and protein kinase C in the potentiation of β-adrenoceptor-mediated cyclic AMP formation by α-ad-renoceptors in rat cerebral cortical slices. Inhibition of ara-chidonic acid metabolism by a range of cyclooxygenase and lipoxygenase inhibitors had no effect on the potentiation of isoprenaline-stimulated cyclic AMP. Conversely, stimulation of leukotriene formation had no effect on the response to isoprenaline. The phospholipase A2 activator, melittin, stimulated cyclic AMP and potentiated the effect of isoprenaline, but these responses were not influenced by cyclooxygenase or lipoxygenase inhibitors. Indomethacin was also ineffective against the potentiation of vasoactive intestinal peptide-stimulated cyclic AMP by noradrenaline. Phorbol ester potentiated the cyclic AMP response to isoprenaline, and this potentiation was antagonized by three different putative protein kinase C inhibitors. However, the same inhibitors did not affect the α-adrenoceptor-stimulated enhancement of the response to isoprenaline. We have found no evidence, therefore, to support the suggestion that arachidonic acid and its metabolites and/or protein kinase C mediate the α-adreno-ceptor modulation of β-adrenoceptor function. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| α-Adrenoceptors Kendall, David A. verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 53(1989), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:53 year:1989 number:2 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1989.tb07367.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 53 1989 2 0 |
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10.1111/j.1471-4159.1989.tb07367.x doi (DE-627)NLEJ240274466 DE-627 ger DE-627 rakwb Robinson, Jean P. verfasserin aut No Role for Phospholipase A2 and Protein Kinase C in the Potentiation by α-Adrenoceptors of β-Adrenoceptor-Mediated Cyclic AMP Formation in Rat Brain Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: This study was undertaken to examine the role of phospholipase A2 and protein kinase C in the potentiation of β-adrenoceptor-mediated cyclic AMP formation by α-ad-renoceptors in rat cerebral cortical slices. Inhibition of ara-chidonic acid metabolism by a range of cyclooxygenase and lipoxygenase inhibitors had no effect on the potentiation of isoprenaline-stimulated cyclic AMP. Conversely, stimulation of leukotriene formation had no effect on the response to isoprenaline. The phospholipase A2 activator, melittin, stimulated cyclic AMP and potentiated the effect of isoprenaline, but these responses were not influenced by cyclooxygenase or lipoxygenase inhibitors. Indomethacin was also ineffective against the potentiation of vasoactive intestinal peptide-stimulated cyclic AMP by noradrenaline. Phorbol ester potentiated the cyclic AMP response to isoprenaline, and this potentiation was antagonized by three different putative protein kinase C inhibitors. However, the same inhibitors did not affect the α-adrenoceptor-stimulated enhancement of the response to isoprenaline. We have found no evidence, therefore, to support the suggestion that arachidonic acid and its metabolites and/or protein kinase C mediate the α-adreno-ceptor modulation of β-adrenoceptor function. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| α-Adrenoceptors Kendall, David A. verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 53(1989), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:53 year:1989 number:2 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1989.tb07367.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 53 1989 2 0 |
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10.1111/j.1471-4159.1989.tb07367.x doi (DE-627)NLEJ240274466 DE-627 ger DE-627 rakwb Robinson, Jean P. verfasserin aut No Role for Phospholipase A2 and Protein Kinase C in the Potentiation by α-Adrenoceptors of β-Adrenoceptor-Mediated Cyclic AMP Formation in Rat Brain Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: This study was undertaken to examine the role of phospholipase A2 and protein kinase C in the potentiation of β-adrenoceptor-mediated cyclic AMP formation by α-ad-renoceptors in rat cerebral cortical slices. Inhibition of ara-chidonic acid metabolism by a range of cyclooxygenase and lipoxygenase inhibitors had no effect on the potentiation of isoprenaline-stimulated cyclic AMP. Conversely, stimulation of leukotriene formation had no effect on the response to isoprenaline. The phospholipase A2 activator, melittin, stimulated cyclic AMP and potentiated the effect of isoprenaline, but these responses were not influenced by cyclooxygenase or lipoxygenase inhibitors. Indomethacin was also ineffective against the potentiation of vasoactive intestinal peptide-stimulated cyclic AMP by noradrenaline. Phorbol ester potentiated the cyclic AMP response to isoprenaline, and this potentiation was antagonized by three different putative protein kinase C inhibitors. However, the same inhibitors did not affect the α-adrenoceptor-stimulated enhancement of the response to isoprenaline. We have found no evidence, therefore, to support the suggestion that arachidonic acid and its metabolites and/or protein kinase C mediate the α-adreno-ceptor modulation of β-adrenoceptor function. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| α-Adrenoceptors Kendall, David A. verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 53(1989), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:53 year:1989 number:2 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1989.tb07367.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 53 1989 2 0 |
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No Role for Phospholipase A2 and Protein Kinase C in the Potentiation by α-Adrenoceptors of β-Adrenoceptor-Mediated Cyclic AMP Formation in Rat Brain |
| abstract |
Abstract: This study was undertaken to examine the role of phospholipase A2 and protein kinase C in the potentiation of β-adrenoceptor-mediated cyclic AMP formation by α-ad-renoceptors in rat cerebral cortical slices. Inhibition of ara-chidonic acid metabolism by a range of cyclooxygenase and lipoxygenase inhibitors had no effect on the potentiation of isoprenaline-stimulated cyclic AMP. Conversely, stimulation of leukotriene formation had no effect on the response to isoprenaline. The phospholipase A2 activator, melittin, stimulated cyclic AMP and potentiated the effect of isoprenaline, but these responses were not influenced by cyclooxygenase or lipoxygenase inhibitors. Indomethacin was also ineffective against the potentiation of vasoactive intestinal peptide-stimulated cyclic AMP by noradrenaline. Phorbol ester potentiated the cyclic AMP response to isoprenaline, and this potentiation was antagonized by three different putative protein kinase C inhibitors. However, the same inhibitors did not affect the α-adrenoceptor-stimulated enhancement of the response to isoprenaline. We have found no evidence, therefore, to support the suggestion that arachidonic acid and its metabolites and/or protein kinase C mediate the α-adreno-ceptor modulation of β-adrenoceptor function. |
| abstractGer |
Abstract: This study was undertaken to examine the role of phospholipase A2 and protein kinase C in the potentiation of β-adrenoceptor-mediated cyclic AMP formation by α-ad-renoceptors in rat cerebral cortical slices. Inhibition of ara-chidonic acid metabolism by a range of cyclooxygenase and lipoxygenase inhibitors had no effect on the potentiation of isoprenaline-stimulated cyclic AMP. Conversely, stimulation of leukotriene formation had no effect on the response to isoprenaline. The phospholipase A2 activator, melittin, stimulated cyclic AMP and potentiated the effect of isoprenaline, but these responses were not influenced by cyclooxygenase or lipoxygenase inhibitors. Indomethacin was also ineffective against the potentiation of vasoactive intestinal peptide-stimulated cyclic AMP by noradrenaline. Phorbol ester potentiated the cyclic AMP response to isoprenaline, and this potentiation was antagonized by three different putative protein kinase C inhibitors. However, the same inhibitors did not affect the α-adrenoceptor-stimulated enhancement of the response to isoprenaline. We have found no evidence, therefore, to support the suggestion that arachidonic acid and its metabolites and/or protein kinase C mediate the α-adreno-ceptor modulation of β-adrenoceptor function. |
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Abstract: This study was undertaken to examine the role of phospholipase A2 and protein kinase C in the potentiation of β-adrenoceptor-mediated cyclic AMP formation by α-ad-renoceptors in rat cerebral cortical slices. Inhibition of ara-chidonic acid metabolism by a range of cyclooxygenase and lipoxygenase inhibitors had no effect on the potentiation of isoprenaline-stimulated cyclic AMP. Conversely, stimulation of leukotriene formation had no effect on the response to isoprenaline. The phospholipase A2 activator, melittin, stimulated cyclic AMP and potentiated the effect of isoprenaline, but these responses were not influenced by cyclooxygenase or lipoxygenase inhibitors. Indomethacin was also ineffective against the potentiation of vasoactive intestinal peptide-stimulated cyclic AMP by noradrenaline. Phorbol ester potentiated the cyclic AMP response to isoprenaline, and this potentiation was antagonized by three different putative protein kinase C inhibitors. However, the same inhibitors did not affect the α-adrenoceptor-stimulated enhancement of the response to isoprenaline. We have found no evidence, therefore, to support the suggestion that arachidonic acid and its metabolites and/or protein kinase C mediate the α-adreno-ceptor modulation of β-adrenoceptor function. |
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No Role for Phospholipase A2 and Protein Kinase C in the Potentiation by α-Adrenoceptors of β-Adrenoceptor-Mediated Cyclic AMP Formation in Rat Brain |
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