Phorbol Esters Attenuate Glutamate-Stimulated Inositol Phospholipid Hydrolysis in Neuronal Cultures
Abstract: The phorbol diesters 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and phorbol-12,13-dibutyrate, but not 4–α-phorbol-didecanoate, inhibited the stimulation of inositol phospholipid hydrolysis by excitatory amino acids and carbamylcholine in primary cultures of cerebellar neurons. This inhibi...
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Gespeichert in:
| Autor*in: |
Canonico, P. L. [verfasserIn] Favit, A. [verfasserIn] Catania, M. V. [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1988 |
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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, 51(1988), 4, Seite 0 |
| Übergeordnetes Werk: |
volume:51 ; year:1988 ; number:4 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1111/j.1471-4159.1988.tb03067.x |
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| 520 | |a Abstract: The phorbol diesters 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and phorbol-12,13-dibutyrate, but not 4–α-phorbol-didecanoate, inhibited the stimulation of inositol phospholipid hydrolysis by excitatory amino acids and carbamylcholine in primary cultures of cerebellar neurons. This inhibition was mimicked by the synthetic diacylglycerol 1,2-dioleoyl-rac-glycerol (DOG) and was selective for a specific glutamate-phosphoinositide receptor subtype (GP2 receptor) activated by glutamate and quis-qualate. TPA was nearly inactive in inhibiting the stimulation of inositol phospholipid hydrolysis by N-methyl-d-aspartate, a selective agonist of the GP1 receptor. Phorbol diesters and DOG attenuated the stimulation of inositol phospholipid hydrolysis by glutamate and quisqualate also in cerebellar slices from 9–15-day-old rats; however, using this preparation, their action was weak and required high concentrations (> 1 μM). The inhibition of signal transduc-tion by phorbol diesters was not consequent to a reduced binding of glutamate to its membrane recognition sites. In fact, TPA induced only a small increase in the KD but no change in the Bmax of [3H]glutamate binding in cerebellar membranes. Phorbol diesters may act to inhibit specific GTP-binding proteins or particular molecular forms of phosphoinositidase C associated with GP2 or muscarinic cholinergic receptors. | ||
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10.1111/j.1471-4159.1988.tb03067.x doi (DE-627)NLEJ240279107 DE-627 ger DE-627 rakwb Canonico, P. L. verfasserin aut Phorbol Esters Attenuate Glutamate-Stimulated Inositol Phospholipid Hydrolysis in Neuronal Cultures Oxford, UK Blackwell Publishing Ltd 1988 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The phorbol diesters 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and phorbol-12,13-dibutyrate, but not 4–α-phorbol-didecanoate, inhibited the stimulation of inositol phospholipid hydrolysis by excitatory amino acids and carbamylcholine in primary cultures of cerebellar neurons. This inhibition was mimicked by the synthetic diacylglycerol 1,2-dioleoyl-rac-glycerol (DOG) and was selective for a specific glutamate-phosphoinositide receptor subtype (GP2 receptor) activated by glutamate and quis-qualate. TPA was nearly inactive in inhibiting the stimulation of inositol phospholipid hydrolysis by N-methyl-d-aspartate, a selective agonist of the GP1 receptor. Phorbol diesters and DOG attenuated the stimulation of inositol phospholipid hydrolysis by glutamate and quisqualate also in cerebellar slices from 9–15-day-old rats; however, using this preparation, their action was weak and required high concentrations (> 1 μM). The inhibition of signal transduc-tion by phorbol diesters was not consequent to a reduced binding of glutamate to its membrane recognition sites. In fact, TPA induced only a small increase in the KD but no change in the Bmax of [3H]glutamate binding in cerebellar membranes. Phorbol diesters may act to inhibit specific GTP-binding proteins or particular molecular forms of phosphoinositidase C associated with GP2 or muscarinic cholinergic receptors. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Phorbol diesters Favit, A. verfasserin aut Catania, M. V. verfasserin aut Nicoletti, F. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 51(1988), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:51 year:1988 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1988.tb03067.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 51 1988 4 0 |
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10.1111/j.1471-4159.1988.tb03067.x doi (DE-627)NLEJ240279107 DE-627 ger DE-627 rakwb Canonico, P. L. verfasserin aut Phorbol Esters Attenuate Glutamate-Stimulated Inositol Phospholipid Hydrolysis in Neuronal Cultures Oxford, UK Blackwell Publishing Ltd 1988 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The phorbol diesters 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and phorbol-12,13-dibutyrate, but not 4–α-phorbol-didecanoate, inhibited the stimulation of inositol phospholipid hydrolysis by excitatory amino acids and carbamylcholine in primary cultures of cerebellar neurons. This inhibition was mimicked by the synthetic diacylglycerol 1,2-dioleoyl-rac-glycerol (DOG) and was selective for a specific glutamate-phosphoinositide receptor subtype (GP2 receptor) activated by glutamate and quis-qualate. TPA was nearly inactive in inhibiting the stimulation of inositol phospholipid hydrolysis by N-methyl-d-aspartate, a selective agonist of the GP1 receptor. Phorbol diesters and DOG attenuated the stimulation of inositol phospholipid hydrolysis by glutamate and quisqualate also in cerebellar slices from 9–15-day-old rats; however, using this preparation, their action was weak and required high concentrations (> 1 μM). The inhibition of signal transduc-tion by phorbol diesters was not consequent to a reduced binding of glutamate to its membrane recognition sites. In fact, TPA induced only a small increase in the KD but no change in the Bmax of [3H]glutamate binding in cerebellar membranes. Phorbol diesters may act to inhibit specific GTP-binding proteins or particular molecular forms of phosphoinositidase C associated with GP2 or muscarinic cholinergic receptors. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Phorbol diesters Favit, A. verfasserin aut Catania, M. V. verfasserin aut Nicoletti, F. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 51(1988), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:51 year:1988 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1988.tb03067.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 51 1988 4 0 |
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10.1111/j.1471-4159.1988.tb03067.x doi (DE-627)NLEJ240279107 DE-627 ger DE-627 rakwb Canonico, P. L. verfasserin aut Phorbol Esters Attenuate Glutamate-Stimulated Inositol Phospholipid Hydrolysis in Neuronal Cultures Oxford, UK Blackwell Publishing Ltd 1988 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The phorbol diesters 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and phorbol-12,13-dibutyrate, but not 4–α-phorbol-didecanoate, inhibited the stimulation of inositol phospholipid hydrolysis by excitatory amino acids and carbamylcholine in primary cultures of cerebellar neurons. This inhibition was mimicked by the synthetic diacylglycerol 1,2-dioleoyl-rac-glycerol (DOG) and was selective for a specific glutamate-phosphoinositide receptor subtype (GP2 receptor) activated by glutamate and quis-qualate. TPA was nearly inactive in inhibiting the stimulation of inositol phospholipid hydrolysis by N-methyl-d-aspartate, a selective agonist of the GP1 receptor. Phorbol diesters and DOG attenuated the stimulation of inositol phospholipid hydrolysis by glutamate and quisqualate also in cerebellar slices from 9–15-day-old rats; however, using this preparation, their action was weak and required high concentrations (> 1 μM). The inhibition of signal transduc-tion by phorbol diesters was not consequent to a reduced binding of glutamate to its membrane recognition sites. In fact, TPA induced only a small increase in the KD but no change in the Bmax of [3H]glutamate binding in cerebellar membranes. Phorbol diesters may act to inhibit specific GTP-binding proteins or particular molecular forms of phosphoinositidase C associated with GP2 or muscarinic cholinergic receptors. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Phorbol diesters Favit, A. verfasserin aut Catania, M. V. verfasserin aut Nicoletti, F. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 51(1988), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:51 year:1988 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1988.tb03067.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 51 1988 4 0 |
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10.1111/j.1471-4159.1988.tb03067.x doi (DE-627)NLEJ240279107 DE-627 ger DE-627 rakwb Canonico, P. L. verfasserin aut Phorbol Esters Attenuate Glutamate-Stimulated Inositol Phospholipid Hydrolysis in Neuronal Cultures Oxford, UK Blackwell Publishing Ltd 1988 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The phorbol diesters 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and phorbol-12,13-dibutyrate, but not 4–α-phorbol-didecanoate, inhibited the stimulation of inositol phospholipid hydrolysis by excitatory amino acids and carbamylcholine in primary cultures of cerebellar neurons. This inhibition was mimicked by the synthetic diacylglycerol 1,2-dioleoyl-rac-glycerol (DOG) and was selective for a specific glutamate-phosphoinositide receptor subtype (GP2 receptor) activated by glutamate and quis-qualate. TPA was nearly inactive in inhibiting the stimulation of inositol phospholipid hydrolysis by N-methyl-d-aspartate, a selective agonist of the GP1 receptor. Phorbol diesters and DOG attenuated the stimulation of inositol phospholipid hydrolysis by glutamate and quisqualate also in cerebellar slices from 9–15-day-old rats; however, using this preparation, their action was weak and required high concentrations (> 1 μM). The inhibition of signal transduc-tion by phorbol diesters was not consequent to a reduced binding of glutamate to its membrane recognition sites. In fact, TPA induced only a small increase in the KD but no change in the Bmax of [3H]glutamate binding in cerebellar membranes. Phorbol diesters may act to inhibit specific GTP-binding proteins or particular molecular forms of phosphoinositidase C associated with GP2 or muscarinic cholinergic receptors. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Phorbol diesters Favit, A. verfasserin aut Catania, M. V. verfasserin aut Nicoletti, F. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 51(1988), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:51 year:1988 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1988.tb03067.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 51 1988 4 0 |
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10.1111/j.1471-4159.1988.tb03067.x doi (DE-627)NLEJ240279107 DE-627 ger DE-627 rakwb Canonico, P. L. verfasserin aut Phorbol Esters Attenuate Glutamate-Stimulated Inositol Phospholipid Hydrolysis in Neuronal Cultures Oxford, UK Blackwell Publishing Ltd 1988 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The phorbol diesters 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and phorbol-12,13-dibutyrate, but not 4–α-phorbol-didecanoate, inhibited the stimulation of inositol phospholipid hydrolysis by excitatory amino acids and carbamylcholine in primary cultures of cerebellar neurons. This inhibition was mimicked by the synthetic diacylglycerol 1,2-dioleoyl-rac-glycerol (DOG) and was selective for a specific glutamate-phosphoinositide receptor subtype (GP2 receptor) activated by glutamate and quis-qualate. TPA was nearly inactive in inhibiting the stimulation of inositol phospholipid hydrolysis by N-methyl-d-aspartate, a selective agonist of the GP1 receptor. Phorbol diesters and DOG attenuated the stimulation of inositol phospholipid hydrolysis by glutamate and quisqualate also in cerebellar slices from 9–15-day-old rats; however, using this preparation, their action was weak and required high concentrations (> 1 μM). The inhibition of signal transduc-tion by phorbol diesters was not consequent to a reduced binding of glutamate to its membrane recognition sites. In fact, TPA induced only a small increase in the KD but no change in the Bmax of [3H]glutamate binding in cerebellar membranes. Phorbol diesters may act to inhibit specific GTP-binding proteins or particular molecular forms of phosphoinositidase C associated with GP2 or muscarinic cholinergic receptors. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Phorbol diesters Favit, A. verfasserin aut Catania, M. V. verfasserin aut Nicoletti, F. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 51(1988), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:51 year:1988 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1988.tb03067.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 51 1988 4 0 |
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phorbol esters attenuate glutamate-stimulated inositol phospholipid hydrolysis in neuronal cultures |
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Phorbol Esters Attenuate Glutamate-Stimulated Inositol Phospholipid Hydrolysis in Neuronal Cultures |
| abstract |
Abstract: The phorbol diesters 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and phorbol-12,13-dibutyrate, but not 4–α-phorbol-didecanoate, inhibited the stimulation of inositol phospholipid hydrolysis by excitatory amino acids and carbamylcholine in primary cultures of cerebellar neurons. This inhibition was mimicked by the synthetic diacylglycerol 1,2-dioleoyl-rac-glycerol (DOG) and was selective for a specific glutamate-phosphoinositide receptor subtype (GP2 receptor) activated by glutamate and quis-qualate. TPA was nearly inactive in inhibiting the stimulation of inositol phospholipid hydrolysis by N-methyl-d-aspartate, a selective agonist of the GP1 receptor. Phorbol diesters and DOG attenuated the stimulation of inositol phospholipid hydrolysis by glutamate and quisqualate also in cerebellar slices from 9–15-day-old rats; however, using this preparation, their action was weak and required high concentrations (> 1 μM). The inhibition of signal transduc-tion by phorbol diesters was not consequent to a reduced binding of glutamate to its membrane recognition sites. In fact, TPA induced only a small increase in the KD but no change in the Bmax of [3H]glutamate binding in cerebellar membranes. Phorbol diesters may act to inhibit specific GTP-binding proteins or particular molecular forms of phosphoinositidase C associated with GP2 or muscarinic cholinergic receptors. |
| abstractGer |
Abstract: The phorbol diesters 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and phorbol-12,13-dibutyrate, but not 4–α-phorbol-didecanoate, inhibited the stimulation of inositol phospholipid hydrolysis by excitatory amino acids and carbamylcholine in primary cultures of cerebellar neurons. This inhibition was mimicked by the synthetic diacylglycerol 1,2-dioleoyl-rac-glycerol (DOG) and was selective for a specific glutamate-phosphoinositide receptor subtype (GP2 receptor) activated by glutamate and quis-qualate. TPA was nearly inactive in inhibiting the stimulation of inositol phospholipid hydrolysis by N-methyl-d-aspartate, a selective agonist of the GP1 receptor. Phorbol diesters and DOG attenuated the stimulation of inositol phospholipid hydrolysis by glutamate and quisqualate also in cerebellar slices from 9–15-day-old rats; however, using this preparation, their action was weak and required high concentrations (> 1 μM). The inhibition of signal transduc-tion by phorbol diesters was not consequent to a reduced binding of glutamate to its membrane recognition sites. In fact, TPA induced only a small increase in the KD but no change in the Bmax of [3H]glutamate binding in cerebellar membranes. Phorbol diesters may act to inhibit specific GTP-binding proteins or particular molecular forms of phosphoinositidase C associated with GP2 or muscarinic cholinergic receptors. |
| abstract_unstemmed |
Abstract: The phorbol diesters 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and phorbol-12,13-dibutyrate, but not 4–α-phorbol-didecanoate, inhibited the stimulation of inositol phospholipid hydrolysis by excitatory amino acids and carbamylcholine in primary cultures of cerebellar neurons. This inhibition was mimicked by the synthetic diacylglycerol 1,2-dioleoyl-rac-glycerol (DOG) and was selective for a specific glutamate-phosphoinositide receptor subtype (GP2 receptor) activated by glutamate and quis-qualate. TPA was nearly inactive in inhibiting the stimulation of inositol phospholipid hydrolysis by N-methyl-d-aspartate, a selective agonist of the GP1 receptor. Phorbol diesters and DOG attenuated the stimulation of inositol phospholipid hydrolysis by glutamate and quisqualate also in cerebellar slices from 9–15-day-old rats; however, using this preparation, their action was weak and required high concentrations (> 1 μM). The inhibition of signal transduc-tion by phorbol diesters was not consequent to a reduced binding of glutamate to its membrane recognition sites. In fact, TPA induced only a small increase in the KD but no change in the Bmax of [3H]glutamate binding in cerebellar membranes. Phorbol diesters may act to inhibit specific GTP-binding proteins or particular molecular forms of phosphoinositidase C associated with GP2 or muscarinic cholinergic receptors. |
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| title_short |
Phorbol Esters Attenuate Glutamate-Stimulated Inositol Phospholipid Hydrolysis in Neuronal Cultures |
| url |
http://dx.doi.org/10.1111/j.1471-4159.1988.tb03067.x |
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| author2 |
Favit, A. Catania, M. V. Nicoletti, F. |
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Favit, A. Catania, M. V. Nicoletti, F. |
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| doi_str |
10.1111/j.1471-4159.1988.tb03067.x |
| up_date |
2024-07-06T09:34:07.607Z |
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