Desensitization of Metabotropic Glutamate Receptors in Neuronal Cultures
Abstract: Preexposure of cultured cerebellar neurons to glutamate reduced the stimulation of polyphosphoinositide (PPI) hydrolysis induced by subsequent addition of glutamate without affecting the response to the muscarinic receptor agonist carbamylcholine. Desensitization of glutamate-stimulated PP...
Ausführliche Beschreibung
Autor*in: |
Catania, M. V. [verfasserIn] Aronica, E. [verfasserIn] Sortino, M. A. [verfasserIn] |
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E-Artikel |
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Oxford, UK: Blackwell Publishing Ltd ; 1991 |
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Online-Ressource |
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2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 56(1991), 4, Seite 0 |
Übergeordnetes Werk: |
volume:56 ; year:1991 ; number:4 ; pages:0 |
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DOI / URN: |
10.1111/j.1471-4159.1991.tb11429.x |
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520 | |a Abstract: Preexposure of cultured cerebellar neurons to glutamate reduced the stimulation of polyphosphoinositide (PPI) hydrolysis induced by subsequent addition of glutamate without affecting the response to the muscarinic receptor agonist carbamylcholine. Desensitization of glutamate-stimulated PPI hydrolysis developed rapidly and persisted up to 48 h after removal of glutamate from the incubation medium. Stimulation of PPI hydrolysis by quisqualate was abolished in cultures pretreated with quisqualate or glutamate, but not with N-methyl-D-aspartate (NMDA). In contrast, pretreatment with NMDA reduced the stimulation of PPI hydrolysis induced by a subsequent addition of NMDA, leaving the action of quisqualate intact. The lack of cross-desensitization between NMDA and quisqualate supports the existence of two distinct subtypes of glutamate receptors coupled to PPI hydrolysis. Desensitization induced by a 30-min (but not by a 6-h) exposure to glutamate was attenuated or prevented by putative protein kinase C inhibitors, including mono- and trisialogangliosides, sphingosine, and polymyxin B, but not by inhibitors of arachidonic acid metabolism, nor by the nonselective calpain inhibitor leupeptin, nor by the lectin concanavalin A. These results suggest that desensitization of metabotropic glutamate receptors involves, at least in its rapid component, activation of protein kinase C. | ||
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10.1111/j.1471-4159.1991.tb11429.x doi (DE-627)NLEJ240264045 DE-627 ger DE-627 rakwb Catania, M. V. verfasserin aut Desensitization of Metabotropic Glutamate Receptors in Neuronal Cultures Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Preexposure of cultured cerebellar neurons to glutamate reduced the stimulation of polyphosphoinositide (PPI) hydrolysis induced by subsequent addition of glutamate without affecting the response to the muscarinic receptor agonist carbamylcholine. Desensitization of glutamate-stimulated PPI hydrolysis developed rapidly and persisted up to 48 h after removal of glutamate from the incubation medium. Stimulation of PPI hydrolysis by quisqualate was abolished in cultures pretreated with quisqualate or glutamate, but not with N-methyl-D-aspartate (NMDA). In contrast, pretreatment with NMDA reduced the stimulation of PPI hydrolysis induced by a subsequent addition of NMDA, leaving the action of quisqualate intact. The lack of cross-desensitization between NMDA and quisqualate supports the existence of two distinct subtypes of glutamate receptors coupled to PPI hydrolysis. Desensitization induced by a 30-min (but not by a 6-h) exposure to glutamate was attenuated or prevented by putative protein kinase C inhibitors, including mono- and trisialogangliosides, sphingosine, and polymyxin B, but not by inhibitors of arachidonic acid metabolism, nor by the nonselective calpain inhibitor leupeptin, nor by the lectin concanavalin A. These results suggest that desensitization of metabotropic glutamate receptors involves, at least in its rapid component, activation of protein kinase C. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Glutamate receptors Aronica, E. verfasserin aut Sortino, M. A. verfasserin aut Canonico, P. L. oth Nicoletti, F. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 56(1991), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:56 year:1991 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1991.tb11429.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 56 1991 4 0 |
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10.1111/j.1471-4159.1991.tb11429.x doi (DE-627)NLEJ240264045 DE-627 ger DE-627 rakwb Catania, M. V. verfasserin aut Desensitization of Metabotropic Glutamate Receptors in Neuronal Cultures Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Preexposure of cultured cerebellar neurons to glutamate reduced the stimulation of polyphosphoinositide (PPI) hydrolysis induced by subsequent addition of glutamate without affecting the response to the muscarinic receptor agonist carbamylcholine. Desensitization of glutamate-stimulated PPI hydrolysis developed rapidly and persisted up to 48 h after removal of glutamate from the incubation medium. Stimulation of PPI hydrolysis by quisqualate was abolished in cultures pretreated with quisqualate or glutamate, but not with N-methyl-D-aspartate (NMDA). In contrast, pretreatment with NMDA reduced the stimulation of PPI hydrolysis induced by a subsequent addition of NMDA, leaving the action of quisqualate intact. The lack of cross-desensitization between NMDA and quisqualate supports the existence of two distinct subtypes of glutamate receptors coupled to PPI hydrolysis. Desensitization induced by a 30-min (but not by a 6-h) exposure to glutamate was attenuated or prevented by putative protein kinase C inhibitors, including mono- and trisialogangliosides, sphingosine, and polymyxin B, but not by inhibitors of arachidonic acid metabolism, nor by the nonselective calpain inhibitor leupeptin, nor by the lectin concanavalin A. These results suggest that desensitization of metabotropic glutamate receptors involves, at least in its rapid component, activation of protein kinase C. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Glutamate receptors Aronica, E. verfasserin aut Sortino, M. A. verfasserin aut Canonico, P. L. oth Nicoletti, F. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 56(1991), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:56 year:1991 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1991.tb11429.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 56 1991 4 0 |
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10.1111/j.1471-4159.1991.tb11429.x doi (DE-627)NLEJ240264045 DE-627 ger DE-627 rakwb Catania, M. V. verfasserin aut Desensitization of Metabotropic Glutamate Receptors in Neuronal Cultures Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Preexposure of cultured cerebellar neurons to glutamate reduced the stimulation of polyphosphoinositide (PPI) hydrolysis induced by subsequent addition of glutamate without affecting the response to the muscarinic receptor agonist carbamylcholine. Desensitization of glutamate-stimulated PPI hydrolysis developed rapidly and persisted up to 48 h after removal of glutamate from the incubation medium. Stimulation of PPI hydrolysis by quisqualate was abolished in cultures pretreated with quisqualate or glutamate, but not with N-methyl-D-aspartate (NMDA). In contrast, pretreatment with NMDA reduced the stimulation of PPI hydrolysis induced by a subsequent addition of NMDA, leaving the action of quisqualate intact. The lack of cross-desensitization between NMDA and quisqualate supports the existence of two distinct subtypes of glutamate receptors coupled to PPI hydrolysis. Desensitization induced by a 30-min (but not by a 6-h) exposure to glutamate was attenuated or prevented by putative protein kinase C inhibitors, including mono- and trisialogangliosides, sphingosine, and polymyxin B, but not by inhibitors of arachidonic acid metabolism, nor by the nonselective calpain inhibitor leupeptin, nor by the lectin concanavalin A. These results suggest that desensitization of metabotropic glutamate receptors involves, at least in its rapid component, activation of protein kinase C. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Glutamate receptors Aronica, E. verfasserin aut Sortino, M. A. verfasserin aut Canonico, P. L. oth Nicoletti, F. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 56(1991), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:56 year:1991 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1991.tb11429.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 56 1991 4 0 |
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10.1111/j.1471-4159.1991.tb11429.x doi (DE-627)NLEJ240264045 DE-627 ger DE-627 rakwb Catania, M. V. verfasserin aut Desensitization of Metabotropic Glutamate Receptors in Neuronal Cultures Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Preexposure of cultured cerebellar neurons to glutamate reduced the stimulation of polyphosphoinositide (PPI) hydrolysis induced by subsequent addition of glutamate without affecting the response to the muscarinic receptor agonist carbamylcholine. Desensitization of glutamate-stimulated PPI hydrolysis developed rapidly and persisted up to 48 h after removal of glutamate from the incubation medium. Stimulation of PPI hydrolysis by quisqualate was abolished in cultures pretreated with quisqualate or glutamate, but not with N-methyl-D-aspartate (NMDA). In contrast, pretreatment with NMDA reduced the stimulation of PPI hydrolysis induced by a subsequent addition of NMDA, leaving the action of quisqualate intact. The lack of cross-desensitization between NMDA and quisqualate supports the existence of two distinct subtypes of glutamate receptors coupled to PPI hydrolysis. Desensitization induced by a 30-min (but not by a 6-h) exposure to glutamate was attenuated or prevented by putative protein kinase C inhibitors, including mono- and trisialogangliosides, sphingosine, and polymyxin B, but not by inhibitors of arachidonic acid metabolism, nor by the nonselective calpain inhibitor leupeptin, nor by the lectin concanavalin A. These results suggest that desensitization of metabotropic glutamate receptors involves, at least in its rapid component, activation of protein kinase C. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Glutamate receptors Aronica, E. verfasserin aut Sortino, M. A. verfasserin aut Canonico, P. L. oth Nicoletti, F. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 56(1991), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:56 year:1991 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1991.tb11429.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 56 1991 4 0 |
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10.1111/j.1471-4159.1991.tb11429.x doi (DE-627)NLEJ240264045 DE-627 ger DE-627 rakwb Catania, M. V. verfasserin aut Desensitization of Metabotropic Glutamate Receptors in Neuronal Cultures Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Preexposure of cultured cerebellar neurons to glutamate reduced the stimulation of polyphosphoinositide (PPI) hydrolysis induced by subsequent addition of glutamate without affecting the response to the muscarinic receptor agonist carbamylcholine. Desensitization of glutamate-stimulated PPI hydrolysis developed rapidly and persisted up to 48 h after removal of glutamate from the incubation medium. Stimulation of PPI hydrolysis by quisqualate was abolished in cultures pretreated with quisqualate or glutamate, but not with N-methyl-D-aspartate (NMDA). In contrast, pretreatment with NMDA reduced the stimulation of PPI hydrolysis induced by a subsequent addition of NMDA, leaving the action of quisqualate intact. The lack of cross-desensitization between NMDA and quisqualate supports the existence of two distinct subtypes of glutamate receptors coupled to PPI hydrolysis. Desensitization induced by a 30-min (but not by a 6-h) exposure to glutamate was attenuated or prevented by putative protein kinase C inhibitors, including mono- and trisialogangliosides, sphingosine, and polymyxin B, but not by inhibitors of arachidonic acid metabolism, nor by the nonselective calpain inhibitor leupeptin, nor by the lectin concanavalin A. These results suggest that desensitization of metabotropic glutamate receptors involves, at least in its rapid component, activation of protein kinase C. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Glutamate receptors Aronica, E. verfasserin aut Sortino, M. A. verfasserin aut Canonico, P. L. oth Nicoletti, F. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 56(1991), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:56 year:1991 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1991.tb11429.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 56 1991 4 0 |
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Abstract: Preexposure of cultured cerebellar neurons to glutamate reduced the stimulation of polyphosphoinositide (PPI) hydrolysis induced by subsequent addition of glutamate without affecting the response to the muscarinic receptor agonist carbamylcholine. Desensitization of glutamate-stimulated PPI hydrolysis developed rapidly and persisted up to 48 h after removal of glutamate from the incubation medium. Stimulation of PPI hydrolysis by quisqualate was abolished in cultures pretreated with quisqualate or glutamate, but not with N-methyl-D-aspartate (NMDA). In contrast, pretreatment with NMDA reduced the stimulation of PPI hydrolysis induced by a subsequent addition of NMDA, leaving the action of quisqualate intact. The lack of cross-desensitization between NMDA and quisqualate supports the existence of two distinct subtypes of glutamate receptors coupled to PPI hydrolysis. Desensitization induced by a 30-min (but not by a 6-h) exposure to glutamate was attenuated or prevented by putative protein kinase C inhibitors, including mono- and trisialogangliosides, sphingosine, and polymyxin B, but not by inhibitors of arachidonic acid metabolism, nor by the nonselective calpain inhibitor leupeptin, nor by the lectin concanavalin A. These results suggest that desensitization of metabotropic glutamate receptors involves, at least in its rapid component, activation of protein kinase C. |
abstractGer |
Abstract: Preexposure of cultured cerebellar neurons to glutamate reduced the stimulation of polyphosphoinositide (PPI) hydrolysis induced by subsequent addition of glutamate without affecting the response to the muscarinic receptor agonist carbamylcholine. Desensitization of glutamate-stimulated PPI hydrolysis developed rapidly and persisted up to 48 h after removal of glutamate from the incubation medium. Stimulation of PPI hydrolysis by quisqualate was abolished in cultures pretreated with quisqualate or glutamate, but not with N-methyl-D-aspartate (NMDA). In contrast, pretreatment with NMDA reduced the stimulation of PPI hydrolysis induced by a subsequent addition of NMDA, leaving the action of quisqualate intact. The lack of cross-desensitization between NMDA and quisqualate supports the existence of two distinct subtypes of glutamate receptors coupled to PPI hydrolysis. Desensitization induced by a 30-min (but not by a 6-h) exposure to glutamate was attenuated or prevented by putative protein kinase C inhibitors, including mono- and trisialogangliosides, sphingosine, and polymyxin B, but not by inhibitors of arachidonic acid metabolism, nor by the nonselective calpain inhibitor leupeptin, nor by the lectin concanavalin A. These results suggest that desensitization of metabotropic glutamate receptors involves, at least in its rapid component, activation of protein kinase C. |
abstract_unstemmed |
Abstract: Preexposure of cultured cerebellar neurons to glutamate reduced the stimulation of polyphosphoinositide (PPI) hydrolysis induced by subsequent addition of glutamate without affecting the response to the muscarinic receptor agonist carbamylcholine. Desensitization of glutamate-stimulated PPI hydrolysis developed rapidly and persisted up to 48 h after removal of glutamate from the incubation medium. Stimulation of PPI hydrolysis by quisqualate was abolished in cultures pretreated with quisqualate or glutamate, but not with N-methyl-D-aspartate (NMDA). In contrast, pretreatment with NMDA reduced the stimulation of PPI hydrolysis induced by a subsequent addition of NMDA, leaving the action of quisqualate intact. The lack of cross-desensitization between NMDA and quisqualate supports the existence of two distinct subtypes of glutamate receptors coupled to PPI hydrolysis. Desensitization induced by a 30-min (but not by a 6-h) exposure to glutamate was attenuated or prevented by putative protein kinase C inhibitors, including mono- and trisialogangliosides, sphingosine, and polymyxin B, but not by inhibitors of arachidonic acid metabolism, nor by the nonselective calpain inhibitor leupeptin, nor by the lectin concanavalin A. These results suggest that desensitization of metabotropic glutamate receptors involves, at least in its rapid component, activation of protein kinase C. |
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Desensitization of Metabotropic Glutamate Receptors in Neuronal Cultures |
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Aronica, E. Sortino, M. A. Canonico, P. L. Nicoletti, F. |
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