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Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons
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Zeitschriftentitel: | European Journal of Neuroscience |
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Personen und Körperschaften: | , , , , , |
In: | European Journal of Neuroscience, 15, 2002, 3, S. 465-474 |
Format: | E-Article |
Sprache: | Englisch |
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Wiley
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author_facet |
Carvalho, Ana Luísa Correia, Susana Faro, Carlos J. Duarte, Carlos B. Carvalho, Arsélio P. Pires, Euclides M. V. Carvalho, Ana Luísa Correia, Susana Faro, Carlos J. Duarte, Carlos B. Carvalho, Arsélio P. Pires, Euclides M. V. |
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author |
Carvalho, Ana Luísa Correia, Susana Faro, Carlos J. Duarte, Carlos B. Carvalho, Arsélio P. Pires, Euclides M. V. |
spellingShingle |
Carvalho, Ana Luísa Correia, Susana Faro, Carlos J. Duarte, Carlos B. Carvalho, Arsélio P. Pires, Euclides M. V. European Journal of Neuroscience Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons General Neuroscience |
author_sort |
carvalho, ana luísa |
spelling |
Carvalho, Ana Luísa Correia, Susana Faro, Carlos J. Duarte, Carlos B. Carvalho, Arsélio P. Pires, Euclides M. V. 0953-816X 1460-9568 Wiley General Neuroscience http://dx.doi.org/10.1046/j.0953-816x.2001.01881.x <jats:title>Abstract</jats:title><jats:p>We have previously reported that the activity of α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazole propionate (AMPA) receptors is potentiated by protein kinase C (PKC) in cultured chick retina amacrine neurons, and that constitutive PKC activity is necessary for basal AMPA receptor activity (<jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="#b1">Carvalho <jats:italic>et al</jats:italic>., 1998</jats:ext-link>). In this study, we evaluated the phosphorylation of the GluR4 subunit, which is very abundant in cultured amacrine neurons, to correlate it with the effects of PKC on AMPA receptor activity in these cells. <jats:sup>32</jats:sup>P‐labelling of GluR4 increased upon AMPA receptor stimulation or cell treatment with phorbol 12‐myristate 13‐acetate (PMA) before stimulating with kainate. By contrast, phosphorylation of GluR4 was not changed when PKC was inhibited by treating the cells with the selective PKC inhibitor GF 109203X before stimulation with kainate. We conclude that GluR4 is phosphorylated upon PKC activation and/or stimulation of AMPA receptors in cultured amacrine cells. Additionally, AMPA receptor activation with kainate in cultured chick amacrine cells leads to translocation of conventional and novel PKC isoforms to the cell membrane, suggesting that PKC could be activated upon AMPA receptor stimulation in these cells.</jats:p> Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons European Journal of Neuroscience |
doi_str_mv |
10.1046/j.0953-816x.2001.01881.x |
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Wiley |
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European Journal of Neuroscience |
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49 |
title |
Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons |
title_unstemmed |
Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons |
title_full |
Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons |
title_fullStr |
Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons |
title_full_unstemmed |
Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons |
title_short |
Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons |
title_sort |
phosphorylation of glur4 ampa‐type glutamate receptor subunit by protein kinase c in cultured retina amacrine neurons |
topic |
General Neuroscience |
url |
http://dx.doi.org/10.1046/j.0953-816x.2001.01881.x |
publishDate |
2002 |
physical |
465-474 |
description |
<jats:title>Abstract</jats:title><jats:p>We have previously reported that the activity of α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazole propionate (AMPA) receptors is potentiated by protein kinase C (PKC) in cultured chick retina amacrine neurons, and that constitutive PKC activity is necessary for basal AMPA receptor activity (<jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="#b1">Carvalho <jats:italic>et al</jats:italic>., 1998</jats:ext-link>). In this study, we evaluated the phosphorylation of the GluR4 subunit, which is very abundant in cultured amacrine neurons, to correlate it with the effects of PKC on AMPA receptor activity in these cells. <jats:sup>32</jats:sup>P‐labelling of GluR4 increased upon AMPA receptor stimulation or cell treatment with phorbol 12‐myristate 13‐acetate (PMA) before stimulating with kainate. By contrast, phosphorylation of GluR4 was not changed when PKC was inhibited by treating the cells with the selective PKC inhibitor GF 109203X before stimulation with kainate. We conclude that GluR4 is phosphorylated upon PKC activation and/or stimulation of AMPA receptors in cultured amacrine cells. Additionally, AMPA receptor activation with kainate in cultured chick amacrine cells leads to translocation of conventional and novel PKC isoforms to the cell membrane, suggesting that PKC could be activated upon AMPA receptor stimulation in these cells.</jats:p> |
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author | Carvalho, Ana Luísa, Correia, Susana, Faro, Carlos J., Duarte, Carlos B., Carvalho, Arsélio P., Pires, Euclides M. V. |
author_facet | Carvalho, Ana Luísa, Correia, Susana, Faro, Carlos J., Duarte, Carlos B., Carvalho, Arsélio P., Pires, Euclides M. V., Carvalho, Ana Luísa, Correia, Susana, Faro, Carlos J., Duarte, Carlos B., Carvalho, Arsélio P., Pires, Euclides M. V. |
author_sort | carvalho, ana luísa |
container_issue | 3 |
container_start_page | 465 |
container_title | European Journal of Neuroscience |
container_volume | 15 |
description | <jats:title>Abstract</jats:title><jats:p>We have previously reported that the activity of α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazole propionate (AMPA) receptors is potentiated by protein kinase C (PKC) in cultured chick retina amacrine neurons, and that constitutive PKC activity is necessary for basal AMPA receptor activity (<jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="#b1">Carvalho <jats:italic>et al</jats:italic>., 1998</jats:ext-link>). In this study, we evaluated the phosphorylation of the GluR4 subunit, which is very abundant in cultured amacrine neurons, to correlate it with the effects of PKC on AMPA receptor activity in these cells. <jats:sup>32</jats:sup>P‐labelling of GluR4 increased upon AMPA receptor stimulation or cell treatment with phorbol 12‐myristate 13‐acetate (PMA) before stimulating with kainate. By contrast, phosphorylation of GluR4 was not changed when PKC was inhibited by treating the cells with the selective PKC inhibitor GF 109203X before stimulation with kainate. We conclude that GluR4 is phosphorylated upon PKC activation and/or stimulation of AMPA receptors in cultured amacrine cells. Additionally, AMPA receptor activation with kainate in cultured chick amacrine cells leads to translocation of conventional and novel PKC isoforms to the cell membrane, suggesting that PKC could be activated upon AMPA receptor stimulation in these cells.</jats:p> |
doi_str_mv | 10.1046/j.0953-816x.2001.01881.x |
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imprint | Wiley, 2002 |
imprint_str_mv | Wiley, 2002 |
institution | DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229 |
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physical | 465-474 |
publishDate | 2002 |
publishDateSort | 2002 |
publisher | Wiley |
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recordtype | ai |
series | European Journal of Neuroscience |
source_id | 49 |
spelling | Carvalho, Ana Luísa Correia, Susana Faro, Carlos J. Duarte, Carlos B. Carvalho, Arsélio P. Pires, Euclides M. V. 0953-816X 1460-9568 Wiley General Neuroscience http://dx.doi.org/10.1046/j.0953-816x.2001.01881.x <jats:title>Abstract</jats:title><jats:p>We have previously reported that the activity of α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazole propionate (AMPA) receptors is potentiated by protein kinase C (PKC) in cultured chick retina amacrine neurons, and that constitutive PKC activity is necessary for basal AMPA receptor activity (<jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="#b1">Carvalho <jats:italic>et al</jats:italic>., 1998</jats:ext-link>). In this study, we evaluated the phosphorylation of the GluR4 subunit, which is very abundant in cultured amacrine neurons, to correlate it with the effects of PKC on AMPA receptor activity in these cells. <jats:sup>32</jats:sup>P‐labelling of GluR4 increased upon AMPA receptor stimulation or cell treatment with phorbol 12‐myristate 13‐acetate (PMA) before stimulating with kainate. By contrast, phosphorylation of GluR4 was not changed when PKC was inhibited by treating the cells with the selective PKC inhibitor GF 109203X before stimulation with kainate. We conclude that GluR4 is phosphorylated upon PKC activation and/or stimulation of AMPA receptors in cultured amacrine cells. Additionally, AMPA receptor activation with kainate in cultured chick amacrine cells leads to translocation of conventional and novel PKC isoforms to the cell membrane, suggesting that PKC could be activated upon AMPA receptor stimulation in these cells.</jats:p> Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons European Journal of Neuroscience |
spellingShingle | Carvalho, Ana Luísa, Correia, Susana, Faro, Carlos J., Duarte, Carlos B., Carvalho, Arsélio P., Pires, Euclides M. V., European Journal of Neuroscience, Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons, General Neuroscience |
title | Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons |
title_full | Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons |
title_fullStr | Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons |
title_full_unstemmed | Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons |
title_short | Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons |
title_sort | phosphorylation of glur4 ampa‐type glutamate receptor subunit by protein kinase c in cultured retina amacrine neurons |
title_unstemmed | Phosphorylation of GluR4 AMPA‐type glutamate receptor subunit by protein kinase C in cultured retina amacrine neurons |
topic | General Neuroscience |
url | http://dx.doi.org/10.1046/j.0953-816x.2001.01881.x |