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 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
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series European Journal of Neuroscience
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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
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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>
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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