Involvement of protein kinase C in Ca2+ -signaling pathways to activation of AP-1 DNA-binding activity evoked via NMDA- and voltage-gated Ca2+ channels

Ken Ichi Ohtani, Hiroaki Sakurai, Esther Oh, Emi Iwata, Tomofusa Tsuchiya, Masaaki Tsuda

Research output: Contribution to journalArticle

Abstract

Stimulation of cultured cerebellar granule cells with N-methyl-D-aspartate (NMDA) or kainic acid (KA) leads to activation of activator protein-1 (AP-1) DNA-binding activity, which can be monitored by an increase in 12-O-tetradecanoylphorbol 13-acetate (TPA)-responsive element (TRE)-binding activity, in concert with c-fos induction. For this increase in TRE-binding activity, Ca2+ influx across the plasma membrane is essential. Treatment of cells with an intracellular Ca2+ chelator, BAPTA-AM, abolished this increase. Close correspondence between the dose-response curves of 45Ca2+ uptake and TRE-binding activity by NMDA or KA suggested that Ca2+ influx not only triggered sequential activation of Ca2+-signaling processes leading to the increase in TRE-binding activity, but also controlled its increased level. Stimulation of non-NMDA receptors by KA mainly caused Ca2+ influx through voltage-gated Ca2+ channels, whereas stimulation of NMDA receptors caused Ca2+ influx through NMDA-gated ion channels. The protein kinase C (PKC) inhibitors staurosporine and calphostin C inhibited the increase in TRE-binding activity caused by NMDA and KA at the same concentration at which they inhibited that caused by TPA. Furthermore, down-regulation of PKC inhibited the increase in TRE-binding activity by NMDA and KA. Thus, a common pathway that includes PKC could, at least in part, be involved in the Ca2+-signaling pathways for the increase in TRE-binding activity coupled with the activation of NMDA- and non-NMDA receptors.

Original languageEnglish (US)
Pages (from-to)605-614
Number of pages10
JournalJournal of Neurochemistry
Volume65
Issue number2
StatePublished - Aug 1995
Externally publishedYes

Fingerprint

Transcription Factor AP-1
N-Methylaspartate
Kainic Acid
Protein Kinase C
Chemical activation
DNA
Electric potential
D-Aspartic Acid
Tetradecanoylphorbol Acetate
Acetates
Staurosporine
Protein C Inhibitor
Cell membranes
Protein Kinase Inhibitors
Chelating Agents
N-Methyl-D-Aspartate Receptors
Ion Channels
Down-Regulation
Cells
Cell Membrane

Keywords

  • AP-1
  • c-fos induction
  • Ca influx
  • Cerebellar granule cells
  • Glutamate receptors
  • Protein kinase C

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Involvement of protein kinase C in Ca2+ -signaling pathways to activation of AP-1 DNA-binding activity evoked via NMDA- and voltage-gated Ca2+ channels. / Ohtani, Ken Ichi; Sakurai, Hiroaki; Oh, Esther; Iwata, Emi; Tsuchiya, Tomofusa; Tsuda, Masaaki.

In: Journal of Neurochemistry, Vol. 65, No. 2, 08.1995, p. 605-614.

Research output: Contribution to journalArticle

Ohtani, Ken Ichi ; Sakurai, Hiroaki ; Oh, Esther ; Iwata, Emi ; Tsuchiya, Tomofusa ; Tsuda, Masaaki. / Involvement of protein kinase C in Ca2+ -signaling pathways to activation of AP-1 DNA-binding activity evoked via NMDA- and voltage-gated Ca2+ channels. In: Journal of Neurochemistry. 1995 ; Vol. 65, No. 2. pp. 605-614.
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abstract = "Stimulation of cultured cerebellar granule cells with N-methyl-D-aspartate (NMDA) or kainic acid (KA) leads to activation of activator protein-1 (AP-1) DNA-binding activity, which can be monitored by an increase in 12-O-tetradecanoylphorbol 13-acetate (TPA)-responsive element (TRE)-binding activity, in concert with c-fos induction. For this increase in TRE-binding activity, Ca2+ influx across the plasma membrane is essential. Treatment of cells with an intracellular Ca2+ chelator, BAPTA-AM, abolished this increase. Close correspondence between the dose-response curves of 45Ca2+ uptake and TRE-binding activity by NMDA or KA suggested that Ca2+ influx not only triggered sequential activation of Ca2+-signaling processes leading to the increase in TRE-binding activity, but also controlled its increased level. Stimulation of non-NMDA receptors by KA mainly caused Ca2+ influx through voltage-gated Ca2+ channels, whereas stimulation of NMDA receptors caused Ca2+ influx through NMDA-gated ion channels. The protein kinase C (PKC) inhibitors staurosporine and calphostin C inhibited the increase in TRE-binding activity caused by NMDA and KA at the same concentration at which they inhibited that caused by TPA. Furthermore, down-regulation of PKC inhibited the increase in TRE-binding activity by NMDA and KA. Thus, a common pathway that includes PKC could, at least in part, be involved in the Ca2+-signaling pathways for the increase in TRE-binding activity coupled with the activation of NMDA- and non-NMDA receptors.",
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AU - Ohtani, Ken Ichi

AU - Sakurai, Hiroaki

AU - Oh, Esther

AU - Iwata, Emi

AU - Tsuchiya, Tomofusa

AU - Tsuda, Masaaki

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AB - Stimulation of cultured cerebellar granule cells with N-methyl-D-aspartate (NMDA) or kainic acid (KA) leads to activation of activator protein-1 (AP-1) DNA-binding activity, which can be monitored by an increase in 12-O-tetradecanoylphorbol 13-acetate (TPA)-responsive element (TRE)-binding activity, in concert with c-fos induction. For this increase in TRE-binding activity, Ca2+ influx across the plasma membrane is essential. Treatment of cells with an intracellular Ca2+ chelator, BAPTA-AM, abolished this increase. Close correspondence between the dose-response curves of 45Ca2+ uptake and TRE-binding activity by NMDA or KA suggested that Ca2+ influx not only triggered sequential activation of Ca2+-signaling processes leading to the increase in TRE-binding activity, but also controlled its increased level. Stimulation of non-NMDA receptors by KA mainly caused Ca2+ influx through voltage-gated Ca2+ channels, whereas stimulation of NMDA receptors caused Ca2+ influx through NMDA-gated ion channels. The protein kinase C (PKC) inhibitors staurosporine and calphostin C inhibited the increase in TRE-binding activity caused by NMDA and KA at the same concentration at which they inhibited that caused by TPA. Furthermore, down-regulation of PKC inhibited the increase in TRE-binding activity by NMDA and KA. Thus, a common pathway that includes PKC could, at least in part, be involved in the Ca2+-signaling pathways for the increase in TRE-binding activity coupled with the activation of NMDA- and non-NMDA receptors.

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