Protein Kinase C Potentiates Capacitative Ca^<2+> Entry That Links to Steroidogenesis in Bovine Adrenocortical Cells

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概要

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• I investigated the role of protein kinase C(PKC) in regulation of the capacitative Ca2+ entry and steroidogenesis in bovine adrenocortical(BA)cells.Thapsigargin(TG)-treatment depleted intracellular Ca2+ stores followed by induction of Ca2+ influx from the extracellular pool and also increasing of Mn2+ influx as an indicator of divalent cation influx in BA cells.Calphostin C, a PKC inhibitor, inhibited the TG-induced [Ca2+]i elevation dose-dependently(0.1-1μM)and attenuated Mn2+ entry.Phorbol 12-myristate 13-acetate(PMA), an activator of PKC, potentiated the elevation of[Ca2+]i and enhanced Mn2+ entry by TG treatment.These results suggest that PKC may modulate capacitative Ca2+ entry in BA cells.In the presence of extracellular Ca2+, TG enhanced cortisol production in BA cells.Calphostin C attenuated the TG-induced steroidogenesis dose-dependently(0.25-1μM).PMA enhanced the steroidogenesis dose-dependently(1-100nM).These results suggested that PKC may have a modulatory effect on the capacitative Ca2+ entry that links to steroidogenesis in BA cells.

• 社団法人 日本薬理学会の論文
• 2000-03-01

著者

• KONDO ICHIRO

  Department of Anesthesiology, Jikei University School of Medicine

• Kondo Ichiro

  Department Of Anesthesiology Jikei University School Of Medicine

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• Protein Kinase C Potentiates Capacitative Ca^ Entry That Links to Steroidogenesis in Bovine Adrenocortical Cells

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