Protein Kinase C Potentiates Capacitative Ca2+ Entry That Links to Steroidogenesis in Bovine Adrenocortical Cells

The Japanese Journal of Pharmacology

Ichiro Kondo¹ 

[1] Department of Anesthesiology,Jikei University School of Medicine,3-25-8,Nishi-Shinbashi,Minato-ku,Tokyo 105-8461,Japan

关键词: Capacitative Ca2+ entry;    Protein kinase C;    Adrenocortical cell;   

DOI  :  10.1254/jjp.82.210

学科分类：药理学

来源: Nihon Yakuri Gakkai Henshuubu / Japanese Pharmacological Society

【 摘 要 】

References(31)Cited-By(2)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.

【 授权许可】

Unknown