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Bradykinin-induced phosphoinositide-dependent responses in protein kinase C down-regulated NCB-20 cells

Authors
Journal
Neurochemistry International
0197-0186
Publisher
Elsevier
Publication Date
Volume
18
Issue
3
Identifiers
DOI: 10.1016/0197-0186(91)90175-d
Disciplines
  • Biology

Abstract

Abstract Long-term (12 h) incubation of NCB-20 neuroblastoma × Chinese hamster brain cell hybrid cells with phorbol dibutylate caused a decrease in the enzyme activity of protein kinase C (PKC). Under these conditions, the formation of inositol 1,4,5-trisphosphate [Ins(1,4,5)P 3] and the mobilization of intracellular Ca 2+ triggered by bradykinin (BK), were significantly increased. The alterations in BK-triggered membrane currents in the PKC down-regulated cells were also observed: enhancement of outward currents and decreased inward currents. These results strongly suggested that down-regulation of PKC enhanced BK-induced phosphoinositide metabolism by relieving from the negative feedback control operating between the receptor and phospholipase C, and that the increased Ca 2+ responses due to accumulated Ins(1,4,5)P 3 lead to enhanced outward currents.

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