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

Abstract:

:Long-term (12 h) incubation of NCB-20 neuroblastoma x 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.

journal_name

Neurochem Int

authors

Okano Y,Higashida H,Tao F,Sakai T,Nozawa Y

doi

10.1016/0197-0186(91)90175-d

subject

Has Abstract

pub_date

1991-01-01 00:00:00

pages

419-24

issue

3

eissn

0197-0186

issn

1872-9754

pii

0197-0186(91)90175-D

journal_volume

18

pub_type

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