Bradykinin stimulates GTP hydrolysis in NG108‐15 membranes by a high‐affinity, pertussis toxin‐insensitive GTPase

FEBS Letters

Greiner, Claudia¹  Jakobs, Karl H.¹  Zubin, Palmira¹  Grandt, Rüdiger¹ 

[1] Pharmakologisches Institut der Universität Heidelberg, Im Neuenheimer Feld 366, D-6900 Heidelberg, FRG

关键词: Bradykinin (NG 108-15 cell) Guanine nucleotide-binding protein GTPase Pertussis toxin Phosphoinositide metabolism;   

DOI  :  10.1016/0014-5793(86)80263-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In membranes of neuroblastoma × glioma hybrid (NG108-15) cells, bradykinin (EC₅₀ ≅ 5 nM) stimulates GTP hydrolysis by a high-affinity GTPase (K_m ≅ 0.2 μM). The octapeptide, des-Arg⁹-bradykinin, was inactive. Stimulation of GTP hydrolysis by bradykinin and an opioid agonist was partially additive. Treatment of NG108-15 cells with pertussis toxin, which inactivates N_i, eliminated GTPase stimulation by the opioid agonist but not by bradykinin. The data suggest that bradykinin activates in NG108-15 membranes a guanine nucleotide-binding protein which is not sensitive to pertussis toxin and which may be involved in brady-kinin-induced stimulation of phosphoinositide metabolism in these cells.

【 授权许可】

Unknown