Bradykinin stimulates GTP hydrolysis in NG108-15 membranes by a high-affinity, pertussis toxin-insensitive GTPase
- 17 February 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 196 (2), 279-283
- https://doi.org/10.1016/0014-5793(86)80263-0
Abstract
In membranes of neuroblastoma × glioma hybrid (NG108-15) cells, bradykinin (EC50 ≅ 5 nM) stimulates GTP hydrolysis by a high-affinity GTPase (Km ≅ 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 Ni, 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.Keywords
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