Foetal-calf serum stimulates a pertussis-toxin-sensitive high-affinity GTPase activity in rat glioma C6 BU1 cells
- 15 July 1987
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 245 (2) , 501-505
- https://doi.org/10.1042/bj2450501
Abstract
Cellular proliferation of rat glioma C6 BU1 cells in tissue culture is dependent on the presence of either calf or foetal-calf serum in the medium. Foetal-calf serum stimulated a high-affinity GTPase in membranes derived from C6 BU1 cells. Pretreatment of the cells with pertussis toxin decreased the high-affinity GTPase activity substantially, and attenuated the foetal-calf-serum-stimulated increase in this GTPase activity. Cholera toxin, in contrast, did not modulate the response to foetal-calf serum. Foetal-calf serum did not inhibit adenylate cyclase activity in membranes of these cells, indicating that the G-protein that was stimulated by foetal-calf serum was not Gi (the inhibitory one). Although the nature of the specific component of foetal-calf serum responsible for this pertussis-toxin-sensitive receptor-mediated stimulation of high-affinity GTPase activity has not been identified, it was mimicked neither by bombesin, which can stimulate inositol phospholipid turnover via a guanine nucleotide binding protein, nor by platelet-derived growth factor, which is present in substantial concentrations in foetal-calf serum. This report represents the first demonstration of a pertussis-toxin-substrate-mediated response in this cell line and provides further evidence that G-proteins other than Gi can be functionally inactivated by pertussis toxin.This publication has 26 references indexed in Scilit:
- [57] Sequencing end-labeled DNA with base-specific chemical cleavagesPublished by Elsevier ,2004
- Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain.Journal of Biological Chemistry, 1984
- Use of an antiserum against phosphotyrosine for the identification of phosphorylated components in human fibroblasts stimulated by platelet-derived growth factor.Journal of Biological Chemistry, 1984
- Reduction of epidermal growth factor receptor affinity by heterologous ligands: Evidence for a mechanism involving the breakdown of phosphoinositides and the activation of protein kinase CBiochemical and Biophysical Research Communications, 1984
- ADP-ribosylation of adenylate cyclase by pertussis toxin. Effects on inhibitory agonist binding.Journal of Biological Chemistry, 1984
- Characterization of the receptor for platelet-derived growth factor on human fibroblasts. Demonstration of an intimate relationship with a 185,000-Dalton substrate for the platelet-derived growth factor-stimulated kinase.Journal of Biological Chemistry, 1983
- ADP ribosylation of the specific membrane protein of C6 cells by islet-activating protein associated with modification of adenylate cyclase activity.Journal of Biological Chemistry, 1982
- Opiates inhibit adenylate cyclase by stimulating GTP hydrolysis.Proceedings of the National Academy of Sciences, 1981
- Morphine receptors as regulators of adenylate cyclase activity.Proceedings of the National Academy of Sciences, 1975
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951