Prostaglandin-concentration-dependent desensitization of adenylate cyclase in human erythroleukaemia (HEL) cells is abolished by pertussis toxin and enhanced by induction by dimethyl sulphoxide.
Prostaglandin-regulated cyclic AMP metabolism in human erythroleukaemia (HEL) cells was similar to that previously described in platelets [Ashby (1989) Mol. Pharmacol. 36, 866-873], displaying prostaglandin-concentration-dependent desensitization that could be explained by the presence of separate stimulatory and inhibitory prostaglandin receptors. Pertussis toxin abolished prostaglandin-concentration-dependent desensitization, indicating that the process is mediated through a pertussis toxin-sensitive GTP-binding protein. Treatment of HEL cells for 4 days with the inducer dimethyl sulphoxide enhanced prostaglandin-concentration-dependent desensitization, but did not alter the initial rate of cyclic AMP synthesis or the amount of Gi2 alpha measured by immunoblotting, suggesting that the inhibitory receptor was selectively induced by changing the cells to a more platelet-like form.
Ashby
B
B
Department of Pharmacology, Temple University Medical School, Philadelphia, PA 19140.
Almonor
G O
GO
Wernick
E
E
Selak
M A
MA
D037361:Adenylate Cyclase Toxin; D000262:Adenylyl Cyclases / Q000187:drug effects* / Q000378:metabolism; D000527:Alprostadil / Q000494:pharmacology*; D000242:Cyclic AMP / Q000378:metabolism; D004121:Dimethyl Sulfoxide / Q000494:pharmacology*; D004837:Epinephrine / Q000494:pharmacology; D006801:Humans; D016285:Iloprost / Q000494:pharmacology; D004915:Leukemia, Erythroblastic, Acute / Q000378:metabolism*; D037342:Pertussis Toxin; D014407:Tumor Cells, Cultured; D010566:Virulence Factors, Bordetella / Q000494:pharmacology*
D037361:Adenylate Cyclase Toxin; D010566:Virulence Factors, Bordetella; D000242:Cyclic AMP; D037342:Pertussis Toxin; D000262:Adenylyl Cyclases; D000527:Alprostadil; D016285:Iloprost; D004837:Epinephrine; D004121:Dimethyl Sulfoxide