The expression of a cloned Drosophila octopamine/tyramine receptor (Oc
tyR99AB) is described in Xenopus oocytes. Agonist stimulation of OctyR
99AB receptors increased intracellular Ca2+ levels monitored as change
s in the endogenous inward Ca2+-dependent chloride current. The recept
or is preferentially sensitive to biogenic amines with a single hydrox
yl on the aromatic ring. The G-protein, G(alpha i), appears to be invo
lved in the coupling of the receptor to the production of intracellula
r calcium signals, since the effect is pertussis-toxin sensitive and i
s blocked or substantially reduced in antisense knockout experiments u
sing oligonucleotides directed against G(alpha i) but not by those dir
ected against G(alpha o), G(alpha q), and G(alpha 11).G alpha 11. The
increase in intracellular calcium levels induced by activation of the
OctyR99AB receptor can potentiate the ability of activation of a co-ex
pressed beta(2)-adrenergic receptor to increase oocyte cyclic AMP leve
ls. A comparison of the pharmacological coupling of OctyR99AB to diffe
rent second messenger systems when expressed in Xenopus oocytes with p
revious studies on the expression of the receptor in a Chinese hamster
ovary cell line suggests that the property of agonist-specific coupli
ng of the receptor to different second messenger systems may be cell-s
pecific, depending upon the G-protein environment of any particular ce
ll type. (C) 1997 Elsevier Science B.V.