Abstract
Transfection of a bovine stomach cDNA encoding for an NK 2 receptor into murine fibroblasts produced a clone that exhibited specific binding of NKA, a selective NK 2 agonist. In these transfected cells, NKA mediated hydrolysis of phosphatidyl-inositol (PI) with an EC 50 value of 10 nM and an E max value 7.2 times basal level. Dose response curves of IP 1 accumulation by two other neurokinin agonists demonstrated a rank order of potency of NKA>SP>>senktide. This suggests that the de novo receptor expressed in these transfected cells is functionally coupled to the PI hydrolysis pathway. Stable in vitro expression of NK 2 receptors in a eukaryotik cell line can provide a means of correlating the structurally defined receptor with its ligand binding properties and its functional coupling mechanisms.
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