Abstract
Melatonin receptors in the rabbit spinal cord were studied. Using in vitro quantitative autoradiography we have localized and characterized 2-[ 125I]iodomelatonin ([ 125I]MEL) binding sites in the central gray substance (lamina X) of the rabbit spinal cord. Saturation study revealed a single class of high affinity binding sites in the central gray substance with an equilibrium dissociation constant ( K d) o 38.8 ± 5.25 pM and a maximum number of binding sites of 5.69 ± 0.84 fmol/mg protein in the mid-light period. These [ 125I]MEL binding sites were highly specific for melatonin. Coincubation with 10 μM or 50 μM guanosine 5′- O-(3-thiotriphosphate) produced a significant change in K d. These results suggest that melatonin receptors in the rabbit spinal cord are coupled to a guanine-nucleotide-bind protein (G-protein). Our studies suggest that melatonin exerts a direct action on the rabbit spinal cord.
Published Version
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