Abstract
Specific binding of 3H-labeled[3-Me-His 2]TRH([ 3H]MeTRH) to membranes of rabbit spinal cord (thoracic) involved a homogeneous population of high-affinity sites ( K d = 2.7 ± 0.17 (n= 5)nM, B max= 204 – 12(5)fmol/mg protein). TRH analogs competed for the binding in the following rank order of potency: MeTRH>TRH>TRH-Gly-NH 2 >Ser-His-Pro-NH 2 >Thr-His-Pro-NH 2 > pGlu-His-Pro-NH-C 2H 5>TRH-free acid. Competition experiments with rat amygdala, run in parallel with rabbit spinal cord, revealed a closely similar pattern of activity. These properties help identify binding sites in the rabbit spinal cord as physiological receptors for TRH. The binding sites resemble receptors previously demonstrated in pituitary and CNS tissues of other species. The densities of [ 3H]MeTRH binding sites in different segments were generally similar, although density in the thoracic segment appeared to be somewhat higher. In all segments, binding seemed to be enriched in the dorsal gray matter. Dorsal roots and their associated ganglia, however, displayed little or no binding.
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