Abstract
Previous studies have shown that the neuronal glycine receptor antagonist, strychnine, mimics the cytoprotective effects of glycine in renal proximal tubules (RPT) (1). The goal of this study was to identify and characterize the site of action of strychnine. 3H-Strychnine bound to RPT in a saturable and reversible manner, and was displaced by unlabelled strychnine (IC 50=0.87 mM and a B max=57 nmol/mg protein). However, strychnine binding was not inhibited by glycine or related cytoprotective amino acids. Furthermore, the neurotoxicants bicuculline and norharmane, which share the cytoprotective properties of strychnine, inhibited 3H-strychnine binding. These data support the existence of novel low-affinity strychnine binding site on the RPT plasma membrane that prevents toxic cell death.
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