Localization and characterization of somatostatin binding sites in the mouse retina

We studied the binding of [ 125I]Tyr 11-somatostatin-14 and [ 125I]Leu 8, d-Trp 22, Tyr 25-somatostatin-28 to frozen, unfixed sections of C57BL/6J mouse eyes with autoradiography. Specific binding of both ligands occurred in 3 maxima, a broad band extending from the retinal ganglion cell to the inner nuclear layers, a narrow and inconstant band over the outer plexiform layer, and a band over the retinal pigment epithelium and choroid. We quantified the label over the inner plexiform layer and found evidence for a single, saturable binding site after Scatchard analysis of saturation binding data. With [ 125I]Tyr 11-somatostatin-14 the dissociation constant ( K d) was 1.48 nM and the total number of binding sites ( B max) was 68 fmol/mg protein; in competition experiments the inhibitory binding constant ( K i) was 900 pM for somatostatin-14 and 350 pM for somatostatin-28. With [ 125I]Leu 8, d-Trp 22, Tyr 25-somatostatin-28, K d was 625 pM and B max was 69 fmol/mg protein: in competition experiments K i was 4.58 nM for somatostatin-14 and 710 pM for somatostatin-28. These results demonstrate the existence of somatostatin receptors in the inner plexiform layer of the retina that appear to have greater specificity for somatostatin-28 than for somatostatin-14.