With the use of [125I]iodocyanopindolol as a beta-receptor ligand, beta-receptors were identified and characterized in human amnion tissue. [125I]lodocyanopindolol was found to bind to a total particulate fraction prepared from amnion tissue obtained at term. At low concentrations of [125I]iodocyanopindolol, more than 80% of total [125I]iodocyanopindolol bound was at specific high-affinity sites and could be displaced by an excess of (+/-)-propranolol. The Kd and Bmax for binding of [125I]iodocyanopindolol to amnion beta-receptors were 10.1 +/- 1.1 pM and 46.8 +/- 3.2 fmol/mg protein, respectively. Analysis of the competition for binding to amnion beta-receptors between [125I]iodocyanopindolol and ligands that discriminated between beta 1- and beta 2-receptors revealed that the beta-receptors of human amnion were almost entirely of the beta 2-subtype. The density of beta-receptors found in the amnion at term was approximately three times that found early in the second trimester of gestation. The beta-receptors in human amnion appear to be functional since the in vitro exposure of amnion tissue pieces to isoproterenol (10(-5)M), resulted in a fivefold increase in the intracellular concentration of cyclic adenosine monophosphate. The presence of beta-receptors in the amnion is in keeping with the proposed importance of the catecholamines found in amniotic fluid in the regulation of prostaglandin production by the amnion.