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pubmed-article:2984031pubmed:abstractTextHomogenates of fresh bovine corneal endothelium and of cells from primary cultures exhibited high affinity binding of [3H]-dihydroalprenolol, a specific beta-adrenergic antagonist. The binding was rapid and reversible. Specific binding of the radioligand in each preparation was saturable with half-maximal binding occurring at 0.5 nM. Homogenates of fresh tissue consistently showed a higher maximal binding capacity than did those from cell cultures. Both homogenates bound adrenergic agents in a manner consistent with the labelling of beta-adrenergic receptors. The relative affinities of epinephrine and norepinephrine indicated that beta-adrenergic receptors in both preparations are of the beta 2 subtype. The beta-adrenergic agonist, isoproterenol, increased the cAMP content of intact, cultured endothelial cells 27-fold over control. This effect was completely blocked by the beta-adrenergic antagonist, propranolol. Bovine corneal endothelial cells in primary culture contain beta-adrenergic receptors which are essentially identical to those from in vivo sources and appear to be linked functionally to cAMP synthesis in these cells.lld:pubmed
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pubmed-article:2984031pubmed:articleTitleCharacterization of beta-adrenergic receptors in fresh and primary cultured bovine corneal endothelium.lld:pubmed
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