Summary
We have developed two types of hybridomas producing monoclonal antibodies to the turkey erythrocyte β1-adrenergic receptor in order to study the β-adrenergic-cAMP system of epidermis. Splenic cells from BALB/c mice immunized with partially purified turkey erythrocyte β1-adrenergic were fused with mouse myeloma cell line SP2/0-Ag14. Five hybridomas of 17 positive cells producing antibodies which could precipitate soluble turkey erythrocyte β1-receptors were cloned by the limiting dilution method. The antibodies cross-reacted with β- and β2-adrenergic receptors and stained epidermal basal cells with immunocytochemical techniques. Neither type of antibody interfered with the antagonist binding, i.e., all antibodies bound to sites other than the ligand binding site on the surface. One type of antibody inhibited epinephrine-stimulated adenylate cyclase activity in our “leaky” epidermal cell system. The data suggest that the antibody interferes with the coupling of the receptor to the regulatory protein.
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Itami, S., Tsutsui, M., Kino, J. et al. Monoclonal antibodies to the β-andrenergic receptor: Modulation of catecholamine-sensitive adenylate cyclase by the antibody. Arch Dermatol Res 278, 377–381 (1986). https://doi.org/10.1007/BF00418166
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DOI: https://doi.org/10.1007/BF00418166