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Binding studies of [H]Lyngbyatoxin A and [H]debromoaplysiatoxin to the phorbol ester receptor in a mouse epidermal particulate fraction
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1986
Year
Signal TransductionCatalytic Triton-proton ExchangeBiochemistryPhorbol Ester ReceptorLyngbyatoxin AMedicineUnlabeled TpaNatural SciencesMechanism Of ActionReceptor (Biochemistry)ToxicologyExperimental ToxicologyChemical BiologyPharmacologyCell SignalingToxicological Mechanism
The preparation of [3H]lyngbyatoxin A by catalytic triton-proton exchange of lyngbyatoxin A and [3H]debromoaplysiatoxin by tritiation-debromination of aplysiatoxin is described. The dose-response curves for the binding of [3H]lyngbyatoxin A and [3H]debromoaplysiatoxin to a mouse epidermal particulate fraction are virtually the same as the one previously described for [3H]12-O-tetradecanoylphorbol-13-acetate ([3H]TPA). The specific binding of [3H]TPA, [3H]-lyngbyatoxin A and [3H]debromoaplysiatoxin to the mouse epidermal particulate fraction is inhibited to the same degree by unlabeled TPA, teleocidin, lyngbyatoxin A, aplysiatoxin and debromoaplysiatoxin. This study indicates that TPA, lyngbyatoxin A and debromoaplysiatoxin bind to the same high affinity receptor in mouse skin.