In vivo binding of a biologically active oligopeptide in vegetative buds of the scyphozoan Cassiopea andromeda: demonstration of receptor-mediated induction of metamorphosis

Vegetative buds of Cassiopea andromeda (Cnidaria, Scyphozoa) metamorphose into polyps in the presence of short synthetic peptides containing proline as the preterminal amino acid at the carboxyl terminus. In an in vivo assay, the binding of the biologically active hexapeptide ¹⁴C-dansyl-GPGGPA in buds was shown to be specific and saturable. Scatchard plot analysis of the specific binding data revealed a dissociation constant (K _D) of about 7 M. The total number of receptors was calculated to be approximately 1×10¹⁰ bud^-1 under saturation conditions. In correlation with the results of prior investigations, our finding of receptor-mediated induction of metamorphosis strongly supports the hypothesis that binding of biologically active peptides to receptors leads to initiation of phosphatidylinositol breakdown and activation of protein kinase C.