Binding proteins for a peptide hormone in the shrimp, Sicyonia ingentis: evidence from photoaffinity labeling with red pigment concentrating hormone analogs.

Two photoaffinity analogs of the crustacean erythrophore (red pigment) concentrating hormone (RPCH) have been synthesized and shown to cause pigment concentration in the shrimp Sicyonia ingentis. These two modified oligopeptides have azidosalicylamide groups which allow introduction of an 125I label and enable photochemically induced covalent attachment to a specific binding site. Incubation of [125I]-ASA-Glu1-CC-2 with the 100,000g membrane pellet and cytosol fraction from epidermis, eyestalks, muscle, and central nervous system (CNS), followed by irradiation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and autoradiography results in covalent modification of certain protein bands in the membranes of selected tissues. Two such proteins were observed in neural tissues and showed competitive displacement by excess RPCH, indicative of specific high-affinity binding. This is the first report of peptide hormone-binding proteins in an invertebrate and provides further evidence of a role for RPCH as a neurotransmitter in the CNS.