title: Dermorphins, opioid peptides from amphibian skin, act on opioid receptors of mouse neuroblastoma x rat glioma hybrid cells.
abstract: Dermorphin and its Hyp6 analogue are opiate-like heptapeptides originally discovered in frog skin and characterized by the presence of a D-Ala2 residue in their sequence. They were assayed for their capacity to compete with [3H]Leu-enkephalin for binding to opioid receptors in membranes of neuroblastoma x glioma hybrid cells. In the presence of 7 nM-[3H]Leu-enkephalin, the concentrations at which they caused 50% inhibition of [3H]enkephalin binding (IC50 values) are 0.1 micro M and 0.3 micro M, respectively. In contrast, the synthetic L-Ala2-dermorphin shows very low affinity for the opioid receptors. In addition, like other opioid peptides, dermorphin and hyp6-dermorphin inhibit the elevation by prostaglandin E1 (PGE1) of the level of adenosine 3':5'-cyclic monophosphate (cyclic AMP) (IC50 values 0.2 micro M and 0.4 micro M, respectively). The inhibition is prevented by the opiate antagonist naloxone, L-Ala2-dermorphin is at least three orders of magnitude less potent in inhibiting the PGE1-evoked increase in the level of cyclic AMP. The results show that peptides with an amino acid sequence quite different from that of the enkephalins can bind to opioid receptors of the hybrid cells.
mesh_terms: D000663:Amphibians; D000818:Animals; D001667:Binding, Competitive; D002460:Cell Line; D004743:Enkephalin, Leucine; D004745:Enkephalins / Q000378:metabolism; D005910:Glioma; D006822:Hybrid Cells / Q000378:metabolism*; D007700:Kinetics; D051379:Mice; D009447:Neuroblastoma; D009842:Oligopeptides / Q000494:pharmacology*; D018847:Opioid Peptides; D051381:Rats; D011957:Receptors, Opioid / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D004745:Enkephalins; D009842:Oligopeptides; D018847:Opioid Peptides; D011957:Receptors, Opioid; C030058:dermorphin; D004743:Enkephalin, Leucine; C030059:dermorphin, 4-Hyp(6)-