K receptor activities of the three opioid peptide families.

A large number of opioid peptides derived from the three established precursors, pro-opiomelanocortin (POMC), pro-enkephalin A (pro-enk A), and pro-enkephalin B (pro-enk B) were tested for their ability to inhibit electrically induced contractions of the isolated rabbit vas deferens, a preparation sensitive to k but not to mu opioid ligands. In the presence of enzyme inhibitors, all peptides exhibit roughly similar potencies, but the shorter peptides display lower potencies in the absence of enzyme inhibitors. This suggests that the loss in activity is due to their enzymatic degradation. It is concluded that the pro-enk B gene codes peptides with high k-receptor activities, whereas peptides produced by the POMC gene are devoid of k-receptor activity and the peptides, coded by the pro-enk A gene exhibit weak to moderate k-receptor activity.