Opioid peptides: aspects of their origin, release and metabolism.
At the present time there is evidence for two families of related peptides which act as ligands for opiate receptor sites. The endorphin group of peptides are derived from the ACTH/LPH precursor pro-opiocortin. The enkephalins appear to be formed from a separate precursor or precursors that have yet to be fully characterized. There appear to be a number of different types of opiate receptors and this may be related to the multiplicity of peptide ligands that have so far been identified. The enkephalins and related peptides appear to have a much wider distribution than the endorphins but the latter may act as circulating hormones unlike the enkephalins. It is likely that both endorphins and enkephalins are involved in sensory modulation processes and release of these peptides has been demonstrated during brain stimulation for pain relief. The enkephalins are very rapidly inactivated by tissue proteases, the aminopeptidases appear largely responsible for the inactivation of exogenously administered enkephalins but the dipeptidyl carboxypeptidase, termed enkephalinase, may have a special inactivating function at enkephalinergic synapses. Evidence will be presented for the biosynthesis, the release and inactivation of the enkephalins relating to the above points.
D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000378:metabolism*; D003342:Corpus Striatum / Q000378:metabolism; D004723:Endorphins / Q000096:biosynthesis / Q000378:metabolism*; D004745:Enkephalins / Q000096:biosynthesis / Q000378:metabolism*; D051379:Mice; D014176:Protein Biosynthesis; D011957:Receptors, Opioid / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism; D013329:Structure-Activity Relationship
D004723:Endorphins; D004745:Enkephalins; D011957:Receptors, Opioid