Secondary processing of neurohormones: intracellular proteolytic cleavage of beta-endorphin generates new active neuropeptides.
The following short review considers the physiological significance of naturally occurring peptide fragments derived from intracellular secondary processing of beta-endorphin (beta-EP). Particular attention will be given to the question of whether truncated and/or derivatized forms of beta-EP are true end products subject to release and regulation and might serve important new functions. Since collectively endorphins may play a variety of neurobiological roles which may or may not be mediated through analgesic receptors, most of the material reviewed herein deals with the induction of analgesia, the most commonly used measure of the opiate's acute effects.
Nicolas
P
P
Institut Jacques-Monod, Université Paris VII, France.
D000595:Amino Acid Sequence; D001921:Brain / Q000378:metabolism; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000235:genetics / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000502:physiology; D010902:Pituitary Gland / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D001615:beta-Endorphin / Q000378:metabolism*
D009479:Neuropeptides; D001615:beta-Endorphin; D010447:Peptide Hydrolases