Chromogranins belong to an evolutionarily conserved family of proteins that
serve as neuropeptide pro-proteins, besides having other functions. The se
cretoeranin-II-derived peptide secretoneurin is a 33-amino-acid polypeptide
generated by proteolytic cleavage at paired dibasic sequences that exerts
its effect by binding to specific receptors. Secretoneurin receptors have b
een kinetically and functionally characterized indicating that they an G-pr
otein linked. Localization of secretoneurin and functional studies have hel
ped to elucidate roles for secretoneurin, ranging from effects in the centr
al nervous system to the modulation of the inflammatory response in the per
iphery. It has been shown that secretoneurin possesses biologic activities
such as stimulation of dopamine release from striatal neurons and activatio
n of monocyte migration, suggesting that the peptide may modulate both neur
otransmission and inflammatory response. With an array of actions as divers
e as that seen with other sensory neuropeptides, there is scope for numerou
s studies and therapeutic possibilities. (C) 2000 Elsevier Science Inc. All
rights reserved.