PHEROMONE BIOSYNTHESIS ACTIVATING NEUROPEPTIDES - FUNCTIONS AND CHEMISTRY

Citation
Pea. Teal et al., PHEROMONE BIOSYNTHESIS ACTIVATING NEUROPEPTIDES - FUNCTIONS AND CHEMISTRY, Peptides, 17(2), 1996, pp. 337-344
Citations number
69
Categorie Soggetti
Biology
Journal title
ISSN journal
01969781
Volume
17
Issue
2
Year of publication
1996
Pages
337 - 344
Database
ISI
SICI code
0196-9781(1996)17:2<337:PBAN-F>2.0.ZU;2-5
Abstract
Sex pheromones are critical for reproductive success in most species o f Lepidoptera and their production is regulated by the action of phero mone biosynthesis activating neuropeptides (PBAN). These peptides, com posed of 33-34 amino acids, have approximately 80% sequence homology a nd share the C-terminal sequence FSPRL-NH2, which has been shown to be the minimum sequence required for pheromonotropic activity. This pent amer is structurally similar to the active core (FXPRL-NH2, X = V, T, or G) of the insect myotropic pyrokinins. Structure-activity studies h ave shown that all of the pyrokinins have various degrees of pheromono tropic activity and that some have a superagonistic effect. Peptides t hat only have sequence homology with PBAN in the C-terminal pentapepti de region, but that are pheromonotropic, also have been identified fro m moths. These findings suggest that induction of pheromone biosynthes is may be regulated by more than one peptide, that PBAN may have a num ber of physiological functions, and that these peptides regulate induc tion of pheromone production in a variety of ways.