More than 60 neuropeptides that inhibit juvenile hormone synthesis by the corpora allata have been isolated from the brains of various insect species. Most of them are characterized by a common C-terminal pentapeptide sequence Y/FXFGL/I/V (allatostatin A family, allatostatin superfamily). Besides the allatostatin A family, allatostatic neuropeptides belonging to other two peptide families (W2W9)-allatostatins or allatostatin B family; lepidopteran allatostatin) were reported. So far, only one allatotropin has been identified. Here we discuss latest literature on the multiplicity and multifunctionality of the allatoregulating neuropeptides, their physiological significance as well as their evolutionary conservation in structure and function., Klaus H. Hoffmann, Martina Meyering-Vos, Matthias W. Lorenz, and Lit
Four peptides with allatostatic activity were isolated from brains of the Mediterranean field cricket, Gryllus bimaculatus. Three of them (Grb-AST A3: AGMYSFGL-NH2; Grb-AST A4: SRPFGFGL-NH2; Grb-AST A5: GPDHRFAFGL-NH2) belong to the wide-spread family of Y/FXFGL/I-amide peptides, the fourth (Grb-AST B5: AWDQLRPGW-NH2) is a member of the W2W9 - amide family of neuropeptides. All of these peptides are potent inhibitors of juvenile hormone (JH) biosynthesis by cricket corpora allata in vitro, causing 50% inhibition of JH biosynthesis at 0.4-3 × 10-8 M. The two peptides Grb-AST A5 and Grb-AST B5 have virtually the same potency and efficacy in inhibiting JH biosynthesis in vitro. No synergistic effect of the two peptide families with respect to the inhibition of JH biosynthesis could be observed. Peptides of both families decrease the accumulation of methylfarnesoate, the direct precursor of JH, within CA that have been incubated in farnesol-rich medium. This suggests an involvement of these ASTs in the late steps of JH biosynthesis., Mathias W., Roland Kellner, Klaus H. Hoffmann, and Lit