Four neuropeptides that inhibit juvenile hormone synthesis by the corpora allata have been isolated from brains of the virgin female cockroach Diploptera punctata. These allatostatins are 8-13 amino acids long, are amidated, and show sequence similarity, including a 3-amino acid sequence at the C-terminal end that is common to all four peptides. The peptide sequences are as follows: allatostatin 1, Ala-Pro-Ser-Gly-Ala-Gln-Arg-Leu-Tyr-Gly-Phe-Gly-Leu-

Allatostatins are pleiotropic neuropeptides for which one function in insects is the inhibition of juvenile hormone synthesis. Juvenile hormone, an important regulator of development and reproduction in insects, is produced by the corpora allata. Mandibular organs, the crustacean homologs of insect corpora allata, produce precursors of juvenile hormone with putatively similar functions. Three types of allatostatins in insects have been isolated: FGLamides, W(X)(6)Wamides, and PISCFs. All act rapidly and reversibly; however, although these types occur in all groups of insects studied, they act as inhibitors of juvenile hormone production in only some groups. Only the FGLamide-type peptides have been isolated in crustaceans, in which they may function to stimulate production of hormone by the mandibular glands, as occurs in early cockroach embryos. Much remains to be learned in order to understand the role of allatostatins in the modulation of hormone production.

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The high degree of conservation of the core sequence of the "cockroach-types" of AST and their widespread distribution suggest that they should be considered a ubiquitous family of peptides within the invertebrates, regulating a range of important physiological processes. These functional processes, by either neural or humoral routes of action, include the inhibition of endocrine function, interneuronal functions, neuromodulatory roles, myotropic and myoendocrine roles, and direct action on biosynthetic pathways. The myomodulatory function appears to be conserved through evolutionary time, whereas the JH inhibitory activity appears to be confined to specific orders. This suggests that the myomodulatory role was the more ancestral of these two particular functions. Certainly, further purification and gene cloning as a means to precursor identification and functional analysis will be a prerequisite to understanding the diverse functions of this peptide family.

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