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Different neuroparsin variants were initially identified as anti-gonadotropic peptides from the pars intercerebralis-corpora cardiaca complex of the migratory locust, Locusta migratoria, and further studies revealed the pleiotropic activities of these peptides. Subsequently, additional neuroparsin-like peptides were discovered from other arthropod species. Studies in mosquitoes and locusts suggest that members of this conserved peptide family are involved in the regulation of insect reproduction and can even serve as molecular markers of the fascinating biological process of locust phase transition. Sequence analysis and multiple alignments revealed pronounced sequence similarities between arthropod neuroparsins and the N-terminal, growth factor binding region of vertebrate and mollusc insulin-like growth factor binding proteins (IGFBP). This observation led to the hypothesis that neuroparsins might interact with endogenous insulin-related peptides. The present paper gives an overview of several neuroparsin family members that have hitherto been described in insects, as well as of a number of newly identified neuroparsin precursors from other species.

Peptides form a very versatile class of extracellular messenger molecules that function as chemical communication signals between the cells of an organism. Molecular diversity is created at different levels of the peptide synthesis scheme. Peptide messengers exert their biological functions via specific signal-transducing membrane receptors. The evolutionary origin of several peptide precursor and receptor gene families precedes the divergence of the important animal Phyla. In this chapter, current knowledge is reviewed with respect to the analysis of peptide receptors from insects, incorporating many recent data that result from the sequencing of different insect genomes. Therefore, detailed information is provided on six different peptide receptor families belonging to two distinct receptor categories (i.e., the heptahelical and the single transmembrane receptors). In addition, the remaining problems, the emerging concepts, and the future prospects in this area of research are discussed.

The last decade, a new serine protease inhibitor family has been described in arthropods. Eight members were purified from the locusts Locusta migratoria (LMPI-1-2 and HI) and Schistocerca gregaria (SGPI-1-5) and 11 additional locust peptides were identified by cDNA cloning. Furthermore, the light chain of the 155-kDa heterodimeric protease inhibitor pacifastin, from the freshwater crayfish Pacifastacus leniusculus, was found to be composed of nine consecutive inhibitory domains (PLDs). These domains share a pattern of 6 conserved cysteine residues (Cys-Xaa(9-12)-Cys-Asn-Xaa-Cys-Xaa-Cys-Xaa(2-3)-Gly-Xaa(3-4)-Cys-Thr-Xaa3-Cys) with the locust inhibitors. So far, for most of the PLD-related peptides the biological functions remain obscure. To obtain sufficient amounts of material to perform physiological experiments, we have optimised the production of SGPI-1-2 via a bacterial (Escherichia coli) expression system. The cDNA sequences encoding these peptides were inserted in the pMAL-2pX vector, downstream of the gene encoding the maltose-binding protein (including a signal peptide). As a consequence, both peptides were expressed as fusion proteins (2-3 mg/l) and targeted to the periplasmic space. Following a one-step affinity purification, both fusion proteins were successfully cleaved by Factor Xa and after a methanol extraction, it took only one additional RP-HPLC run to purify both peptides to homogeneity. Finally, the formation of the disulphide bridges and the biological activity of the recombinant peptides were verified by mass spectrometry and a spectrophotometric protease inhibitor assay, respectively.