Sulfakinins (SKs) are neuropeptides structurally and functionally analogous to vertebrate gastrin/cholecystokinins. They regulate feeding behavior, energy metabolism, and digestive processes in insects through G-protein-coupled receptors (GPCRs) . These peptides are characterized by a conserved C-terminal motif (DY(SO3)GHM/LRFamide), with the sulfated tyrosine residue critical for receptor binding and activity .
While no studies explicitly describe recombinant Lucihormetica verrucosa Sulfakinin-1 (LvSK-1), research on sulfakinins in related insects provides a framework for understanding its potential structure and function.
Sulfakinins across insect species share conserved roles in satiety signaling and metabolic regulation. For example:
SK in *Dendroctonus armandi*:
SK in *Bombyx mori*:
L. verrucosa (warty glowspot cockroach) is noted for its sexual dimorphism and carotenoid-dependent pronotal spots . While no studies directly address its sulfakinin system, extrapolation from related species suggests:
Structural Predictions:
Likely retains the DY(SO3)GHMRFamide motif.
Sulfation at tyrosine is critical for receptor interaction.
Functional Hypotheses:
Potential roles in appetite suppression, energy homeostasis, or stress responses.
May interact with GPCRs analogous to BNGR-A9 or DaSKR.
Recombinant SK production typically involves:
Gene Cloning: Amplify SK precursor cDNA from target species.
Peptide Synthesis: Use E. coli or yeast systems for expression, followed by sulfation via tyrosylprotein sulfotransferases .
Functional Assays:
Receptor activation tests (e.g., IP3/Ca²⁺ flux in HEK293 cells).
In vivo feeding assays (e.g., body weight tracking post-injection).
Unresolved Questions:
Sequence and receptor specificity of LvSK-1.
Sulfation efficiency in recombinant systems.
Potential Applications:
Pest control via appetite suppression.
Metabolic studies in cockroach models.