leucosulfakinin and leucomyosuppressin

The insect neuropeptides FMRF amide, leucomyosupressin (LMS) and neuropeptide analogues leucosulfakinins (FLSK and LSK II Ser (SO(3)H)), perisulfakinin (PSK), proleucosulfakinin (PLSK), 14A[phi1]WP-I, 542phi1, and 378A[5b]WP-I were assayed for their effects on the release of amylase and protease from the midgut tissue of larvae of Opisina arenosella. In the bioassay, empty midgut tubes ligated at both ends using hair were incubated with insect saline containing neuropeptides/analogues in a bioassay apparatus at 37 degrees C for 30 min. After incubation the contents of the midgut preparations were analyzed for amylase and protease activity. In control experiments, the midgut preparations were incubated in insect saline without neuropeptides. The results of the study reveal that for stimulating amylase release from midgut tissue, the peptides require an FXRF amide (X may be methionine or leucine) sequence at the C-terminal. The presence of HMRF amide at C-terminal of peptides may inhibit the release of amylase. Meanwhile, peptides with both FMRF and HMRF amide sequence at the C-terminal are found to be effective in stimulating protease release. The tetrapeptide segment at the C-terminal probably represent the active core of the neuropeptide.

Topics: Amino Acid Sequence; Amylases; Animals; Digestive System; Endopeptidases; FMRFamide; In Vitro Techniques; Insect Hormones; Larva; Lepidoptera; Leucine; Methionine; Molecular Sequence Data; Neuropeptides

Topics: Amino Acid Sequence; Animals; Cockroaches; In Vitro Techniques; Insect Hormones; Molecular Sequence Data; Muscle Contraction; Neuropeptides; Oligopeptides; Pyrrolidonecarboxylic Acid; Structure-Activity Relationship; Tuftsin