J. Michalik et al., HYPERTREHALOSEMIC INSECT PEPTIDE PERIPLANETIN CC-2 AND ITS ANALOGS - SYNTHESIS AND BIOLOGICAL EVALUATION, European journal of entomology, 95(1), 1998, pp. 1-7
The effects of hypertrehalosaemic octapeptides (peptides from AKH fami
ly) on transcription and trehalosegenesis in the fat body of adult fem
ales of Tenebrio molitor L. were examined. A synthetic hypertrehalosae
mic peptide from CC of Periplaneta americana periplanetin CC-2 (Pea-CA
H-II) Glp-Leu-Thr-Phe-Thr-Pro-Asn-Trp-amide (1), its new synthetic ana
logues Glp-Leu-Thr-Phe-Thr-Pro-Asn-Phe-amide (2), Glp-Leu-Thr-Phe-Thr-
Pro-Asn-D-Trp-amide (3), Glp-Leu-Thr-Phe-Thr-Pro-Asn-D-Phe-amide (4),
and an octapeptide from T. molitor Glp-Leu-Asn-Phe-Ser-Pro-Asn-Trp-ami
de (Tem-HrTH) (5) were tested. Peptides 2, 3 and 5 suppress transcript
ion in the fat body tissue measured as incorporation of [H-3]-uridine
into total RNA. The rate of RNA inhibition in the tissue depends on th
e peptide concentration. Periplanetin CC-2 (2) was inactive in this te
st. Endogenic T. molitor octapeptide (5) stimulates trehalose release
from the fat body of females, whereas Pea-CAH-II analogues (2-4) do no
t increase trehalose release from this tissue.