HYPERTREHALOSEMIC INSECT PEPTIDE PERIPLANETIN CC-2 AND ITS ANALOGS - SYNTHESIS AND BIOLOGICAL EVALUATION

Citation
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
Citations number
21
Categorie Soggetti
Entomology
ISSN journal
12105759
Volume
95
Issue
1
Year of publication
1998
Pages
1 - 7
Database
ISI
SICI code
1210-5759(1998)95:1<1:HIPPCA>2.0.ZU;2-#
Abstract
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.