Activity and mechanism of action of insect oostatic peptides in flesh fly.
The relationship between structure and activity of insect oostatic decapeptide (Aed-TMOF) analogues in flesh fly was analyzed. The highest oostatic activity was exhibited by the pentapetide and tetrapeptide analogues, H-Tyr-Asp-Pro-Ala-Pro-OH and H-Tyr-Asp-Pro-Ala-OH, respectively. The tetrapeptide, either native or tritiated, was used to study its metabolism in the ovaries and hemolymph and to detect putative binding sites in the flesh fly ovaries and head. A high metabolism of the tetrapeptide with a half-life in the hemolymph and ovaries less than 1h was determined. The initial limiting step in the degradation is tyrosine(1) cleavage. Other degradation products were detected only transiently in low quantities. Using tritiated tetrapeptide, we found that only very low specific binding was detected in the homogenates of ovaries and in the rough membrane preparation in the presence and absence of protease inhibitors.
Slaninová
Jirina
J
Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo 2, 166 10 Prague 6, Czech Republic.
Bennettová
Blanka
B
Nazarov
Elsan S
ES
Simek
Petr
P
Holík
Josef
J
Vlasáková
Vera
V
Hlavácek
Jan
J
Cerný
Bohuslav
B
Tykva
Richard
R
D000818:Animals; D001665:Binding Sites; D001673:Biodegradation, Environmental; D004175:Diptera / Q000187:drug effects*; D005260:Female; D006257:Head; D006458:Hemolymph / Q000378:metabolism; D007313:Insecta; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism* / Q000493:pharmacokinetics; D010053:Ovary / Q000187:drug effects* / Q000378:metabolism; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000378:metabolism / Q000493:pharmacokinetics; D010599:Pharmacokinetics; D011480:Protease Inhibitors / Q000494:pharmacology
D009842:Oligopeptides; D010446:Peptide Fragments; D011480:Protease Inhibitors; C065612:Peptide oostatic hormone