Publication
Title
In vitro degradation of the Neb-Trypsin Modulating Oostatic Factor (Neb-TMOF) in gut luminal content and hemolymph of the grey fleshfly, **Neobellieria bullata**
Author
Abstract
The unblocked hexapeptidic Trypsin Modulating Oostatic Factor of the fleshfly, an inhibitor of both trypsin and ecdysone biosynthesis, resists very well proteolytic breakdown by enzymes present in the lumen of the gut of previtellogenic fleshflies. However, when incubated in hemolymph of adult flies, females and males, its half-life time is a mere 0.5 min. In hemolymph of last instar larvae, this value increases to about 1.5 min. Whereas PMSF, a potent inhibitor of serine proteases has no effect, captopril and lisinopril, both known to be specific inhibitors of mammalian angiotensin I converting enzyme (ACE), effectively inhibit TMOF breakdown in fly hemolymph. Digestion of Neb-TMOF by recombinant Drosophila AnCE on itself results in identical degradation products as with total hemolymph. In both cases ESI-Qq-oa-Tof mass spectrometry demonstrated the appearance of peptide fragments with the sequences HPTN, LH and NP. These observations not only confirm the reported presence of circulating ACE-like activity in flies but also strongly suggest that in flies this hemolymph ACE-like activity might be involved in the regulation of the oostatic activity as exerted by Neb-TMOF. (C) 2001 Elsevier Science Ltd. All rights reserved.
Language
English
Source (journal)
Insect biochemistry and molecular biology. - Bristol
Publication
Bristol : 2001
ISSN
0965-1748
Volume/pages
31:1(2001), p. 87-95
ISI
000166418400010
Full text (Publisher's DOI)
Full text (publisher's version - intranet only)
UAntwerpen
Faculty/Department
Publication type
Subject
External links
Web of Science
Record
Identification
Creation 25.03.2015
Last edited 07.10.2017