Author:

Keywords:

neb-tmof, spodoptera frugiperda, schistocerca gregaria, leucophaea maderae, hemolymph, proteolytic breakdown, angiotensin converting enzyme, midgut, epithelial transport, angiotensin-converting enzyme, musca-domestica, absorption, biosynthesis, expression, analogs, extract, ovaries, growth, system, Science & Technology, Life Sciences & Biomedicine, Entomology, Physiology, Zoology, Neb-TMOF, Spodoptera frugiperda, Schistocerca gregaria, Leucophaea maderae, ANGIOTENSIN-CONVERTING ENZYME, MUSCA-DOMESTICA, ABSORPTION, BIOSYNTHESIS, EXPRESSION, ANALOGS, EXTRACT, OVARIES, GROWTH, SYSTEM, 0604 Genetics, 0606 Physiology, 0608 Zoology, 3109 Zoology, 3208 Medical physiology

Abstract:

The degradation of the unblocked hexapeptide, trypsin modulating oostatic factor of the flesh fly Neobellieria (Sarcophaga) bullata (Neb-TMOF) was studied in vitro in the hemolymph of the lepidopteran Spodoptera frugiperda, the orthopteran Schistocerca gregaria and the dictyopteran Leucophaea maderae. The half-life in the different species varied from similar to3 min in L. maderae to similar to 25 min in S. gregaria. Purification of the degradation products and ESI-Qq-oa-Tof mass spectrometry revealed the fragments Asn-Pro-Thr-Asn, Leu-His and Asn-Pro, which were the same in the hemolymph of all species. Except in Leucophaea, Neb-TMOF was cleaved in dipeptides starting from the C-terminus and the reaction could be, at least partially, inhibited by captopril. These observations suggest that a dipeptidase, which has very similar enzymatic properties as mammalian angiotensin converting enzyme (ACE) and which circulates in the hemolymph, apparently is involved in the breakdown of Neb-TMOF and might be a common but not a universal enzyme in insect hemolymph.