Immunocytochemical distribution of angiotensin I-converting enzyme-like immunoreactivity in the brain and testis of insects

Schoofs, Liliane; Veelaert, Dirk; Loof, Arnold De; Huybrechts, Roger; Isaac, Elwyn

doi:10.1016/s0006-8993(97)01398-x

Cited by 51 publications

(32 citation statements)

References 46 publications

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“…ACE have been described as nonspecific dipeptydyl carboxypeptidases [28] and have been characterised in a number of insects, including Bombyx mori, D. melanogaster, L. migratoria, Musca domestica, and S. littoralis [29][30][31][32][33]. In insects, ACE are thought to be involved in regulating peptide hormones and neuropeptides by removing dipeptides, dipeptideamides and tripeptideamides from the C terminus of short peptides ( [31,32,34,35], reviewed in [36]). The matched protein identified here from pea aphid saliva is homologous to Drosophila ACE (Ance; AAF53353).…”

Section: Discussionmentioning

confidence: 99%

The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry

et al. 2009

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Nine proteins secreted in the saliva of the pea aphid Acyrthosiphon pisum were identified by a proteomics approach using GE-LC-MS/MS and LC-MS/MS, with reference to EST and genomic sequence data for A. pisum. Four proteins were identified by their sequences: a homolog of angiotensin-converting enzyme (an M2 metalloprotease), an M1 zinc-dependant metalloprotease, a glucose-methanol-choline (GMC)-oxidoreductase and a homolog to regucalcin (also known as senescence marker protein 30). The other five proteins are not homologous to any previously described sequence and included an abundant salivary protein (represented by ACYPI009881), with a predicted length of 1161 amino acids and high serine, tyrosine and cysteine content. A. pisum feeds on plant phloem sap and the metalloproteases and regucalcin (a putative calcium-binding protein) are predicted determinants of sustained feeding, by inactivation of plant protein defences and inhibition of calcium-mediated occlusion of phloem sieve elements, respectively. The amino acid composition of ACYPI009881 suggests a role in the aphid salivary sheath that protects the aphid mouthparts from plant defences, and the oxidoreductase may promote gelling of the sheath protein or mediate oxidative detoxification of plant allelochemicals. Further salivary proteins are expected to be identified as more sensitive MS technologies are developed.

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Section: Discussionmentioning

confidence: 99%

The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry

et al. 2009

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“…Recently in several insects, a peptidyl dipeptidase that has very similar enzymatic properties to mammalian ACE has been found (Lamango and Isaac, 1994;Cornell et al, 1995;Wijffels et al, 1996;Schoofs et al, 1998). Two genes that code for ACE homologues, AnCE and Acer, were identified in Drosophila melanogaster.…”

Section: Introductionmentioning

confidence: 99%

The angiotensin converting enzyme inhibitor captopril reduces oviposition and ecdysteroid levels in Lepidoptera

Vercruysse

Gelman

Raes

et al. 2004

Arch Insect Biochem Physiol

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The role of angiotensin converting enzyme (ACE, peptidyl dipeptidase A) in metamorphic- and reproductive-related events in the Egyptian cotton leafworm, Spodoptera littoralis (Lepidoptera, Noctuidae) was studied by using the selective ACE inhibitor captopril. Although oral administration of captopril had no effect on larval growth, topical administration to new pupae resulted in a large decrease of successful adult formation. Oviposition and overall appearance of adults emerging from treated larvae did not differ significantly from those emerging from non-treated larvae. In contrast, topical or oral administration of captopril to newly emerged adults caused a reduction in oviposition. By evaluating the effect of captopril on ecdysteroid titers and trypsin activity, we revealed an additional physiological role for ACE. Captopril exerted an inhibitory effect on ecdysteroid levels in female but not in male adults. Larvae fed a diet containing captopril exhibited increased trypsin activity. A similar captopril-induced increase in trypsin activity was observed in female adults. In male adults, however, captopril elicited reduced levels of trypsin activity. Our results suggest that captopril downregulates oviposition by two independent pathways, one through ecdysteroid biosynthesis regulation, and the other through regulation of trypsin activity. Apparently, fecundity is influenced by a complex interaction of ACE, trypsin activity, and ecdysteroid levels.

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“…Comparative studies showed that in several insect species, in particular in Diptera, ACE activ-ity is present and gene sequences encoding the active domain of the enzyme are highly conserved (Lamango and Isaac, 1994;Cornell et al, 1995;Wijffels et al, 1996;Schoofs et al, 1998). Enzymes of either origin are capable of hydrolysing identical substrates in vitro (Isaac et al, , 2000.…”

Section: Introductionmentioning

confidence: 99%

Captopril, a specific inhibitor of angiotensin converting enzyme, enhances both trypsin and vitellogenin titers in the grey fleshflyNeobellieria bullata

Vandingenen

Hens

Macours

et al. 2001

Arch Insect Biochem Physiol

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A strong and constitutive angiotensin converting enzyme- or ACE-like activity was demonstrated in the hemolymph of the adult grey fleshfly Neobellieria bullata. In a competition assay, the N. bullata trypsin modulating oostatic factor (Neb-TMOF) was confirmed to be an in vitro substrate for this circulating Neb-ACE. Oral uptake of captopril, a selective and specific inhibitor of ACE, resulted in a complete phenotypic knockout of circulating ACE activity. When compared with control animals, captopril-fed female flies showed an increase in the liver meal-induced trypsin peak in the midgut and elevated levels of protein meal-induced yolk polypeptides in the hemolymph. The latter effect was not due to a slower vitellogenin uptake by the ovaries, because oocyte growth was not affected by the captopril treatment. The apparent synergism between the demonstrated ACE functionality and the previously reported effects of the oostatic peptide Neb-TMOF are discussed in the context of our recent finding that Neb-TMOF represents a prime candidate for being the first known in vivo substrate for circulating insect ACE. Arch.

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Immunocytochemical distribution of angiotensin I-converting enzyme-like immunoreactivity in the brain and testis of insects

Cited by 51 publications

References 46 publications

The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry

The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry

The angiotensin converting enzyme inhibitor captopril reduces oviposition and ecdysteroid levels in Lepidoptera

Captopril, a specific inhibitor of angiotensin converting enzyme, enhances both trypsin and vitellogenin titers in the grey fleshflyNeobellieria bullata

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