Isolation of angiotensin converting enzyme from testes of Locusta migratoria (Orthoptera)

Macours, Nathalie; Vandingenen, Anick; Gielens, Constant; Hens, Korneel; Baggerman, Geert; Schoofs, Liliane; Huybrechts, Roger

doi:10.14411/eje.2003.070

Cited by 9 publications

(5 citation statements)

References 36 publications

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“…Purification and cloning of several insect ACE homologues indicate that the general structure of the insect enzyme is similar to the single domain, testicular form of vertebrate ACE ( Fig. 1) (Lamango et al, 1996;Wijffels et al, 1996;Ekbote et al, 1999;Quan et al, 2001;Macours et al, 2003a). To date, a functional two-domain form of insect ACE, as is seen in the somatic form of ACE in vertebrates (sACE), has not yet been reported.…”

Section: Angiotensin-converting Enzymementioning

confidence: 99%

Zinc-metalloproteases in insects: ACE and ECE

Macours

Hens

2004

Insect Biochemistry and Molecular Biology

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Section: Angiotensin-converting Enzymementioning

confidence: 99%

Zinc-metalloproteases in insects: ACE and ECE

Macours

Hens

2004

Insect Biochemistry and Molecular Biology

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“…It activates angiotensin I by converting it into the vasoconstrictive peptide angiotensin II and deactivates the vasodilator, bradykinin I, resulting in an increase in blood pressure (Erdö s and Skidgel, 1987). The prevalence of insect ACE in hemo-lymph (Macours et al, 2003;Ekbote et al, 2003, Lemeire et al, 2008, together with its broad in vitro substrate specificity suggests a role in the processing of neuropeptides and peptide hormones (Isaac et al, 2000). The first described insect ACE from the housefly Musca domestica hydrolyzes several C-terminally amidated neuropeptides like leucokinin I and II, locustatachykinin I and II, allatostatin I, SchistoFLRFamide, and Culex depolarizing peptides I and II (Lamango et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Effect of ace inhibitors and TMOF on growth, development, and trypsin activity of larval Spodoptera littoralis

Lemeire

Borovsky

Camp

et al. 2008

Arch Insect Biochem Physiol

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Angiotensin converting enzyme (ACE) is a zinc metallopeptidase capable of cleaving dipeptide or dipeptideamide moieties at the C-terminal end of peptides. ACE is present in the hemolymph and reproductive tissues of insects. The presence of ACE in the hemolymph and its broad substrate specificity suggests an important role in processing of bioactive peptides. This study reports the effects of ACE inhibitors on larval growth in the cotton leafworm Spodoptera littoralis. Feeding ACE inhibitors ad lib decreased the growth rate, inhibited ACE activity in the larval hemolymph, and down-regulated trypsin activity in the larval gut. These results indicate that S. littoralis ACE may influence trypsin biosynthesis in the larval gut by interacting with a trypsin-modulating oostatic factor (TMOF). Injecting third instar larvae with a combination of Aea-TMOF and the ACE inhibitor captopril, down-regulated trypsin biosynthesis in the larval gut indicating that an Aea-TMOF gut receptor analogue could be present. Injecting captopril and enalapril into newly molted fifth instar larvae stopped larval feeding and decreased weight gain. Together, these results indicate that ACE inhibitors are efficacious in stunting larval growth and ACE plays an important role in larval growth and development.

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“…This peptidyl dipeptidase is strongly expressed as a glycosylated protein of 72 kDa in several tissues, including male reproductive tissues, the larval and adult midgut, larval trachea and adult salivary gland2627. Other insect species also express ACE in reproductive tissues of both sexes, suggesting a broader physiological role for the enzyme in insect reproduction19282930313233343536. Insect ACE not only resembles the mammalian enzyme in its substrate specificity, but also in susceptibility to inhibitors such as captopril, lisinopril, fosinoprilat, enalapril and trandolaprilat, but apart from captopril these inhibitors can be far less potent towards insect ACE compared to mammalian ACE2223.…”

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The toxicity of angiotensin converting enzyme inhibitors to larvae of the disease vectors Aedes aegypti and Anopheles gambiae

Hasan

Williams

Ismail

et al. 2017

Sci Rep

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The control of mosquitoes is threatened by the appearance of insecticide resistance and therefore new control chemicals are urgently required. Here we show that inhibitors of mosquito peptidyl dipeptidase, a peptidase related to mammalian angiotensin-converting enzyme (ACE), are insecticidal to larvae of the mosquitoes, Aedes aegypti and Anopheles gambiae. ACE inhibitors (captopril, fosinopril and fosinoprilat) and two peptides (trypsin-modulating oostatic factor/TMOF and a bradykinin-potentiating peptide, BPP-12b) were all inhibitors of the larval ACE activity of both mosquitoes. Two inhibitors, captopril and fosinopril (a pro-drug ester of fosinoprilat), were tested for larvicidal activity. Within 24 h captopril had killed >90% of the early instars of both species with 3rd instars showing greater resistance. Mortality was also high within 24 h of exposure of 1st, 2nd and 3rd instars of An. gambiae to fosinopril. Fosinopril was also toxic to Ae. aegypti larvae, although the 1st instars appeared to be less susceptible to this pro-drug even after 72 h exposure. Homology models of the larval An. gambiae ACE proteins (AnoACE2 and AnoACE3) reveal structural differences compared to human ACE, suggesting that structure-based drug design offers a fruitful approach to the development of selective inhibitors of mosquito ACE enzymes as novel larvicides.

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Isolation of angiotensin converting enzyme from testes of Locusta migratoria (Orthoptera)

Cited by 9 publications

References 36 publications

Zinc-metalloproteases in insects: ACE and ECE

Zinc-metalloproteases in insects: ACE and ECE

Effect of ace inhibitors and TMOF on growth, development, and trypsin activity of larval Spodoptera littoralis

The toxicity of angiotensin converting enzyme inhibitors to larvae of the disease vectors Aedes aegypti and Anopheles gambiae

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