Isolation and characterization of an angiotensin converting enzyme substrate from vitellogenic ovaries of Neobellieria bullata

Vandingenen, Anick; Hens, Korneel; Baggerman, Geert; Macours, Nathalie; Schoofs, Liliane; Loof, Arnold De; Huybrechts, Roger

doi:10.1016/s0196-9781(02)00144-4

Cited by 12 publications

(18 citation statements)

References 46 publications

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“…In contrast to these results are the reports of Vandingenen et al (2001Vandingenen et al ( , 2002 and Hens et al (2002) concerning the interaction between ACE, ACE-inhibitors, and trypsin modulating oostatic factor (TMOF). TMOF was first identified in the mosquito Aedes aegypti and named Aea-TMOF (Borovsky et al, 1990).…”

Section: Discussionmentioning

confidence: 66%

“…Females that had been mated with these ACE-inhibited males showed a dramatic reduction in fecundity (Ekbote et al, 2003a). In addition, Vandingenen et al (2001Vandingenen et al ( , 2002 treated female adults of the grey fleshfly Neobellieria bullata with captopril and studied the in vivo relationship between Neb-TMOF (trypsin modulating oostatic factor) and Neb-ACE. Since Neb-TMOF is an in vivo substrate for Neb-ACE, the captopril treatment had a direct effect on trypsin activity and vitellogenin concentrations.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 66%

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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“…Insect ACE, like the mammalian enzyme, is a promiscuous peptidase that cleaves dipeptides from the carboxyl end of oligopeptides and, in some instances, can cleave amidated di- or tri-peptides from substrates with an amidated carboxyl terminus, a common feature of insect neuropeptides161718192021. Insect ACEs are generally soluble enzymes secreted from cells into the extracellular milieu, where like their mammalian counterparts they degrade peptides by sequential removal of dipeptides16222324.…”

mentioning

confidence: 99%

“…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.…”

mentioning

confidence: 99%

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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“…For example, angiotensin-converting enzyme (ACE) activity in invertebrates has been suggested to inactivate neuropeptides (Lamango and Issac, 1994;Laurent and Salzet, 1996a,b;Lamango et al, 1996). Moreover, the wide distribution of ACE activity, including central nervous tissues, reproductive tissues, hemocytes, and hemolymph, may further implicate ACE in a putative role in other physiological actions such as metamorphosis, reproduction, and immunity in corresponding tissues (Vandenbroeke et al, 1997;Hens et al, 2002;Vandingenen et al, 2002;Ekbote et al, 2003;Salzet and Verger-Bocquet, 2001;Macours et al, 2003;Laurent et al, 1997;Leung et al, 1992). In crustaceans, angiotensin-converting enzyme-like activity (ACELA) was initially reported in the gills of the blue crab, Callinectes sapidus (Smiley and Doig, 1994) and in the terrestrial crab, Chasmagnathus granulatus (Delorenzi et al, 1996).…”

Section: Archives Of Insect Biochemistry and Physiology July 2008mentioning

confidence: 99%

Angiotensin‐converting enzyme‐like activity in crab gills and its putative role in degradation of crustacean hyperglycemic hormone

Chung

Webster

2008

Arch Insect Biochem Physiol

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Angiotensin-converting enzyme-like enzyme activity (ACELA) was found in Carcinus maenas using reverse phase high performance liquid chromatography (RP-HPLC) analysis of degradation kinetics of a synthetic substrate (Hippuryl-histidyl-leucine) and a specific inhibitor (captopril). Gills contained the highest ACELA, then brain, muscle, and testis, respectively, while no activity was detected in the following tissues: hepatopancreas, hindgut, hypodermis, heart, and hemolymph. ACELA present in gill membranes exhibited a K(m) of 0.23 mM and V(max) of 7.6 nmol with synthetic substrate. The enzyme activity was dependent on Cl- concentration and was markedly inhibited by captopril, lisinopril, and EDTA. Addition of Zn2+ to membranes previously treated with EDTA restored 89% activity, suggesting that C. maenas ACELA is a Zn2+ metalloenzyme. Gill membranes prepared from premolt crabs showed similar levels of ACELA to those of the intermolt animals. Administration of captopril in vivo lengthened the half life of circulating CHH, while in vitro incubation of gill membranes with captopril reduced CHH. These results suggest that C. maenas ACELA present in gills is likely to be involved in degradation of this neuropeptide.

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Isolation and characterization of an angiotensin converting enzyme substrate from vitellogenic ovaries of Neobellieria bullata

Cited by 12 publications

References 46 publications

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

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

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

Angiotensin‐converting enzyme‐like activity in crab gills and its putative role in degradation of crustacean hyperglycemic hormone

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