title: Immunocytochemical distribution of angiotensin I-converting enzyme-like immunoreactivity in the brain and testis of insects.
abstract: Angiotensin converting enzyme (ACE) is Zn2+ metallopeptidase which plays an important role in blood pressure homeostasis in mammals and other vertebrates. Homologues of ACE involved in the biosynthesis of mammalian peptide hormones have also been identified in the insects, Musca domestica, Drosophila melanogaster and Haematobia irritans exigua. In the pursuit of the biological role of insect ACE, this work focused on the tissue and cellular distribution of ACE in several insect species. The localisation of ACE in the central nervous system and reproductive tissues from a number of insect species suggests that ACE is of physiological importance in these tissues. By means of an antiserum to housefly ACE, we found that ACE-like immunoreactivity was abundantly present in the neuropil areas of the brain of all insects investigated, suggesting a role for ACE in the metabolic inactivation of peptide neurotransmitters. Especially in the fleshfly, Neobellieria bullata neuropile staining is abundant. In the cockroach Leucophaea maderae, immunoreactive staining was abundant in the neuronal perikarya as well as in the neuropilar regions. Staining in neurosecretory cells was also observed in the brains of the lepidopteran species, Bombyx mori and Mamestra brassica. The localisation of ACE in neurosecretory cells is consistent with the role as a processing hormone, involved in the generation of active peptide hormones. ACE was found to be co-localised with peptides of the FXPRLamide family in M. brassica and in B. mori, suggesting a role for the biosynthesis of these hormones. Finally, we found ACE-like immunoreactivity in the testis of Locusta migratoria, N. bullata and Leptinotarsa decemlineata, providing additional evidence for its important role in insect reproduction.
authors.affiliation: Zoological Institute, Katholieke Universiteit Leuven, Naamsestraat 59, B-3000 Leuven, Belgium. liliane.schoofs@bio.kuleuven.ac.be
authors.forename: L
authors.initials: L
authors.lastname: Schoofs
authors.forename: D
authors.initials: D
authors.lastname: Veelaert
authors.forename: A
authors.initials: A
authors.lastname: De Loof
authors.forename: R
authors.initials: R
authors.lastname: Huybrechts
authors.forename: E
authors.initials: E
authors.lastname: Isaac
mesh_terms: D000818:Animals; D001921:Brain / Q000166:cytology / Q000201:enzymology; D004331:Drosophila melanogaster / Q000201:enzymology; D006110:Grasshoppers / Q000201:enzymology; D006793:Houseflies / Q000201:enzymology; D007150:Immunohistochemistry; D007313:Insecta / Q000201:enzymology*; D007915:Lepidoptera / Q000201:enzymology; D008297:Male; D007703:Peptidyl-Dipeptidase A / Q000032:analysis*; D013737:Testis / Q000166:cytology / Q000201:enzymology
chemical_list: D007703:Peptidyl-Dipeptidase A