Insect peptidyl-dipeptidase A [angiotensin I - converting enzyme (ACE)] is a soluble single-domain peptidyl-dipeptidase that has many properties in common with the C-domain of mammalian somatic ACE and with the single-domain mammalian ACE. In agreement with a variety of insects, immunocytochemical studies reveal the presence of an ACE-like protein in Locusta migratoria. ACE-like immunoreactivity is present in neurosecretory cells of the pars intercerebralis. These cells have axons projecting into the nervus corporis cardiaci I and into the storage part of the corpus cardiacum, a neuroendocrine organ directly releasing into the aorta. The localisation of ACE in neurosecretory cells is consistent with its proposed role as a processing enzyme that is involved in the generation of active peptide hormones., Dirk Veelaert, Liliane Scoofs, Nathalie Macours, Anick Vandingenen, Arnold De Loof, Elwyn Isaac, Michel Salzet, Roger Huybrechts, and Lit
An inbred strain of a newly isolated spontaneous albino mutant of Schistocerca gregaria (Forsk.) was examined for the presence of the neuropeptide [His7]-corazonin by immunocytochemical and mass spectrometric methods. It was concluded that this peptide is definitely present in a limited number of neurosecretory cells in the pars lateralis as well as in the corpora cardiaca (CC). Injection of either synthetic [His7]-corazonin or of extracts of CC of the normal coloured phenotype of S. gregaria failed to induce darkening of the cuticle, while albino Locusta migratoria, used as a positive control, turned dark. The conclusion is that the cause of albinism in the new S. gregaria albino is probably due to a defect in the receptor system for [His7]-corazonin or in the biosynthetic pathway of melanin.