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E Isaac

Publications and source records attributed to E Isaac.

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

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.

Animals

Angiotensin II and angiotensin-converting enzyme as candidate compounds modulating the effects of testis ecdysiotropin in testes of the gypsy moth, Lymantria dispar1.

Lymantria dispar testes synthesize immunodetectable ecdysteroid in vitro in response to the brain peptide, testis ecdysiotropin (TE), acting primarily via a cascade involving Gi protein, diacyl glycerol, and phosphokinase C. However, a component of TE activation also involves the opposite cascade, Gs protein, cAMP, and phosphokinase A. Excess cAMP inhibits the action of TE, acting as a feedback modulator. Here, we show that bovine angiotensin II (AII) and bovine angiotensin converting enzyme (ACE) act like cAMP, inducing synthesis of immunodetectable ecdysteroid by pupal testes in vitro, but are antagonistic to coincubated TE. In addition, an insect ACE antibody clearly stains the spermatogenic cells through all stages of development, as well as testis sheath tissue where ecdysteroid is synthesized. AII induces synthesis of cAMP by pupal testes in vitro. Therefore, insect homologs of mammalian AII and ACE are good candidates for the peptides responsible for the cAMP cascade and as modulators of TE action in lepidopteran testes. Saralasin, an analog of AII that blocks angiotensin receptors in mammals, behaved like AII in inducing ecdysteroid secretion with ecdysteroidogenic effects additive to either angiotensin or ACE. Therefore, the receptors for the insect form of angiotensin on lepidopteran testis cells are probably different from those in mammals. Saralasin also inhibited ecdysteroid synthesis when combined with TE, as did AII.

Angiotensin II

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Calcium Hydroxide