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.