Hydrolysis of Insect Neuropeptides by an Angiotensin-Converting Enzyme From the Housefly, Musca domestica
1997; Elsevier BV; Volume: 18; Issue: 1 Linguagem: Inglês
10.1016/s0196-9781(96)00232-x
ISSN1873-5169
AutoresNazarius S. Lamango, Ronald J. Nachman, Timothy K. Hayes, Allison Strey, R. Elwyn Isaac,
Tópico(s)Neurobiology and Insect Physiology Research
ResumoLamango, N. S., R. J. Nachman, T. K. Hayes, A. Strey and R. E. Isaac. Hydrolysis of insect neuropeptides by an angiotensin-converting enzyme from the housefly, Musca domestica. Peptides 18(1) 47–52, 1997.—The presence in insect tissues of peptides with structural similarities to angiotensin I and to bradykinin, the two best known substrates of mammalian angiotensin-converting enzyme, has not been reported. As part of our study to identify potential substrates for insect angiotensin-converting enzyme, we have investigated the susceptibility of a number of known insect peptide hormones and neurotransmitters to hydrolysis by Musca domestica angiotensin-converting enzyme. Insect peptides belonging to the red pigment-concentrating hormone, leucokinin, locust tachykinin, and depolarizing peptide families were hydrolyzed by housefly angiotensin-converting enzyme, whereas proctolin and crustacean cardioactive peptide were not substrates. Cus-DP II, LK I, LK II, and Lom-TK I were all cleaved at the penultimate C-terminal peptide bond to release a dipeptide amide as a major fragment with Km values of 94 ± 11, 634 ± 81, and 296 ± 35 μM for Cus-DP II, LK I, and Lom-TK I, respectively. The ability of insect angiotensin-converting enzyme to hydrolyze C-terminally amidated peptides in vitro might be of functional significance because the enzyme has been localized to neuropile regions of the insect brain and is present in the hemolymph of houseflies.
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