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Juvenile hormone metabolism in the plasma, integument, midgut, fat body, and brain during the last instar of the tobacco hornworm, Manduca sexta (L.)
Author(s) -
Jesudason Princy,
Anspaugh Douglas D.,
Roe R. Michael
Publication year - 1992
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940200202
Subject(s) - manduca sexta , biology , juvenile hormone , midgut , sphingidae , epoxide hydrolase , integument , esterase , endocrinology , medicine , biochemistry , hemolymph , enzyme , microsome , insect , hormone , anatomy , larva , ecology , botany
Juvenile hormone (JH) III esterase and JH III epoxide hydrolase activity was found in the integument, midgut, fat body, and brain during last instar development of the tobacco hornworm, Manduca sexta . JH esterase activity was primarily located in the cytosol in these tissues while the majority of the JH epoxide hydrolase activity was found in the microsomes. A prewandering (on day 3) and postwandering (on day 8) peak in plasma JH III esterase activity occurs in the last instar of gate I M. sexta . The JH esterase activity profile in integument, midgut, fat body, and brain followed a similar pattern to that of the plasma. The only exception to this was the absence of the postwandering, prepupal (on day 8) JH esterase peak in the fat body. The topical application of the juvenoid, (RS)‐methoprene, failed to induce fat body JH esterase activity but increased activity in the plasma, integument, midgut, and brain in M. sexta prepupae. These results indicate that the source of plasma JH esterase activity is not always the fat body as previously hypothesized. The developmental profile of tissue JH epoxide hydrolase activity was also similar to that of JH esterase suggesting that both enzymes may be regulated partly by the same factors and that JH epoxide hydrolase may also have an important, previously unrecognized functional role in JH regulation and insect metamorphosis. Multiple isoelectric forms of tissue‐specific JH esterases and JH epoxide hydrolases were found in integument, midgut, fat body, and brain. The JH esterases in these tissues had isoelectric points more acidic than that for plasma. Tissue α‐naphthyl acetate esterase, developmental profiles, and inhibitor sensitivity to 3‐(octylthio)‐1,1,1‐trifluoropropan‐2‐one differed significantly from that for JH esterase, suggesting that they represent different enzymes. ©1992 Wiley‐Liss, Inc.