Apparent inhibition of in vitro juvenile hormone biosynthesis by the corpus cardiacum of adult crickets (Gryllus bimaculatus and Acheta domesticus) is due to juvenile hormone esterase

When measuring the in vitro JH III-biosynthesis by corpora allata (CA) from adult female crickets in the presence of corpora cardiaca (CC), the amount of JH III in the medium decreased in a dose dependent manner. The CC of a 4-day-old female Gryllus bimaculatus contain 42 pmol.pair CC⁻¹ Grb-AKH, 0.62 pmol.pair CC⁻¹ octopamine, and a JH-esterase activity of 9.8 pmol JH.h⁻¹.pair CC⁻¹. Comparable values for Acheta domesticus are 21 pmol.pair CC⁻¹ Grb-AKH, 0.53 pmol.pair CC⁻¹ octopamine, and 6.5 pmolJH.h⁻¹.pair CC⁻¹ of JH-esterase activity. Even if the entire octopamine content of the CC were released into the medium, the concentration would be below the 10⁻⁵ M threshold for octopamine inhibition of JH synthesis. An in vitro AKH inhibition of JH III synthesis was observed, but only at a relatively high concentration (10⁻⁵ M). If the entire AKH content (10⁻⁶ M) of the CC were released into the medium, the AKH concentration would approach JH synthesis inhibiting levels. However, the rate of release of AKH in vitro was very low, and, therefore, AKH from the CC could not affect JH synthesis. In contrast, a specific JH-esterase, released by isolated CC into the medium, was sufficiently high in both cricket species to account for the observed decrease in JH III present. OTFP-sulfone (10⁻⁵ M) restored apparent JH synthesis of the CA to the control level. There was no reduction in the amount of JH released when CA were incubated with heat treated CC. The CA themselves contained almost no JH-esterase activity. © 1997 Wiley-Liss, Inc.     

The genetics of esterases in Drosophila. VIII. The gene regulating the activity of JH-esterase in D. virilis

The content of JH-esterase was assayed by radial immunodiffusion in Drosophila virilis pupae under normal conditions and under the effects of extreme factors. It was found that JH-esterase content is the same (not different from the control) in pupae showing a high activity of the enzyme and in those not showing it. These data are evidence for a gene controlling JH-esterase activity. It was also shown that a regulatory factor converts inactive into active JH-esterase when homogenates of pupae, with active and inactive forms, were mixed and incubated together. It was demonstrated that the source of the activating factor is the larval brain. Sublines 147-R and 147-I were produced by introducing the second chromosome pair of stocks 103 and 101, which are heat resistant, into the genome of individuals of stock 147, which is heat sensitive. Sublines 160-III, 160-IV, 160-V, and 160-VI were produced by introducing the third, fourth, fifth, and sixth chromosome pairs of stock 147 into the genome of stock 160S, which is heat-resistant. The results of analysis of JH-esterase activity and the viability of individuals of these sublines at high temperatures indicated that the gene regulating the activity of JH-esterase is located in the sixth chromosome of D. virilis.