@article{khalil_anspaugh_roe_2006, title={Role of juvenile hormone esterase and epoxide hydrolase in reproduction of the cotton bollworm, Helicoverpa zea}, volume={52}, ISSN={["0022-1910"]}, DOI={10.1016/j.jinsphys.2006.03.004}, abstractNote={The role of juvenile hormone (JH) esterase (JHE) and epoxide hydrolase (EH) in reproduction of the cotton bollworm, Helicoverpa zea, was investigated. Peak emergence of male and female bollworm adults occurred early in the scotophase. Female adults were added to males in a 1:2 ratio, respectively, at the beginning of the first photophase after emergence (d0). The highest oviposition rates for mated females were noted on d 2-4. The in vitro JH III esterase and JH III EH activity was measured in whole body homogenates of virgin and mated females from d0 to d8 post-emergence. Maximal JHE activity for virgin females occurred on d2 (1.09+/-0.14(+/-1 SEM) nmol of JH III degraded/min/mg protein), which was approximately twice that of mated females on the same day. The same results were observed for EH where the activity peaked on d2 at 0.053+/-0.003 as compared to 0.033+/-0.003 nmol of JH III degraded/min/mg protein, respectively. By d4, both JHE and JH EH activities declined significantly in virgin and mated females and were the same through d7. The developmental changes and effects of mating on JH degradation were similar when measured per insect. The highest levels of JHE and JH EH activity/min/mg protein in d2 virgin and mated females was found in ovaries followed by the carcass and then haemolymph; no EH activity was found in haemolymph as expected. For ovary, the JHE and JH EH activity was highest in virgin compared to mated females. The role of both enzymes in the regulation of reproduction is discussed.}, number={7}, journal={JOURNAL OF INSECT PHYSIOLOGY}, author={Khalil, Sayed M. S. and Anspaugh, Douglas D. and Roe, R. Michael}, year={2006}, month={Jul}, pages={669–678} }
 @article{anspaugh_roe_2005, title={Regulation of JH epoxide hydrolase versus JH esterase activity in the cabbage looper, Trichoplusia ni, by juvenile hormone and xenobiotics}, volume={51}, ISSN={["1879-1611"]}, DOI={10.1016/j.jinsphys.2004.12.008}, abstractNote={JH III esterase and JH III epoxide hydrolase (EH) in vitro activity was compared in whole body Trichoplusia ni homogenates at each stage of development (egg, larva, pupa and adult). While activity of both enzymes was detected at all ages tested, JH esterase was significantly higher than EH activity except for day three of the fifth (last) stadium (L5D3). For both enzymes, activity was highest in eggs. Adult virgin females had 4.6- and 4.0-fold higher JH esterase and EH activities, respectively, than adult virgin males. JH III metabolic activity also was measured in whole body homogenates of fifth stadium T. ni that were fed a nutritive diet (control) or starved on a non-nutritive diet of alphacel, agar and water. With larvae that were starved for 6, 28 and 52 h, EH activity per insect equivalent was 48%, 5% and 1%, respectively, of the control insects. At the same time points, JH esterase activity levels in starved T. ni were 29%, 4% and 3% of that of insects fed the nutritive diet. Selected insect hormones and xenobiotics were administered topically or orally to fifth stadium larvae for up to 52 h, and the effects on whole body EH and JH esterase activity analyzed. JH III increased the JH III esterase activity as high as 2.2-fold, but not the JH III EH activity. The JH analog, methoprene, increased both JH esterase and EH activity as high as 2.5-fold. The JH esterase inhibitor, 3-octylthio-1,1,1-trifluoropropan-2-one (OTFP), had no impact on EH activity. The epoxides trans- and cis-stilbene oxide (TSO and CSO) in separate experiments increased the EH activity approximately 2.0-fold. TSO did not alter JH esterase levels when topically applied, but oral administration reduced activity to 70% of the control at 28 h, and then increased the activity 1.8-fold at 52 h after the beginning of treatment. CSO had no effect on JH esterase activity. Phenobarbital increased EH activity by 1.9-fold, but did not change JH esterase levels. Clofibrate and cholesterol 5alpha,6alpha-epoxide had no effect on EH. JH esterase activity also was not affected by clofibrate, but cholesterol 5alpha,6alpha-epoxide reduced the JH esterase activity to 60-80% of the control. The biological significance of these results is discussed.}, number={5}, journal={JOURNAL OF INSECT PHYSIOLOGY}, author={Anspaugh, DD and Roe, RM}, year={2005}, month={May}, pages={523–535} }
 @article{roe_hodgson_rose_thompson_devorshak_anspaugh_linderman_harris_tomalski_1998, title={Basic principles and rationale for the use of insect genes in bioremediation: esterases, phosphotriesterase, cytochrome P450 and epoxide hydrolase}, volume={2}, number={1998}, journal={Reviews in Toxicology}, author={Roe, R. M. and Hodgson, E. and Rose, R. L. and Thompson, D. M. and Devorshak, C. and Anspaugh, D. D. and Linderman, R. J. and Harris, S. V. and Tomalski, M. D.}, year={1998}, pages={169–178} }
 @article{roe_anspaugh_venkatesh_linderman_graves_1997, title={A novel geminal diol as a highly specific and stable in vivo inhibitor of insect juvenile hormone esterase}, volume={36}, ISSN={["1520-6327"]}, DOI={10.1002/(SICI)1520-6327(1997)36:3<165::AID-ARCH2>3.0.CO;2-T}, abstractNote={Thio-containing and acetylenic trifluoromethyl ketones were potent inhibitors of insect juvenile hormone (JH) esterase with greater inhibitory activity than aliphatic and α,β-unsaturated homologs. Octylthio-1,1,1-trifluoropropan-2-one was the most potent inhibitor with the greatest equilibrium hydration constant in pure water. However, a keto/hydrate equilibrium was not necessary for JH esterase inhibition. The carbonyl tautomer of 1-octyl [1-(3,3,3-trifluoropropan-2,2- dihydroxy)] sulfone (OTPdOH-sulfone) was not detectable, and yet OTPdOH-sulfone was a potent in vitro inhibitor of JH esterase with an I50 of 1.2 nM. The mechanism of JH esterase inhibition by these compounds is discussed. OTPdOH-sulfone inhibited JH esterase with minimal activity toward insect 1-naphthyl acetate esterase and electric eel acetylcholinesterase. The inhibitor was also active in vivo, selective for JH esterase, and persistent for over 32 h. OTPdOH-sulfone when topically applied to larval and adult cabbage loopers, Trichoplusia ni, elicited juvenoid activity apparently because of the specific in vivo inhibition of JH metabolism. Arch. Insect Biochem. Physiol. 36:165–179, 1997. © 1997 Wiley-Liss, Inc.}, number={3}, journal={ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY}, author={Roe, RM and Anspaugh, DD and Venkatesh, K and Linderman, RJ and Graves, DM}, year={1997}, pages={165–179} }
 @article{anspaugh_kennedy_roe_1995, title={Purification and Characterization of a Resistance-Associated Esterase from the Colorado Potato Beetle, Leptinotarsa decemlineata (Say)}, volume={53}, ISSN={0048-3575}, url={http://dx.doi.org/10.1006/pest.1995.1057}, DOI={10.1006/pest.1995.1057}, abstractNote={Abstract Two strains of the Colorado potato beetle (CPB), Leptinotarsa decemlineata (Say) (Coleoptera: Chrysomelidae), were found to be resistant to carbofuran and azinphosmethyl when compared to a susceptible strain in bioassays using a discriminating insecticide dose. The percentage of mortalities for carbofuran were 115.1- and 70.8-fold lower in the resistant New York (NY) and Hot Spot (HS) strains, respectively, than in susceptible beetles. When treated with azinphosmethyl, the percentages of mortalities for the NY and HS populations were 65.1- and 4.4-fold lower, respectively, than the susceptible strain. The synergist S,S,S-tributyl phosphorotrithioate (DEF) increased azinphosmethyl toxicity, suggesting esterase involvement in azinphosmethyl resistance. Although 1-naphthyl acetate esterase activities in individual fourth instars of resistant strains were not significantly different, a novel resistance-associated esterase (RAE) (p I = 6.23) was discovered in the first and fourth instars and adults of NY and HS CPBs, but not in the susceptible strain. The RAE was purified from fourth stadium NY CPBs by Rotofor followed by polyacrylamide gel isoelectric focusing. Methyl paraoxon was the most potent inhibitor of the purified RAE with an I 50 of 0.1 μ M . The esterase inhibitors octylihio-1,1,1-trifluoropropan-2-one (OTFP), DEF, and azinphosmethyl had I 50 s of 1.1, 5.5, and 9.8 μ M, respectively. Carbofuran and eserine hemisulfate were poor inhibitors, with I 50 s greater than 100 μ M . In substrate competition assays with the RAE, methyl paraoxon and OTFP were competitive inhibitors.}, number={2}, journal={Pesticide Biochemistry and Physiology}, publisher={Elsevier BV}, author={Anspaugh, D.D. and Kennedy, G.G. and Roe, R.M.}, year={1995}, month={Oct}, pages={84–96} }
 @article{anspaugh_rose_koehler_hodgson_roe_1994, title={MULTIPLE MECHANISMS OF PYRETHROID RESISTANCE IN THE GERMAN-COCKROACH, BLATTELLA-GERMANICA (L)}, volume={50}, ISSN={["0048-3575"]}, DOI={10.1006/pest.1994.1066}, abstractNote={Abstract Pyrethroid-resistant German cockroaches known as the Village Green strain were compared to a susceptible (Orlando Normal) strain in respect to possible mechanisms of insecticide resistance. Male adults of the resistant strain weighed 15% more than susceptible roaches of the same cumulative age from adult eclosion. Based on the topical application of different concentrations of permethrin, the KD 50 for resistant roaches was 20-times greater than that for susceptible insects. Reduced penetration of [ 14 C]permethrin was observed in resistant insects during 24 hr after treatment along with increased in vivo metabolism as compared with susceptible controls. The cytochrome P450 content and monooxygenase activity when measured with methoxyresorufin and benzo[ a ]pyrene was elevated in resistant roaches by as much as 6.9-fold but no difference was found with benzphetamine. The glutathione transferase activity was also increased (1.6-fold with chlorodinitrobenzene) and elevated esterase activity was detected with the substrates, 1-naphthyl acetate (1.7-fold) and p -nitrophenyl acetate (2.1-fold). Using isoelectric focusing, a novel E 2 esterase was identified in resistant cockroaches not found in the susceptible population. E 2 may be partly responsible for the increased esterase activity observed in resistant roaches. Increased esterase activity toward p -nitrophenyl acetate was used to develop a kinetic, diagnostic assay that could rapidly discriminate resistant from susceptible individuals.}, number={2}, journal={PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY}, author={ANSPAUGH, DD and ROSE, RL and KOEHLER, PG and HODGSON, E and ROE, RM}, year={1994}, month={Oct}, pages={138–148} }