Affiliation:
1. Department of Medicine, University of Toledo Medical School, 3000 Arlington Avenue, 202 Health Education Building, Mail Stop 1025, Toledo, OH 43614, USA
2. Department of Biological Sciences, Bowling Green State University, Bowling Green, OH 43403, USA
3. Instituto de Quimica Medica (IQM-CSIC), Juan de la Cierva 3, 28006 Madrid, Spain
Abstract
The plant allelochemical, quinizarin (1,4-dihydroxy-9,10-anthraquinone), and five anthraquinones that were synthesized from quinizarin, namely, 1,4-anthraquinone; 2-hydroxy-1,4-anthraquinone; 2-methoxy-1,4-anthraquinone; 9-hydroxy-1,4-anthraquinone; and 9-methoxy-1,4-anthraquinone, were assessed as to their effects on the essential, P450-dependent ecdysone 20-monooxygenase system of the insect modelManduca sexta(tobacco hornworm). This steroid hydroxylase converts the arthropod molting hormone, ecdysone, to the physiologically required 20-hydroxyecdysone form.M. sextafifth larval instar midgut homogenates were incubated with increasing concentrations (10−8to 10−3 M) of each of the six anthraquinones followed by ecdysone 20-monooxygenase assessments using a radioenzymological assay. Four of the five anthraquinones exhibitedI50’s of about4×10-6to6×10-2 M. The most effective inhibitors were 2-methoxy-1,4-anthraquinone and 1,4-anthraquinone followed by 9-hydroxy-1,4 anthraquinone and 9-methoxy-1,4-anthraquinone. At lower concentrations the latter anthraquinone stimulated E20M activity. Quinizarin was less inhibitory and 2-hydroxy-1,4-anthraquinone was essentially without effect. Significantly, these studies make evident for the first time that anthraquinones can affect insect E20M activity, and thus insect endocrine regulation and development, and that a relationship between anthraquinone structure and effectiveness is apparent. These studies represent the first demonstrations of anthraquinones affecting any steroid hydroxylase system.
Subject
Animal Science and Zoology