Modulatory Effects of Natural Curcuminoids on P-Glycoprotein ATPase of Insecticide-Resistant Pest Helicoverpa armigera (Lepidopetera: Noctüidae)
| Autor: | S. K. Jayalakshmi, K. Sreeramulu, Ravindra M. Aurade |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Curcumin
endocrine system diseases Physiology ATPase Biophysics Moths Helicoverpa armigera Insecticide Resistance chemistry.chemical_compound Curcuma polycyclic compounds Animals ATP Binding Cassette Transporter Subfamily B Member 1 Curcuminoid P-glycoprotein Adenosine Triphosphatases Quenching (fluorescence) integumentary system biology Plant Extracts Substrate (chemistry) Cell Biology biology.organism_classification female genital diseases and pregnancy complications Enzyme Activation carbohydrates (lipids) Biochemistry chemistry biology.protein Noctuidae |
| Zdroj: | The Journal of Membrane Biology. 236:271-278 |
| ISSN: | 1432-1424 0022-2631 |
| DOI: | 10.1007/s00232-010-9299-5 |
| Popis: | Three major curcuminoids (I, II and III) were purified from turmeric and tested for their ability to modulate the function of P-glycoprotein ATPase of the insecticide-resistant pest Helicoverpa armigera (Ha-Pgp). The curcumin mixture inhibited the activity of Ha-Pgp ATPase by 80-90% at 100 μM concentration. Along with curcuminoids I, II and III, it inhibited the verapamil- and ethylparaoxon-stimulated Ha-Pgp ATPase activity. Curcuminoid binding was quantitated by quenching the intrinsic Trp fluorescence of purified Ha-Pgp ATPase. Transport was monitored in proteoliposomes containing Ha-Pgp ATPase using the high-affinity fluorescent substrate tetramethylrosamine (TMR) in real time. Addition of the curcuminoid mixture collapsed the TMR concentration gradient generated by Ha-Pgp ATPase. Inhibition studies on Ha-Pgp ATPase activity are important to develop strategies to overcome insecticide resistance in this pest. |
| Databáze: | OpenAIRE |
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