Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractVolatilome of Aleppo Pine litter over decomposition process    Next AbstractProfiles of Volatile Biomarkers Detect Tuberculosis from Skin »

FEBS Lett


Title:The proregion of papaya proteinase IV inhibits Colorado potato beetle digestive cysteine proteinases
Author(s):Visal S; Taylor MA; Michaud D;
Address:"Centre de Recherche en Horticulture, FSAA, Universite Laval, Sainte-Foy, Que., Canada"
Journal Title:FEBS Lett
Year:1998
Volume:434
Issue:3
Page Number:401 - 405
DOI: 10.1016/s0014-5793(98)01018-7
ISSN/ISBN:0014-5793 (Print) 0014-5793 (Linking)
Abstract:"Three distinct digestive protease systems were induced in larvae of the herbivorous pest, Colorado potato beetle (CPB; Leptinotarsa decemlineata Say), and used as a model to assess the ability of the proregion of papaya proteinase IV (PPIV; glycyl endopeptidase, EC 3.4.22.25) to act as an inhibitor of insect digestive cysteine proteinases. As shown by gelatin/PAGE and complementary inhibition assays, a recombinant form of the proregion produced in Escherichia coli inhibited a fraction of the insect proteases also inhibited by the well-characterized inhibitor of cysteine proteinases, oryzacystatin I (OCI). In contrast with OCI, the inhibitory potency of the proregion was affected by an increase of the temperature, suggesting a certain alteration of its structural integrity by the insect non-target proteases. This apparent susceptibility to proteolysis was confirmed by SDS-PAGE, after challenging the proregion with the different insect extracts. As seen on gel, selective inhibition of the insect aspartate proteinase, cathepsin D, with the inhibitor pepstatin A preserved the activity of the proregion against cysteine proteinases by preventing its hydrolysis. Taken together, these observations suggest the potential of plant protease proregions as regulators of cysteine proteinases in biotechnological systems, and show the ability of protease inhibitors to preserve the integrity of 'companion' defense-related proteins from the action of insensitive proteases in target pests"
Keywords:Animals Coleoptera/*enzymology Cystatins/pharmacology Cysteine Endopeptidases/chemistry/*metabolism Cysteine Proteinase Inhibitors/*metabolism Digestive System/*enzymology Larva/enzymology;
Notes:"MedlineVisal, S Taylor, M A Michaud, D eng Research Support, Non-U.S. Gov't England 1998/09/22 FEBS Lett. 1998 Sep 4; 434(3):401-5. doi: 10.1016/s0014-5793(98)01018-7"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 22-11-2024