Abstract

In order to further elucidate the biochemical mechanisms responsible for insecticide resistance in insects, we have determined changes in the activity levels of a comprehensive range of proteolytic enzymes (cytoplasmic and lysosomal proteinases and peptidases, which play a key role in normal cell functioning) in fenitrothion-resistant (571ab) and susceptible (Cooper) strains of Musca domestica following in vivo exposure to the insecticide fenitrothion. Untreated insects of the resistant strain had significantly higher levels (20–100%) of activity for many protease types compared to the susceptible strain (whole body analysis). Exposure to fenitrothion resulted in further activity increases for most proteases at some point during the subsequent 24 h period in resistant strain insects; susceptible strain insects were also capable of similar increases in protease activities. We therefore suggest that it must be the combination of intrinsically higher protease levels (prior to pesticide exposure), together with the capacity to further increase protease activities following insecticide exposure, which is important in the mechanism by which proteases may confer survival advantages in insecticide resistant insects. We further speculate that this mechanism may involve increased supply of precursor amino acids from proteolytic degradation products to the intracellular pool, prior to de novo synthesis of detoxifying enzymes following insecticide exposure

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