Journal of Chemical Ecology

, Volume 28, Issue 7, pp 1329–1347

Gut-Based Antioxidant Enzymes in a Polyphagous and a Graminivorous Grasshopper

  • Raymond V. Barbehenn
Article

Abstract

Graminivorous species of grasshoppers develop lethal lesions in their midgut epithelia when they ingest tannic acid, whereas polyphagous grass- hoppers are unaffected by ingested tannins. This study tests the hypothesis that polyphagous species are defended by higher activities of antioxidant enzymes (constitutive or inducible) in their guts than are graminivorous species. Comparisons were made between four antioxidant enzymes: superoxide dismutase (SOD), catalase (CAT), ascorbate peroxidase (APOX), and glutathione transferase peroxidase (GSTPX). Enzyme activities were measured in the gut lumens and midgut tissues of Melanoplus sanguinipes (polyphagous) and Aulocara ellioti (graminivorous). The results of this study do not support the hypothesis that M. sanguinipes is better defended by antioxidant enzymes than is A. ellioti, nor are these enzymes more inducible in M. sanguinipes than in A. ellioti when insects consume food containing 15% dry weight tannic acid. Instead, tannic acid consumption reduced SOD, APOX, and GSTPX activities in both species. This study reports the first evidence that SOD is secreted into the midgut lumen in insects, with activities two- to fourfold higher than those found in midgut tissues. The spatial distribution of GSTPX and APOX activities observed in both species suggests that ingested plant antioxidant enzymes may function as acquired defenses in grasshoppers. In addition, the results of this study permit the first comparison between the antioxidant enzyme defenses of Orthoptera and Lepidoptera. Most notably, grasshoppers have higher SOD activities than caterpillars, but completely lack APOX in their midgut tissues.

Grasshopper Orthoptera Acrididae graminivorous polyphagous herbivore Melanoplus Aulocara antioxidant enzyme superoxide dismutase catalase ascorbate peroxidase glutathione transferase peroxidase 

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Copyright information

© Plenum Publishing Corporation 2002

Authors and Affiliations

  • Raymond V. Barbehenn
    • 1
  1. 1.Department of Ecology and Evolutionary Biology, Department of Molecular, Cellular and Developmental BiologyUniversity of MichiganAnn Arbor

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