Defense of parsnip webworm against phototoxic furanocoumarins: Role of antioxidant enzymes

Lee, Keywan; Berenbaum, May R.

doi:10.1007/bf01017468

Cited by 39 publications

(22 citation statements)

References 22 publications

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“…1) but substantially higher than levels reported for whole body homogenates in other lepidopterans [18,21]. The activity ranged from 5.4 to 6.7 nmollminlmg protein in the four replicates.…”

Section: Glutathione Reductasecontrasting

confidence: 41%

Ascorbate oxidation reduction in Helicoverpa zea as a scavenging system against dietary oxidants

Felton

Duffey

1992

Arch Insect Biochem Physiol

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We provide evidence of an important role for ascorbate free radical (AFR) reductase, dehydroascorbate (DHA) reductase, glutathione, and glutathione reductase as components of an oxidant-scavenging system in the midgut of larval Helicoverpa zea. Also, midgut ortho-quinone reductase is a potentially important constituent of the protective system against quinones. The midgut activities of AFR reductase, DHA reductase, glutathione reductase, and orthoquinone reductase were, respectively, 168,22.1,6, and 39.5 nmol/min/mg protein. The relatively high activity of these enzymes in the midgut provides circumstantial evidence for a protective mechanism utilizing ascorbate as an antioxidant and glutathione and/or NADPH as reductants. To our knowledge, the enzymes AFR reductase and DHA reductase have not been reported in insects. The particular relevance of this system to antioxidant protection, and in particular to the detoxication of quinones formed in damaged leaf tissues, is discussed.

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“…1) but substantially higher than levels reported for whole body homogenates in other lepidopterans [18,21]. The activity ranged from 5.4 to 6.7 nmollminlmg protein in the four replicates.…”

Section: Glutathione Reductasecontrasting

confidence: 41%

Ascorbate oxidation reduction in Helicoverpa zea as a scavenging system against dietary oxidants

Felton

Duffey

1992

Arch Insect Biochem Physiol

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“…The spring triticales strongly aVected SOD and CAT in the bird cherry-oat aphids. Lee and Berenbaum (1990) assumed that induction of the antioxidant enzymes in Depressaria pastinacella (Duponchel) (Lepidoptera, Oecophoridae) was associated with low level of cytochrome P-450-dependant polysubstrate monooxygenases (PSMO). Low PSMO leads to the accumulation of phototoxins within insect tissues and increased activity of antioxidant enzymes (Bull et al 1986).…”

Section: Discussionmentioning

confidence: 99%

Effect of host plant alternation on some adaptive enzymes of the bird cherry–oat aphid, Rhopalosiphum padi (L.)

Łukasik¹

2008

J Pest Sci

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Changes in the activity of some adaptive enzymes of the bird cherry-oat aphid R. padi after transfer from primary (bird cherry) to secondary (triticales) host plants were assessed. The following groups of enzymes were studied: (1) transferases-glutathione S-transferase (GST) and UDP-glucosyltransferase (UDPGT); (2) antioxidant enzymes-superoxide dismutase (SOD) and catalase (CAT); (3) oxidoreductases-polyphenol oxidase (PPO) and peroxidase (PX); and (4) glucoside hydrolases--and -glucosidase. The activity of the transferases and the antioxidant enzymes increased after transfer to the secondary host, but the level of activity was closely associated with feeding duration on the secondary host. The strongest induction was noted for SOD, the activity of which was more than three times greater on the secondary than on the primary host. In contrast, transfer of the bird cherry-oat aphid was accompanied by a decline in activity of PPO, PX, and -glucosidase; PPO and PX activity was 50% less in aphids fed on the secondary host rather than on the primary host. Activity of -glucosidase increased after prolonged feeding on the secondary host. The results indicated that the adaptive enzymes of the bird cherry-oat aphid enable it to feed on distantly related host plants.

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“…(Ahmad and Pardini, 1990;Lee and Berenbaum, 1990;Lee 1991;Aucoin et al, 1991;Felton and Duffey, 1991). Large amounts of ROS may be formed in insect tissues during flight or in specialized cases such as bioluminescence.…”

Section: Antioxidant Enzymatic Defensesmentioning

confidence: 99%

Antioxidant systems in insects

Felton

Summers

1995

Arch Insect Biochem Physiol

506

309

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Insects possess a suite of antioxidant enzymes and small molecular weight antioxidants that may form a concatenated response to an onslaught of dietary and endogenously produced oxidants. Antioxidant enzymes such as superoxide dismutase, catalase, glutathione transferase, and glutathione reductase have been characterized in insects. Water-soluble and lipid-soluble antioxidants such as ascorbate, glutathione, tocopherols, and carotenoids have not been well studied in insects but may play very important antioxidant roles. Additionally, the peritrophic matrix and trehalose may possess important antioxidant functions in insects. The enzymatic recycling of ascorbate, first noted in green plants, may also exist in insects. A greater understanding of these antioxidant systems may provide greater understanding about the ecological relationships of insects with their hosts.

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Defense of parsnip webworm against phototoxic furanocoumarins: Role of antioxidant enzymes

Cited by 39 publications

References 22 publications

Ascorbate oxidation reduction in Helicoverpa zea as a scavenging system against dietary oxidants

Ascorbate oxidation reduction in Helicoverpa zea as a scavenging system against dietary oxidants

Effect of host plant alternation on some adaptive enzymes of the bird cherry–oat aphid, Rhopalosiphum padi (L.)

Antioxidant systems in insects

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