Properties of the digestive enzymes and the permeability of the peritrophic membrane of Spodoptera frugiperda (Lepidoptera) larvae

Ferreira, Clélia; Capella, A.; Sitnik, Roberta; Terra, Walter R.

doi:10.1016/0300-9629(94)90362-x

Cited by 74 publications

(54 citation statements)

References 33 publications

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“…Amylase and trypsin are derived from membrane-bound forms, and are released in a soluble form by a microapocrine mechanism into the ectoperitrophic space and diffused into the endoperitrophic space (Ferreira et al, 1994b). Part of the amylase (13%) and trypsin (18%) remains membrane-bound and some is incorporated into the peritrophic membrane (PM) (Ferreira et al, 1994a). That almost all trypsin and amylase activity in the current study is found in the ventricular lumen, and only about 20% in the cellular fraction, corroborates that earlier study.…”

Section: Discussionmentioning

confidence: 99%

Control of the release of digestive enzymes in the larvae of the fall armyworm, Spodoptera frugiperda

Lwalaba

Hoffmann

Woodring

2009

Arch Insect Biochem Physiol

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There is a basal level of enzyme activity for trypsin, aminopeptidase, amylase, and lipase in the gut of unfed larval (L6) Spodoptera frugiperda. Trypsin activity does not decrease with non-feeding, possibly because of the low protein levels in plants along with high amino acid requirements for growth and storage (for later reproduction in adults). Therefore, trypsin must always be present so that only a minimal protein loss via egestion occurs. Larvae, however, adjust amylase activity to carbohydrate ingestion, and indeed amylase activity is five-fold higher in fed larvae compared to unfed larvae. Gut lipase activity is low, typical of insects with a high carbohydrate diet. A flat-sheet preparation of the ventriculus was used to measure the release of enzymes in response to specific nutrients and known brain/gut hormones in S. frugiperda. Sugars greatly increase (>300%) amylase release, but starch has no effect. Proteins and amino acids have little or no effect on trypsin or aminopeptidase release. The control of enzyme release in response to food is likely mediated through neurohormones. Indeed, an allatostatin (Spofr-AS A5) inhibits amylase and trypsin, and allatotropin (Manse- AT) stimulates amylase and trypsin release. Spofr-AS A5 also inhibits ileum myoactivity and Manse-AT stimulates myoactivity. The epithelial secretion rate of amylase and trypsin was about 20% of the amount of enzyme present in the ventricular lumen, which, considering the efficient counter-current recycling of enzymes, suggests that the secretion rate is adequate to replace egested enzymes.

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Section: Discussionmentioning

confidence: 99%

Control of the release of digestive enzymes in the larvae of the fall armyworm, Spodoptera frugiperda

Lwalaba

Hoffmann

Woodring

2009

Arch Insect Biochem Physiol

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“…SKTI and CpTI (cowpea trypsin inhibitor) were shown to be active against tomato moth larvae (L. oleracea). Serine proteinases [24] acted on H. armigera, H. virenscens and L. cuprina, in which SKTI was the most effective among the inhibitors tested [54][55][56][57][58][59]. ApTI (Adenanthera pavonina trypsin inhibitor) and DMTI-II (Dimorphandra mollis trypsin inhibitor) inhibited 84% [20] and 80% [47] of the digestive trypsin-like enzymes of C. maculatus, a Colepteran (Bruchidae).…”

Section: Discussionmentioning

confidence: 99%

Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

Gomes

Barbosa

Macedo

et al. 2005

Plant Physiology and Biochemistry

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“…This suggests that aminopeptidase-carrying vesicles are more easily solubilized in the ectoperitrophic fluid before incorporation than those carrying amylase and trypsin. The significant amounts of aminopeptidase recovered inside PM may correspond to a minor aminopeptidase distinct from the major microvillar aminopeptidase (Ferreira et al 1994a). …”

Section: Association Of Digestive Enzymes With Pm and Midgut Contentsmentioning

confidence: 98%

“…The new pellet corresponds to the vesicles and the new supernatant to the fluid. Calculated from Ferreira et al (1994a). c PM cleaned from contents was homogenized in dissecting saline.…”

Section: Effect Of Calcofluor In the Distribution Of Proteinases Alonmentioning

confidence: 99%

The peritrophic membrane of Spodoptera frugiperda: Secretion of peritrophins and role in immobilization and recycling digestive enzymes

Bolognesi

Ribeiro

Terra

et al. 2001

Arch Insect Biochem Physiol

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A peritrophin from the Spodoptera frugiperda peritrophic membrane (PM) and microvillar proteins from S. frugiperda anterior midgut cells were isolated and used to raise antibodies in a rabbit. These antibodies, as well as a Tenebrio molitor amylase antibody that cross-reacts with S. frugiperda amylases, and wheat-germ aglutinin were used in immunolocalization experiments performed with the aid of confocal fluorescence and immunogold techniques. The results showed that the peritrophin was secreted by anterior midgut columnar cells in vesicles pinched-off the microvilli (microapocrine secretion). The resulting double membrane vesicles become single membrane vesicles by membrane fusion, releasing peritrophin and part of the amylase and trypsin. The remaining membranes still containing microvillar proteins and membrane-bound amylase and trypsin are incorporated into a jelly-like material associated with PM. Calcofluor-treated larvae lacking a PM were shown to lose the decreasing gradient of trypsin and chymotrypsin observed along the midgut of control larvae. This gradient is thought to be formed by a countercurrent flux of fluid (in the space between PM and midgut cells) that powers enzyme recycling.

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Properties of the digestive enzymes and the permeability of the peritrophic membrane of Spodoptera frugiperda (Lepidoptera) larvae

Cited by 74 publications

References 33 publications

Control of the release of digestive enzymes in the larvae of the fall armyworm, Spodoptera frugiperda

Control of the release of digestive enzymes in the larvae of the fall armyworm, Spodoptera frugiperda

Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

The peritrophic membrane of Spodoptera frugiperda: Secretion of peritrophins and role in immobilization and recycling digestive enzymes

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