Exogenous and endogenous protease inhibitors in the gut of the fall armyworm larvae, Spodoptera frugiperda.
A dose-dependent inhibition of endogenous trypsin and aminopeptidase occurs in the lumen of Spodoptera frugiperda after feeding L6 larvae exogenous inhibitors soybean trypsin inhibitor (SBTI), tosyl-L-lysine chloromethyl ketone-HCl (TLCK), or bestatin, respectively, for 3 days. TLCK inhibits trypsin in tissue extracts and in secretions more strongly than SBTI. The aminopeptidase released into the lumen (containing the peritrophic membrane) is strongly inhibited by bestatin, but the membrane-bound enzyme is not. A bound enzyme may be more resistant to an inhibitor than unbound. A cross-class elevation of aminopeptidase activity occurs in response to ingested trypsin inhibitor, but there was no cross-class effect of aminopeptidase inhibitor (bestatin) on trypsin activity. An endogenous trypsin and aminopeptidase inhibitor is present in the lumen and ventricular cells. The strength of the endogenous trypsin inhibition seems to be in the same range as that resulting from ingestion of the exogenous inhibitor SBTI. In some insect species, considerable trypsin secretion occurs in unfed as well as in fed animals, and endogenous protease inhibitors might function to protect the ventricular epithelium by inactivation of trypsin when less food is available.
Lwalaba
Digali
D
Department of Animal Ecology I, University of Bayreuth, Bayreuth, Germany.
Weidlich
Sandy
S
Hoffmann
Klaus H
KH
Woodring
Joseph
J
D000626:Aminopeptidases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000818:Animals; D007814:Larva / Q000235:genetics / Q000378:metabolism; D018411:Spodoptera / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000235:genetics* / Q000378:metabolism* / Q000494:pharmacology
D014361:Trypsin Inhibitors; D000626:Aminopeptidases; D014357:Trypsin