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Biomedical subjects

L B Brattsten

Publications and source records attributed to L B Brattsten.

8 recordsLinked to original sources

Sex-related differences in the tolerance of Oriental fruit moth (Grapholita molesta) to organophosphate insecticides.

In vivo toxicity assays have shown that organophosphate insecticides are less toxic to male than to female Oriental fruit moths Grapholita molesta. While male moths have higher levels of acetylcholinesterase and general esterase activities, female moth acetylcholinesterase enzymes are less sensitive to aromatic and aliphatic organophosphates than male enzymes. Elevated esterase and acetylcholinesterase activities in male moths explain their greater tolerance to aromatic and aliphatic organophosphates. Male and female acetylcholinesterase enzymes are equally tolerant to heteroaromatic organophosphates, the most widely used of this class of insecticides in G molesta control. This observation, in contrast to the greater sensitivity of male acetylcholinesterases to aromatic and aliphatic organophosphates, shows the potential for the evolution of insensitive target sites in male moths, which would increase male G molesta tolerance to these insecticides. Significant sex-linked differences in insecticide tolerance have not been reported previously in lepidopterans. The practical implications of the observed differences in tolerance in male and female G molesta question the practice of using pheromone traps to monitor populations of these moths in orchards.

Acetylcholinesterase↗

Induction by carrot allelochemicals of insecticide-metabolising enzymes in the southern armyworm (Spodoptera eridania).

Carrot foliage monoterpenes induce cytochrome P-450 up to 2.9-fold, NADPH cytochrome c (P-450) reductase up to 1.6-fold, NADPH-oxidation up to 3.8-fold, aldrin epoxidation up to 1.5-fold in southern armyworm larval midgut tissues when incorporated in their diet at 0.2% for 3 days. Stigmasterol and ergosterol did not substantially induce microsomal oxidase activities and significantly inhibited GSH S-aryltransferase activity and sulfotransferase activity. Coumarin did not substantially affect microsomal oxidase and sulfotransferase activity but is the most potent inducer of GSH S-aryltransferase activity, increasing this activity 7-fold. None of the chemicals is acutely toxic to the sixth instar larvae or affect the larval weight gain except coumarin which significantly depressed the maximal body weight attained.

Animals↗

Insecticide solvents: interference with insecticidal action.

Several commercial solvent mixtures commonly used as insecticide carriers in spray formulations increase by more than threefold the microsomal N-demethylation of p-chloro N-methylaniline in midgut preparations of southern army-worm (Spodoptera eridania) larvae exposed orally to the test solvents. Under laboratory conditions, the same solvent mixtures exhibit a protective action against the in vivo toxicity of the insecticide carbaryl to the larvae. The data are discussed with respect to possible solvent-insecticide interactions occurring under field conditions and, more broadly, to potential toxicological hazards of these solvents to humans.

Enzyme Induction↗

Further toxicologic studies with commercial and candidate flame retardant chemicals. Part II.

A number of commercial and candidate flame retardants were studied with regard to their toxicity to goldfish, inhibition of cholinesterase, inhibition of acetyl choline binding to its receptor and insecticidal properties. Several of the flame retardants were notably toxic to fish. Some of the compounds showed modest inhibition of cholinesterase and/or microsomal oxidases, but none inhibited acetyl choline receptor binding. Whereas several of the flame retardants showed little or no insecticidal properties when added alone to a housefly diet, piperonyl butoxide greatly synergised their toxicity to houseflies.

Acetylcholine↗

Properties of 5-aminolaevulinate synthetase and its relationship to microsomal mixed-function oxidation in the southern armyworm (Spodoptera eridania).

1. Activity of 5-aminolaevulinate synthetase was measured in the midgut and other tissues of the last larval instar of the southern armyworm (Spodoptera eridania Cramer, formerly Prodenia eridania Cramer). 2. Optimum conditions for measuring the activity were established with respect to all variables involved and considerable differences from those reported for mammalian enzyme preparations were found. 3. Maximum activity (20 nmol/h per mg of protein) occurs 18-24 h after the fifth moult and thereafter decreases to trace amounts as the larvae age and approach pupation. 4. Synthetase activity was rapidly induced by oral administration (in the diet) of pentamethylbenzene, phenobarbital, diethyl 1,4-dihydro-2,4,6-trimethylpyridine-3, 5-dicarboxylate, and 2-allyl-2-isopropylacetamide. 5. Puromycin inhibited the induction of synthetase by pentamethylbenzene. 6. Induction of 5-aminolaevulinate synthetase correlated well with the induction of microsomal N-demethylation of p-chloro-N-methylaniline, except for phenobarbital, which induced the microsomal oxidase relatively more than the synthetase.

5-Aminolevulinate Synthetase↗