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Binding of 1,1,1-trichloro-2,2-di-p-chlorophenylethane (DDT) with subcellular fractions of rat brain.

ABSTRACT: DDT (1,1,1-trichloro-2,2-di-p-chlorophenylethane) and DDE (1,1-dichloro-2,2-di-p-chlorophenylethylene, a non-insecticidal analogue of DDT) were found to bind with various nerve components of rat brain. The amount of DDT binding exceeded that of DDE only in the fraction containing mainly the nerve endings. Among various components in the nerve-ending fraction, a subfraction containing mainly the pre- and post-synaptic complexes had the highest affinity for DDT in comparison with that for DDE. By using an ;acetone-powdering' technique on brain preparations, the Sephadex-column method was shown to provide reliable results for studies on the binding of DDT or DDE with soluble proteins in the nerve tissues. From these results it was concluded that DDE had a higher affinity for soluble components of the rat brain than did DDT.

SUBMITTER: Brunnert H

PROVIDER: S-EPMC1184805 | biostudies-other | 1969 Aug

REPOSITORIES: biostudies-other

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Evidence for Dual Binding Sites for 1,1,1-Trichloro-2,2-bis(p-chlorophenyl)ethane (DDT) in Insect Sodium Channels.

Project description:1,1,1-Trichloro-2,2-bis(p-chlorophenyl)ethane (DDT), the first organochlorine insecticide, and pyrethroid insecticides are sodium channel agonists. Although the use of DDT is banned in most of the world due to its detrimental impact on the ecosystem, indoor residual spraying of DDT is still recommended for malaria control in Africa. Development of resistance to DDT and pyrethroids is a serious global obstacle for managing disease vectors. Mapping DDT binding sites is necessary for understanding mechanisms of resistance and modulation of sodium channels by structurally different ligands. The pioneering model of the housefly sodium channel visualized the first receptor for pyrethroids, PyR1, in the II/III domain interface and suggested that DDT binds within PyR1. Previously, we proposed the second pyrethroid receptor, PyR2, at the I/II domain interface. However, whether DDT binds to both pyrethroid receptor sites remains unknown. Here, using computational docking of DDT into the Kv1.2-based mosquito sodium channel model, we predict that two DDT molecules can bind simultaneously within PyR1 and PyR2. The bulky trichloromethyl group of each DDT molecule fits snugly between four helices in the bent domain interface, whereas two p-chlorophenyl rings extend into two wings of the interface. Model-driven mutagenesis and electrophysiological analysis confirmed these propositions and revealed 10 previously unknown DDT-sensing residues within PyR1 and PyR2. Our study proposes a dual DDT-receptor model and provides a structural background for rational development of new insecticides.

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1,1,1-Trichloro-2,2-bis-(4-iodo-phen-yl)ethane.

Project description:In the structure of the title compound, C(14)H(9)Cl(3)I(2), which is the 4-iodo-phenyl analogue of the insecticide DDT [1,1,1-tri-chloro-2,2-bis-(4-chloro-phen-yl)ethane], isomorphism between the two compounds has been confirmed. In the mol-ecule, the dihedral angle between the planes of the two benzene rings is 65.8 (4)° which compares with 64.7 (7)° in DDT.

| S-EPMC3414957 | biostudies-literature

2,2-Bis(4-but-oxy-phen-yl)-1,1,1-trichloro-ethane.

Project description:In the structure of the title compound, C(22)H(27)Cl(3)O(2), which is the 4-but-oxy-phenyl analogue of the insecticidally active 4-meth-oxy-phenyl compound meth-oxy-chlor, the dihedral angle between the two benzene rings is 79.61 (11)°. Present also in the structure is an intra-molecular aromatic C-H⋯Cl inter-action.

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The inhibition of 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane (DDT) dehydrochlorinase and glutathione S-aryltransferase in grass-grub and housefly preparations.

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1,1,1-Trichloro-2,2-bis-(4-eth-oxy-phen-yl)ethane.

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| S-EPMC3515304 | biostudies-other

Role of cyclic adenosine 3':5'-monophosphate in the action of 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane (DDT)on hepatic and renal metabolism.

Project description:The possibility whether alterations in the cyclic AMP-adenylate cyclase-phosphodiesterase system play a role in the action of 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane (DDT) on hepatic and renal carbohydrate metabolism was investigated. Administration of exogenous cyclic AMP (10mg/100g) was found to mimic the action of DDT which enhanced the activities of pyruvate carboxylase, phosphoenolpyruvate carboxylase, fructose 1,6-diphosphatase and glucose 6-phosphatase in both liver and kidney cortex, elevated the concentration of blood glucose and urea and decreased the amount of hepatic glycogen. Treatment with theophylline augmented the effects of a submaximal dose of this halogenated hydrocarbon on serum urea and glucose as well as the key gluconeogenic enzymes in liver and kidney cortex. Addition of DDT in vitro to liver and kidney homogenates resulted in a significant enhancement of adenylate cyclase activity. Hepatic and renal slices from rats already treated with DDT displayed an increased ability to convert [(3)H]adenosine into cyclic [(3)H]AMP. Whereas kidney-cortex slices excised from rats given caffeine and DDT produced an even greater amount of cyclic [(3)H]AMP, imidazole, propranolol and hydrazine prevented the insecticide-stimulated rise in cyclic nucleotide production. In contrast, prostaglandin E(1) failed to exert any significant effect on DDT-induced increases in cyclic [(3)H]AMP synthesis from radioactive adenosine. The present study and our previous findings (Kacew & Singhal, 1973e) support the concept that the DDT-induced alterations in carbohydrate metabolism of liver and kidney cortex may be related to an initial stimulation of the cyclic AMP-adenylate cyclase system in these tissues.

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The separation of multiple forms of housefly 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane (DDT) dehydrochlorinase from glutathione S-aryltransferase by electrofocusing and electrophoresis.

Project description:Electrophoresis in a sucrose gradient at pH values between 5 and 8 separated housefly DDT [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane] dehydrochlorinase into two major fractions. GSH S-aryltransferase under similar conditions migrated as a single peak of activity. Separation of housefly homogenates or partially purified enzyme preparations by electrofocusing in a natural pH gradient also showed the presence of multiple forms of DDT dehydrochlorinase.

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Project description:Homogenates of liver were obtained from control rats and from rats that had received DDT [1,1,1-trichloro-2,2-bis(p-chlorophenyl)ethane]. The postmicrosomal supernatant fractions were used for the purification of elongation factor 1 by hydroxyapatite chromatography and phosphocellulose chromarography. The amount of binding factor present was essentially the same for both groups of animals, but the specific activity, as measured by the binding assay, was about twice as high in the DDT-treated preparations. After sucrose-gradient sedimentation, the difference in specific activity was found to reside in the low-molecular-weight (50000) form of elongation factor 1. The implications of an increased reactivity of elongation factor 1 during the induction of membrane enzymes are discussed.

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The effect of diet and 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane (DDT) on microsomal hydroxylating enzymes and on sensitivity of rats to carbon tetrachloride poisoning.

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