Influence of formamidines on batrachotoxin in a 20α-benzoate binding to neural membranes from pyrethroid susceptible and resistant tobacco budworm moths Heliothis virescens
{"title":"Influence of formamidines on batrachotoxin in a 20α-benzoate binding to neural membranes from pyrethroid susceptible and resistant tobacco budworm moths Heliothis virescens","authors":"C.J. Church, S.F. Abd-Elghafar, C.O. Knowles","doi":"10.1016/0742-8413(93)90084-X","DOIUrl":null,"url":null,"abstract":"<div><p>1. Amitraz stimulated [<sup>3</sup>H]batrachotoxin in A 20-α-benzoate ([<sup>3</sup>H]BTX-B) binding to neural membranes from pyrethroid susceptible (S) and resistant (R) tobacco budworm moths, but <em>N</em>′-(2,4-xylyl)-<em>N</em>-methylformamidine (SN 49844) stimulated binding only with S moths.</p><p>2. Chlordimeform stimulated [<sup>3</sup>H]BTX-B binding only with R moths, and <em>N</em>-(4-chloro-<em>o</em>-tolyl)-<em>N</em>-methylformamidine (demethylchlordimeform) yielded no significant stimulation with either strain.</p><p>3. A mixture of amitraz and deltamethrin, a pyrethroid that previously had been shown to enhance [<sup>3</sup>H]BTX-B binding with tobacco budworm moths, also gave significant stimulation of radioligand binding with S moths.</p><p>4. When membranes were prepared from S moths at various intervals following topical application of amitraz, deltamethrin, or a mixture of amitraz and deltamethrin, biphasic stimulation of [<sup>3</sup>H]BTX-B binding was observed, with maximum enhancement occurring at 2 and 6 hr.</p><p>5. These results provided a basis for suggesting that a formamidine binding site is located on or closely associated with the sodium channel protein.</p><p>6. Whether this site is the same as the pyrethroid/DDT binding domain remains to be demonstrated; however, similarities in responses elicited by amitraz and deltamethrin alone and in combination indicate that some relationship may exist.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 3","pages":"Pages 443-449"},"PeriodicalIF":0.0000,"publicationDate":"1993-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90084-X","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Comparative biochemistry and physiology. C: Comparative pharmacology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/074284139390084X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 2
Abstract
1. Amitraz stimulated [3H]batrachotoxin in A 20-α-benzoate ([3H]BTX-B) binding to neural membranes from pyrethroid susceptible (S) and resistant (R) tobacco budworm moths, but N′-(2,4-xylyl)-N-methylformamidine (SN 49844) stimulated binding only with S moths.
2. Chlordimeform stimulated [3H]BTX-B binding only with R moths, and N-(4-chloro-o-tolyl)-N-methylformamidine (demethylchlordimeform) yielded no significant stimulation with either strain.
3. A mixture of amitraz and deltamethrin, a pyrethroid that previously had been shown to enhance [3H]BTX-B binding with tobacco budworm moths, also gave significant stimulation of radioligand binding with S moths.
4. When membranes were prepared from S moths at various intervals following topical application of amitraz, deltamethrin, or a mixture of amitraz and deltamethrin, biphasic stimulation of [3H]BTX-B binding was observed, with maximum enhancement occurring at 2 and 6 hr.
5. These results provided a basis for suggesting that a formamidine binding site is located on or closely associated with the sodium channel protein.
6. Whether this site is the same as the pyrethroid/DDT binding domain remains to be demonstrated; however, similarities in responses elicited by amitraz and deltamethrin alone and in combination indicate that some relationship may exist.