{"title":"Effects of lectins and tunicamycin on IL-1 binding to YT cells.","authors":"S C Speziale, L C Ginsberg, J W Paslay","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Specific binding of iodinated-interleukin-1 alpha or beta to YT cells could be inhibited by the lectins wheat germ agglutinin (WGA) and concanavalin A (Con A). WGA and Con A inhibition of IL-1 binding was abrogated by previous exposure of these plant proteins to the lectin-specific sugars N-acetylglucosamine (GlcNAc) and methyl glucoside (MG), respectively. Tunicamycin, an inhibitor of glycosylation, decreased interleukin-1 (IL-1) binding to YT cells, but also reduced total protein synthesis. These observations suggest that carbohydrate moieties on or near the interleukin-1 receptor may be important for optimal receptor binding of IL-1 to intact YT cells.</p>","PeriodicalId":18130,"journal":{"name":"Lymphokine research","volume":"8 1","pages":"1-8"},"PeriodicalIF":0.0000,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Lymphokine research","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Specific binding of iodinated-interleukin-1 alpha or beta to YT cells could be inhibited by the lectins wheat germ agglutinin (WGA) and concanavalin A (Con A). WGA and Con A inhibition of IL-1 binding was abrogated by previous exposure of these plant proteins to the lectin-specific sugars N-acetylglucosamine (GlcNAc) and methyl glucoside (MG), respectively. Tunicamycin, an inhibitor of glycosylation, decreased interleukin-1 (IL-1) binding to YT cells, but also reduced total protein synthesis. These observations suggest that carbohydrate moieties on or near the interleukin-1 receptor may be important for optimal receptor binding of IL-1 to intact YT cells.