Gary J. Murray , Thomas W. Doebber , T.Y. Shen , M.S. Wu , M.M. Ponpipom , R.L. Bugianesi , Roscoe O. Brady , John A. Barranger
{"title":"靶向合成糖基化人胎盘糖脑苷酶","authors":"Gary J. Murray , Thomas W. Doebber , T.Y. Shen , M.S. Wu , M.M. Ponpipom , R.L. Bugianesi , Roscoe O. Brady , John A. Barranger","doi":"10.1016/0006-2944(85)90117-6","DOIUrl":null,"url":null,"abstract":"<div><p>Human placental β-glucocerebrosidase modified by covalent attachment of <em>N</em><sup>2</sup>-{<em>N</em><sup>2</sup>,<em>N</em><sup>6</sup>-bis[3-(α-<span>d</span>-mannopyranosylthio)propionyl]-<span>l</span>-lysyl}-<em>N</em><sup>6</sup>-[3-(α-<span>d</span>-mannopyr-anosylthio) propionyl]-<span>l</span>-lysine was administered to rats by intravenous injection. Comparison of enzyme distribution in isolated liver cell populations indicates an increase in enzyme-specific activity of 18-fold in nonparenchymal cells and only 1.5-fold to hepatocytes compared to uninjected control animals. This macrophage-specific delivery of an active lysosomal enzyme has potential for application in enzyme replacement trials.</p></div>","PeriodicalId":8781,"journal":{"name":"Biochemical medicine","volume":"34 2","pages":"Pages 241-246"},"PeriodicalIF":0.0000,"publicationDate":"1985-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-2944(85)90117-6","citationCount":"15","resultStr":"{\"title\":\"Targeting of synthetically glycosylated human placental glucocerebrosidase\",\"authors\":\"Gary J. Murray , Thomas W. Doebber , T.Y. Shen , M.S. Wu , M.M. Ponpipom , R.L. Bugianesi , Roscoe O. Brady , John A. Barranger\",\"doi\":\"10.1016/0006-2944(85)90117-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Human placental β-glucocerebrosidase modified by covalent attachment of <em>N</em><sup>2</sup>-{<em>N</em><sup>2</sup>,<em>N</em><sup>6</sup>-bis[3-(α-<span>d</span>-mannopyranosylthio)propionyl]-<span>l</span>-lysyl}-<em>N</em><sup>6</sup>-[3-(α-<span>d</span>-mannopyr-anosylthio) propionyl]-<span>l</span>-lysine was administered to rats by intravenous injection. Comparison of enzyme distribution in isolated liver cell populations indicates an increase in enzyme-specific activity of 18-fold in nonparenchymal cells and only 1.5-fold to hepatocytes compared to uninjected control animals. This macrophage-specific delivery of an active lysosomal enzyme has potential for application in enzyme replacement trials.</p></div>\",\"PeriodicalId\":8781,\"journal\":{\"name\":\"Biochemical medicine\",\"volume\":\"34 2\",\"pages\":\"Pages 241-246\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1985-10-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0006-2944(85)90117-6\",\"citationCount\":\"15\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemical medicine\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0006294485901176\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemical medicine","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0006294485901176","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Targeting of synthetically glycosylated human placental glucocerebrosidase
Human placental β-glucocerebrosidase modified by covalent attachment of N2-{N2,N6-bis[3-(α-d-mannopyranosylthio)propionyl]-l-lysyl}-N6-[3-(α-d-mannopyr-anosylthio) propionyl]-l-lysine was administered to rats by intravenous injection. Comparison of enzyme distribution in isolated liver cell populations indicates an increase in enzyme-specific activity of 18-fold in nonparenchymal cells and only 1.5-fold to hepatocytes compared to uninjected control animals. This macrophage-specific delivery of an active lysosomal enzyme has potential for application in enzyme replacement trials.
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