{"title":"Recombinant epithelial cell mucin (MUC-1) expressed in baculovirus resembles antigenically tumor associated mucin, target for cancer immunotherapy.","authors":"P Ciborowski, O J Finn","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Epithelial cell mucin encoded by the gene MUC-1, is expressed on several human adenocarcinomas in an aberrantly glycosylated form, and as such it has been identified as the target of human cellular as well as humoral responses. In order to harness this immunity to combat mucin-expressing tumors, various forms of this molecule, synthetic or highly purified, are being tested as possible cancer vaccines. We have expressed MUC-1 in baculovirus, and we report that the recombinant product has important similarities with the MUC-1 expressed on tumors, especially in regard to its aberrant glycosylation.</p>","PeriodicalId":8980,"journal":{"name":"Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity","volume":"1 3","pages":"193-8"},"PeriodicalIF":0.0000,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity","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
Epithelial cell mucin encoded by the gene MUC-1, is expressed on several human adenocarcinomas in an aberrantly glycosylated form, and as such it has been identified as the target of human cellular as well as humoral responses. In order to harness this immunity to combat mucin-expressing tumors, various forms of this molecule, synthetic or highly purified, are being tested as possible cancer vaccines. We have expressed MUC-1 in baculovirus, and we report that the recombinant product has important similarities with the MUC-1 expressed on tumors, especially in regard to its aberrant glycosylation.