Precision Mapping of Serum MUC1 Glycopeptide eptiopes expressed by Non-Small Cell Lung Carcinoma
详细信息 查看官网全文
- 英文论文题名：Precision Mapping of Serum MUC1 Glycopeptide eptiopes expressed by Non-Small Cell Lung Carcinoma
- 论文作者：Xu Xiukun ; Pan Deng ; Li Yunsen ; Zhou Dapeng
- 英文论文作者：Xu Xiukun ; Pan Deng ; Li Yunsen ; Zhou Dapeng ; Institutes of Biology and Medical Science ; Soochow University ; Shanghai Pulmonary Hospital affiliated with Tongji University School of Medicine
- 年：2016
- 作者机构：Institutes of Biology and Medical Science,Soochow University;Shanghai Pulmonary Hospital affiliated with Tongji University School of Medicine;
- 英文论文关键词：non-small cell lung cancer ; MUC1 ; glycomics ; monoclonal antibody
- 会议召开时间：2016-11-04
- 会议录名称：第十一届全国免疫学学术大会摘要汇编
- 英文会议录名称：Abstracts of 2016 CSI Congress on Immunology
- 语种：英文
- 分类号：R734.2
- 学会代码：IGMD
- 会议名称：第十一届全国免疫学学术大会
- 会议地点：中国安徽合肥
- 主办单位：中国免疫学会
- 学会名称：中国免疫学会
- 页数：1
- 文件大小：352k
- 原文格式：D
- 会议级别：全国
摘要
Glycoproteins such as CA125 and CA153 were among first-identified biomarkers in cancer diagnosis and monitoring oftumor burden and relapse. However, glycoprotein biomarkers only have very limited value for non-small cell lung cancer(NSCLC). The aim of this study is to generate a precise map for MUC1 glycopeptides expressed by NSCLC patientswith a panel of monoclonal antibodies, and to develop a sandwich ELISA assay through capturing serum MUC1. Wefirst studied the O-glycans of banked non-small cancer cell carcinoma tissue, and identified four types of major O-glycanstructures. Focusing on 5 O-glycosylation sites of MUC1 tandem repeat, we tested 121 monoclonal antibody pairs in their binding to MUC1 secreted by NSCLC cells. A pair of monoclonal antibodies with strongest binding to all NSCLCMUC1 were selected. Banked serum samples from 198 lung cancer patients(Stages II-IV) were studied, in comparisonto 153 healthy control. Antibody pair specific for glyco-epitopes in MUC1 testing showed a sensitivity of 78.1% andspecificity of 66.2% respectively. When combined with CEA(>10 ng/ml), the sensitivity and specificity were increasedto 90.2% and 77.3% respectively. Our results indicate that secreted MUC1 glycopeptide epitopes might be a clinicallyvaluable cancer biomarker. The precision mapping of secreted MUC1 glycopeptide epitopes may lead to invention of critical technologies for early detection of NSCLC.
Glycoproteins such as CA125 and CA153 were among first-identified biomarkers in cancer diagnosis and monitoring oftumor burden and relapse. However, glycoprotein biomarkers only have very limited value for non-small cell lung cancer(NSCLC). The aim of this study is to generate a precise map for MUC1 glycopeptides expressed by NSCLC patientswith a panel of monoclonal antibodies, and to develop a sandwich ELISA assay through capturing serum MUC1. Wefirst studied the O-glycans of banked non-small cancer cell carcinoma tissue, and identified four types of major O-glycanstructures. Focusing on 5 O-glycosylation sites of MUC1 tandem repeat, we tested 121 monoclonal antibody pairs in their binding to MUC1 secreted by NSCLC cells. A pair of monoclonal antibodies with strongest binding to all NSCLCMUC1 were selected. Banked serum samples from 198 lung cancer patients(Stages II-IV) were studied, in comparisonto 153 healthy control. Antibody pair specific for glyco-epitopes in MUC1 testing showed a sensitivity of 78.1% andspecificity of 66.2% respectively. When combined with CEA(>10 ng/ml), the sensitivity and specificity were increasedto 90.2% and 77.3% respectively. Our results indicate that secreted MUC1 glycopeptide epitopes might be a clinicallyvaluable cancer biomarker. The precision mapping of secreted MUC1 glycopeptide epitopes may lead to invention of critical technologies for early detection of NSCLC.
Glycoproteins such as CA125 and CA153 were among first-identified biomarkers in cancer diagnosis and monitoring oftumor burden and relapse. However, glycoprotein biomarkers only have very limited value for non-small cell lung cancer(NSCLC). The aim of this study is to generate a precise map for MUC1 glycopeptides expressed by NSCLC patientswith a panel of monoclonal antibodies, and to develop a sandwich ELISA assay through capturing serum MUC1. Wefirst studied the O-glycans of banked non-small cancer cell carcinoma tissue, and identified four types of major O-glycanstructures. Focusing on 5 O-glycosylation sites of MUC1 tandem repeat, we tested 121 monoclonal antibody pairs in their binding to MUC1 secreted by NSCLC cells. A pair of monoclonal antibodies with strongest binding to all NSCLCMUC1 were selected. Banked serum samples from 198 lung cancer patients(Stages II-IV) were studied, in comparisonto 153 healthy control. Antibody pair specific for glyco-epitopes in MUC1 testing showed a sensitivity of 78.1% andspecificity of 66.2% respectively. When combined with CEA(>10 ng/ml), the sensitivity and specificity were increasedto 90.2% and 77.3% respectively. Our results indicate that secreted MUC1 glycopeptide epitopes might be a clinicallyvaluable cancer biomarker. The precision mapping of secreted MUC1 glycopeptide epitopes may lead to invention of critical technologies for early detection of NSCLC.
引文