人类β3GnT8/β3GalT7对人4IgB7-H3蛋白的翻译后糖基化修饰作用  

Role of β3GnT8/β3GalT7 in the Process of B7-H3 Protein Post-translational Modification

作　　者：唐春花[1,2] 蒋俊华[1,2] 王建浩[1,2] 岳爱环[1,2] 徐云霞[3] 李婷[3] 周迎会[1,2] 吴士良[1,2] 

机构地区：[1]苏州大学医学部生物化学与分子生物学系,江苏苏州215123 [2]苏州大学生化工程研究所,江苏苏州215123 [3]苏州大学医学部,2005级临床1班江苏苏州215123

出　　处：《苏州大学学报（医学版）》2009年第5期834-837,847,F0003,共6页Suzhou University Journal of Medical Science

基　　金：国家自然科学基金资助项目(30771958;30670462);江苏省高校自然科学基金资助项目(06KJD310166)

摘　　要：目的探讨人类β1,3N-乙酰氨基葡萄糖基转移酶8/β3半乳糖基转移酶7(β3GnT8/β3GalT7)与人4IgB7-H3蛋白的相互作用,以期阐明该糖基转移酶对人4IgB7-H3蛋白的翻译后糖基化修饰作用。方法在线预测软件预测人4IgB7-H3蛋白氨基酸序列上潜在的糖基转移酶作用位点;免疫共沉淀探讨β3GnT8/β3GalT7与人4IgB7-H3蛋白的相互结合作用;细胞免疫荧光化学技术研究两种蛋白质在细胞内的空间定位。结果人4IgB7-H3蛋白氨基酸序列上潜在的N-糖基化位点共有8个,O-β-GlcNAc的附着位置共有18个;β3GnT8/β3GalT7与人4IgB7-H3蛋白能相互结合而被共沉淀;两种蛋白质能在人肺癌A549细胞中共定位。结论人类β3GnT8/β3GalT7可能对人4IgB7-H3蛋白有糖基化修饰作用。Objective To research the interaction between 4IgB7 -H3 and β1,3 -N-acetylglu-cosaminyltranserase 8/β3 galactosyltransferase 7 （β3GnT8/β3GalT7） and study the role of β3GnT8/ β3GalT7 in the process of B7-H3 protein post-translational modification. Methods One online soft was used to predicted glycosylation site in 4IgB7-H3 sequence. Co-immunoprecipitation was used to study the combination of 4IgB7-H3 protein and β3GnT8 /β3GalT7 protein. Cyto-immunofluorescence was used to study the co-location of these two proteins in the cells. Results There were 8 potential N-glycolation sites and 18 O-（beta）-GlcNAc sites in 4IgB7 -H3 sequence. 4IgB7 -H3 protein and β3GnT8/β3GalT7 protein were able to combine to each other and colocate in cell. Conclusion 4IgB7-H3 protein and β3GnT8/β3GalT7 may combine together and can be coimmunoprecipitated. These two proteins also colocate in human lung cancer A549 cells. Therefore,β3GnT8/β3GalT7 may modify 4IgB7-H3 protein by glycosylation.

关 键 词：β3GnT8/β3GalT7 B7-H3 免疫共沉淀 亚细胞定位 

分 类 号：R512.63[医药卫生—内科学] R978.7[医药卫生—临床医学]