癌源性免疫球蛋白G全分子相互作用蛋白质的质谱鉴定及其功能分析

Functional analysis of cancer-derived immunoglobulin G whole molecule-interacting proteins identified by LC-MS/MS

目的鉴定与癌源性免疫球蛋白G(Ig G)全分子相互作用的蛋白质,为研究其生物功能提供重要的线索。方法分别用兔抗人Ig G全分子抗体和兔Ig G在宫颈癌细胞系He La中进行免疫共沉淀,将得到的免疫复合物经电泳分离后进行银染。经比较分析后3条差异条带切下来做质谱鉴定,质谱数据经Swiss-Prot数据库分析。最后对所得的蛋白质进行筛选和功能注释分析。结果最终得到6个可能与癌源性Ig G全分子相互作用的蛋白质。结论通过免疫共沉淀结合质谱分析的方法最终得到了6个可能与癌源性Ig G全分子相互作用的蛋白质,为其功能研究提供了重要线索。

Objective To identify cancer- derived immunoglobulin G（Ig G） whole molecule- interacting proteins to provide important clues for studying Ig G biological functions. Methods He La cell lysate was immunoprecipitated with rabbit antihuman Ig G whole molecule antibody and normal rabbit Ig G. The immunocomplex underwent sodium dodecyl sulfate polyacrylamide gel electrophoresis（SDS- PAGE） and was detected with silver staining. Three prominently enhanced bands were subjected to protein identification with liquid chromatography-tandem mass spectrometry（LC-MS/MS）, and the MS data were analyzed with Swiss- Prot database. Cancer- derived Ig G whole molecule- interacting proteins were screened and functionally annotated. Results and Conclusion We identified 6 potential cancer- derived Ig G whole molecule- interacting proteins with co-immunoprecipitation combined with LC-MS/MS, which provides valuable clues for studying the function of cancer-derived Ig G.