Identification of Ubiquitinated Proteins from Human Multiple Myeloma U266 Cells by Proteomics

Objective To identify ubiquitinated proteins from complex human multiple myeloma （MM） U266 cells,a malignant disorder of differentiated human B cells.Methods Employing a globally proteomic strategy combining of immunoprecipitation,LC-MS/MS and SCX-LC-MS analysis to identified ubiquitination sites,wh...

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Bibliographic Details
Published in:Biomedical and environmental sciences 2011-08, Vol.24 (4), p.422-430
Main Authors: JIA, HongLing, LIU, ChaoWu, GE, Feng, XIAO, ChuanLe, LU, ChunHua, WANG, Tong, HE, QingYu
Format: Article
Language:English
Subjects:
B细胞
Cell Line, Tumor
Gene Expression Profiling
Gene Expression Regulation, Neoplastic - physiology
Humans
Immunoprecipitation
LC-MS/MS
Multiple myeloma
Multiple Myeloma - metabolism
Neoplasm Proteins - genetics
Neoplasm Proteins - metabolism
Proteomics - methods
Ubiquitinated proteins
Ubiquitination
分类分析
多发性骨髓瘤
泛素化
蛋白质组学
通过检测
鉴定
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Summary:Objective To identify ubiquitinated proteins from complex human multiple myeloma （MM） U266 cells,a malignant disorder of differentiated human B cells.Methods Employing a globally proteomic strategy combining of immunoprecipitation,LC-MS/MS and SCX-LC-MS analysis to identified ubiquitination sites,which were identified by detecting signature peptides containing a GG-tag （114.1 Da） and an LRGG-tag （383.2 Da）.Results In total,52 ubiquitinated proteins containing 73 ubiquitination sites of which 14 and 59 sites contained LRGG-tag and GG-tag were identified,respectively.Conclusion Classification analysis by of the proteins identified in the study based on the PANTHER showed that they were associated with multiple functional groups.This suggested the involvement of many endogenous proteins in the ubiquitination in MM.
ISSN:0895-3988
2214-0190
DOI:10.3967/0895-3988.2011.04.014