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

JIA HongLing; LIU ChaoWu; GE Feng; XIAO ChuanLe; LU ChunHua; WANG Tong; HE QingYu

doi:10.3967/0895-3988.2011.04.014

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Volume 24 Issue 4

Aug. 2011

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Article Navigation > Biomedical and Environmental Sciences > 2011 > 24(4): 422-430

JIA HongLing, LIU ChaoWu, GE Feng, XIAO ChuanLe, LU ChunHua, WANG Tong, HE QingYu. Identification of Ubiquitinated Proteins from Human Multiple Myeloma U266 Cells by Proteomics[J]. Biomedical and Environmental Sciences, 2011, 24(4): 422-430. doi: 10.3967/0895-3988.2011.04.014

Citation:

JIA HongLing, LIU ChaoWu, GE Feng, XIAO ChuanLe, LU ChunHua, WANG Tong, HE QingYu. Identification of Ubiquitinated Proteins from Human Multiple Myeloma U266 Cells by Proteomics[J]. Biomedical and Environmental Sciences, 2011, 24(4): 422-430. doi: 10.3967/0895-3988.2011.04.014

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

doi: 10.3967/0895-3988.2011.04.014

Institute of Life and Health Engineering/National Engineering Research Center of Genetic Medicine, Jinan University, Guangzhou 510632, Guangdong, China
Guangdong Institute of Microbiology, Guangzhou 510070,Guangdong, China

Funds: the 2007 Chang-Jiang Scholars Program,National Natural Science Foundation of China(30973393 & 30400071)%"211" Projects grant (Biotechnology & Bioengineering Medicine and Biomaterial & Tissue Engineering)

Abstract

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.
- Ubiquitination,
- Multiple myeloma,
- Immunoprecipitation,
- Ubiquitinated proteins
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通讯作者: 陈斌, bchen63@163.com

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沈阳化工大学材料科学与工程学院沈阳 110142

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

doi: 10.3967/0895-3988.2011.04.014

Institute of Life and Health Engineering/National Engineering Research Center of Genetic Medicine, Jinan University, Guangzhou 510632, Guangdong, China

Guangdong Institute of Microbiology, Guangzhou 510070,Guangdong, China

Key words:

Abstract: 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.

Citation:

JIA HongLing, LIU ChaoWu, GE Feng, XIAO ChuanLe, LU ChunHua, WANG Tong, HE QingYu. Identification of Ubiquitinated Proteins from Human Multiple Myeloma U266 Cells by Proteomics[J]. Biomedical and Environmental Sciences, 2011, 24(4): 422-430. doi: 10.3967/0895-3988.2011.04.014