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Identification of ubiquitinated proteins from human multiple myeloma U266 cells by proteomics.

AbstractOBJECTIVE:
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.
AuthorsHongLing Jia, ChaoWu Liu, Feng Ge, ChuanLe Xiao, ChunHua Lu, Tong Wang, QingYu He
JournalBiomedical and environmental sciences : BES (Biomed Environ Sci) Vol. 24 Issue 4 Pg. 422-30 (Aug 2011) ISSN: 0895-3988 [Print] China
PMID22108332 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
CopyrightCopyright © 2011 The Editorial Board of Biomedical and Environmental Sciences. Published by Elsevier B.V. All rights reserved.
Chemical References
  • Neoplasm Proteins
Topics
  • Cell Line, Tumor
  • Gene Expression Profiling
  • Gene Expression Regulation, Neoplastic (physiology)
  • Humans
  • Multiple Myeloma (metabolism)
  • Neoplasm Proteins (genetics, metabolism)
  • Proteomics (methods)
  • Ubiquitination

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