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Detection of Abundant Proteins in Multiple Myeloma Cells by Proteomics

Chun-Hua Lu1, 2#, Feng Ge1#, Zhi Liu3, Rong Li3, Chuan-Le Xiao1, Hui-Lan Zeng4, Xin-Peng Lu1 and Qing-Yu He1*

1Institute of Life and Health Engineering / National Engineering and Research Center of Genetic Medicine, Jinan University, Guangzhou 510632, China.
2College of Life Science and Technology, Guangxi University, Nanning, 530004, China.
3Department of Hematology / Oncology, Nanfang Hospital, Southern Medical University, Guangzhou, 510515, China.
4Department of Hematology, the First Affiliated Hospital, Jinan University, Guangzhou 510632, China.
#Equally contributed to this work
*Corresponding author:
Dr. Qing-Yu He, PhD,
Institute of Life and Health Engineering,
Jinan University, Guangzhou 510632, China,
Tel/Fax: +86- 20-85227039,
E-mail : tqyhe@jnu.edu.cn.
Received December 04, 2009; Accepted January 06, 2010; Published January 06, 2010
Citation: Lu CH, Ge F, Liu Z, Li R, Xiao CL, et al. (2010) Detection of Abundant Proteins in Mult iple Myeloma Cells by Proteomics. J Proteomics Bioinform 3: 005-009. doi:10.4172/jpb.1000115
 
Copyright: © 2010 Lu CH, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
 
Abstract
Abundant proteins of human multiple myeloma (MM) were globally analyzed and identified by using two- dimensional gel electrophoresis (2DE) and MALDI-TOF/TOF mass spectrometry (MS). Spots of 517 corresponding to 268 different proteins were detected on 2DE gels of protein lysate from plasma cells isolated from eight newly diagnosed MM patients. These identified proteins were classified into different categories based on their molecular functions and biological processes. The detailed experimental procedures and MS spectra of all the identified proteins have been deposited in the Proteomics Identifications Database (PRIDE) (http://www.ebi.ac.uk/pride) with Accession No. 8846 & 8847. This 2DE map of MM proteins will be an invaluable resource for further proteomics research that investigates proteomic changes associated with biomarker identification and carcinogenesis analysis of multiple myeloma.
 
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