Detection of Abundant Proteins in Multiple Myeloma Cells by Proteomics
- *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 : [email protected]
Received Date: December 04, 2009; Accepted Date: January 06, 2010; Published Date: January 06, 2010
Citation: Lu CH, Ge F, Liu Z, Li R, Xiao CL, et al. (2010) Detection of Abundant Proteins in Multiple 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.
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) (https://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.