Email updates

Keep up to date with the latest news and content from BMC Medical Genomics and BioMed Central.

Open Access Research article

Mitochondrial proteomics of nasopharyngeal carcinoma metastasis

Jianping Liu1234, Xianquan Zhan12*, Maoyu Li12, Guoqing Li125, Pengfei Zhang1, Zhefeng Xiao12, Meiying Shao12, Fang Peng12, Rong Hu12 and Zhuchu Chen12*

Author Affiliations

1 Key Laboratory of Cancer Proteomics of Chinese Ministry of Health, Xiangya Hospital, Central South University, 87 Xiangya Road, Changsha, Hunan, 410008, P.R. China

2 Hunan Engineering Laboratory for Structural Biology and Drug Design, Xiangya Hospital, Central South University, 87 Xiangya Road, Changsha, Hunan, 410008, P.R. China

3 Cancer Research Institute, Xiangya School of Medicine, Central South University, 88 Xiangya Road, Changsha, Hunan, 410078, P.R. China

4 Bio-Analytical Chemistry Research Laboratory, Modern Analytical Testing Center, Central South University, 88 Xiangya Road, Changsha, Hunan, 410078, P.R. China

5 Department of Biology, School of Pharmacy and Life Science, University of South China, Hengyang, 421001, P.R. China

For all author emails, please log on.

BMC Medical Genomics 2012, 5:62  doi:10.1186/1755-8794-5-62

Published: 6 December 2012

Abstract

Background

Mitochondrial proteomic alterations of nasopharyngeal carcinoma metastasis remain unknown. Our purpose is to screen mitochondrial proteins for the elucidation of the molecular mechanisms of nasopharyngeal carcinoma metastasis and the discovery of metastasis-related biomarkers.

Methods

Mitochondria were isolated from nasopharyngeal carcinoma metastatic (5-8F) and nonmetastatic (6-10B) cell lines, respectively. After characterization of isolated mitochondria, mitochondrial differentially expressed proteins (DEPs) were quantified by two-dimensional difference in-gel electrophoresis (2D-DIGE), and identified by peptide mass fingerprint (PMF) and tandem mass spectrometry (MS/MS). A functional enrichment analysis and a protein-protein interaction sub-network analysis for DEPs were carried out with bioinformatics. Furthermore, siRNAs transient transfections were used to suppress expressions of some up-regulated DEPs in metastatic cells (5-8F), followed by Transwell Migration assay.

Results

Sixteen mitochondrial DEPs including PRDX3 and SOD2 were identified. Those 5-8F cells with suppression of PRDX3 showed an increased mobility potential. The functional enrichment analyses of DEPs discovered five significant biological processes including cellular response to reactive oxygen species, hydrogen peroxide metabolic process, regulation of mitochondrial membrane potential, cell redox homeostasis and oxidation reduction, and five significant molecular functions including oxidoreductase activity, caspase inhibitor activity, peroxiredoxin activity, porin activity and antioxidant activity. A protein-protein interaction sub-network of DEPs was generated with literature data. Ten mitochondrial DEPs including PRDX3, PRDX6, SOD2, ECH1, SERPINB5, COX5A, PDIA5, EIF5A, IDH3B, and PSMC4 were rationalized in the tumor-stroma co-evolution model that mitochondrial oxidative stress directly contributes to tumor metastasis.

Conclusions

Sixteen mitochondrial DEPs were identified with mass spectrometry and ten of them were rationalized in the tumor-stroma co-evolution model. Those 5-8F cells with suppression of PRDX3 showed an increased mobility potential. These data suggest that those mitochondrial DEPs are potential biomarkers for NPC metastasis, and their dysregulation would play important roles in mitochondria oxidative stress-mediated NPC metastatic process.

Keywords:
Nasopharyngeal carcinoma; Tumor metastasis; Mitochondria; Proteome; Differentially expressed proteins; Functional enrichment analysis; Literature data mining; PRDX3