Proteomic analysis of meningiomas.

Abstract

Meningiomas represent one-third of all primary brain tumors and cause 35,000 new cases each year. Because of this high incidence, we sought to determine if there are proteomic differences between meningiomas and neighboring tissues. Two-dimensional gel electrophoresis and mass spectrometry were used to detect differentially expressed proteins in tumor samples, using arachnoid tissue as a control. Western blot analysis was used to validate the identified candidate proteins. We obtained quantitative data on 112 proteins, 17 of which were down-regulated and 26 of which were up-regulated in meningiomas relative to normal arachnoid tissue. Our analysis showed that the expression of galectin-3, vimentin, and endoplasmin was decreased significantly in meningiomas. The expression of 40S ribosomal protein S12, glutathione S-transferase P, and hypoxia up-regulated protein 1 was increased significantly (P < 0.05). The six above-mentioned differentially expressed proteins might be closely involved with the development of meningiomas. The results of this study provide basic insights into the proteome of meningiomas and provide a preliminary database for further research to enhance understanding of meningioma development.

• Authors: G Q Cui, A H Jiao, C M Xiu, Y B Wang, P Sun, L M Zhang, X G Li
• Journal: Acta neurologica Belgica (Acta Neurol Belg) Vol. 114 Issue 3 Pg. 187-94 (Sep 2014) ISSN: 2240-2993 [Electronic] Italy
• PMID: 24085542 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Topics

• Adult
• Aged
• Electrophoresis, Gel, Two-Dimensional
• Female
• Gene Expression Regulation, Neoplastic (physiology)
• Humans
• Male
• Meningeal Neoplasms (metabolism, pathology)
• Meningioma (metabolism, pathology)
• Middle Aged
• Proteomics
• Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization