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Downregulated expression of HSP27 in human low-grade glioma tissues discovered by a quantitative proteomic analysis

Authors :
Li Ronghui
Xia Xiangying
Xiao Shiyin
Zhou Liangxue
Xu Zhizhong
Liang Shufang
Shen Guobo
Liao Ying
You Chao
Wei Yuquan
Source :
Proteome Science, Vol 8, Iss 1, p 17 (2010)
Publication Year :
2010
Publisher :
BMC, 2010.

Abstract

Abstract Background Heat shock proteins (HSPs), including mainly HSP110, HSP90, HSP70, HSP60 and small HSP families, are evolutionary conserved proteins involved in various cellular processes. Abnormal expression of HSPs has been detected in several tumor types, which indicates that specific HSPs have different prognostic significance for different tumors. In the current studies, the expression profiling of HSPs in human low-grade glioma tissues (HGTs) were investigated using a sensitive, accurate SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative proteomic strategy. Results The five HSP family members were detected and quantified in both HGTs and autologous para-cancerous brain tissues (PBTs) by the SILAC-based mass spectrometry (MS) simultaneously. HSP90 AB1, HSP A5(70 KDa), and especially HSP27 were significantly downregulated in HGTs, whereas the expression level of HSPA9 (70 KDa) was little higher in HGTs than that in PBTs. It was noted that the downregulation ratio of HSP27 was 0.48-fold in HGTs versus PBTs, which was further validated by results from RT-PCR, western blotting and immunohistochemistry. Furthermore, we detected HSP27 expression changes along with cell growth under heat shock treatment in glioma H4 cells. Conclusion The SILAC-MS technique is an applicable and efficient novel method, with a high-throughput manner, to quantitatively compare the relative expression level of HSPs in brain tumors. Different HSP family members have specific protein expression levels in human low-grade glioma discovered by SILAC-MS analysis. HSP27 expression was obviously downregulated in HGTs versus PBTs, and it exhibited temporal and spatial variation under heat shock treatment (43°C/0-3 h) in vitro. HSP27's rapid upregulation was probably correlated with the temporary resistance to heat shock in order to maintain the survival of human glioma cells.

Subjects

Subjects :
Cytology
QH573-671

Details

Language :
English
ISSN :
14775956
Volume :
8
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Proteome Science
Publication Type :
Academic Journal
Accession number :
edsdoj.83c841708545476a965f037baba09ea8
Document Type :
article
Full Text :
https://doi.org/10.1186/1477-5956-8-17