ArticleProteome science2010
Downregulated expression of HSP27 in human low-grade glioma tissues discovered by a quantitative proteomic analysis.
Article in Proteome science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.
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Who cites it
8 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Proteomic analysis of cerebrospinal fluid: toward the identification of biomarkers for gliomas.Neurosurgical review · 2014Pooled it
- Targeting Heat Shock Proteins in Malignant Brain Tumors: From Basic Research to Clinical Trials.Cancers · 2022Review
- Cytochrome C as a potential clinical marker for diagnosis and treatment of glioma.Frontiers in oncology · 2022Article
- SAE1 promotes human glioma progression through activating AKT SUMOylation-mediated signaling pathways.Cell communication and signaling : CCS · 2019Article
- Systematic tracking of altered modules identifies the key biomarkers involved in chronic lymphocytic leukemia.Oncology letters · 2019Article
- Exosomal Chaperones and miRNAs in Gliomagenesis: State-of-Art and Theranostics Perspectives.International journal of molecular sciences · 2018Review
- Different immunohistochemical levels of Hsp60 and Hsp70 in a subset of brain tumors and putative role of Hsp60 in neuroepithelial tumorigenesis.European journal of histochemistry : EJH · 2013Article
- Comparison of the expression of 5 heat shock proteins in benign and malignant salivary gland tumor tissues.Oncology letters · 2013Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundHeat 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.
resultsThe 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.
conclusionThe 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 degrees 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.
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Registered trials
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