Research Article

Potential role of heat-shock proteins in giant cell tumors

Published: December 29, 2015
Genet. Mol. Res. 14 (4) : 19144-19154 DOI: https://doi.org/10.4238/2015.December.29.24
Cite this Article:
(2015). Potential role of heat-shock proteins in giant cell tumors. Genet. Mol. Res. 14(4): gmr5558. https://doi.org/10.4238/2015.December.29.24
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Abstract

We investigated the differential expression protein profile of giant cell tumors (GCTs), which can be used to monitor the tumor’s recurrence and metastasis, to provide preliminary results for further study. We also explored heat-shock protein (HSP) inhibitor that prevents tumors from recurring and migrating. A stable isotope-labeling strategy using isobaric tags for relative and absolute quantitation coupled with two-dimensional liquid chromatography tandem mass spectrometry was used to separate and identify differentially expressed proteins. A total of 467 differentially expressed proteins were identified in GCT tissues. Up to 311 proteins were upregulated, whereas 156 proteins were downregulated in GCT tissues. Three of the differentially expressed HSPs, namely HP90A, HSPB1, and HSPB2, were upregulated. The differentially expressed proteins of GCT tissues will provide a scientific foundation for tumor prognosis, and for further studies exploring HSP inhibitor to prevent tumor recurrence and migration.

We investigated the differential expression protein profile of giant cell tumors (GCTs), which can be used to monitor the tumor’s recurrence and metastasis, to provide preliminary results for further study. We also explored heat-shock protein (HSP) inhibitor that prevents tumors from recurring and migrating. A stable isotope-labeling strategy using isobaric tags for relative and absolute quantitation coupled with two-dimensional liquid chromatography tandem mass spectrometry was used to separate and identify differentially expressed proteins. A total of 467 differentially expressed proteins were identified in GCT tissues. Up to 311 proteins were upregulated, whereas 156 proteins were downregulated in GCT tissues. Three of the differentially expressed HSPs, namely HP90A, HSPB1, and HSPB2, were upregulated. The differentially expressed proteins of GCT tissues will provide a scientific foundation for tumor prognosis, and for further studies exploring HSP inhibitor to prevent tumor recurrence and migration.