Analysis of the Correlation between Expressions of HSP90α, HSP90β, and GRP94, and the Clinicopathologic Characteristics in Tissues of Non-Small Cell Lung Cancer Patients

분석 김미경 김해대학교 임상병리과 Heat shock proteins (HSPs) are induced as a self-defense mechanism of cells when exposed to various external stresses, such as high fever, infection, free radicals, and heavy metals. They affect the prognosis in the process of tumor formation. HSP is classified into four families: HSP27, HSP60, HSP90, and HSP100, depending on molecular weight. Heat shock protein 90 (HSP90), a molecular chaperone, plays an important role in the cellular protection against various stressful stimuli and in the regulation of cell cycle progression and apoptosis. In the present study, we assessed the differential expression of HSP90 family proteins in non-small cell lung cancer (NSCLC), and the correlation of their expression levels with clinicopathologic factors and patient survival rates. The result of this study can be summarized as follows; HSP90  showed higher expression in patients with no lymphovascular invasion (p=0.014). HSP90  showed a higher expression of squamous cell carcinoma (p=0.003), and an over expression of glucose-related protein (GRP94) was significantly associated with poor differentiation (p=0.048). However, none of the HSP90 proteins showed a significant association with the survival status in patients with NSCLC. This study also indicates that HSP90  might contribute more to the carcinogenesis of NSCLC than HSP90  , and GRP94 and isoform selectivity should be considered when HSP90 inhibitors are