Àá½Ã¸¸ ±â´Ù·Á ÁÖ¼¼¿ä. ·ÎµùÁßÀÔ´Ï´Ù.
KMID : 1101420170490040460
Korean Journal of Clinical Laboratory Science
2017 Volume.49 No. 4 p.460 ~ p.469
Analysis of the Correlation between Expressions of HSP90¥á, HSP90¥â, and GRP94, and the Clinicopathologic Characteristics in Tissues of Non-Small Cell Lung Cancer Patients
Kim Mi-Kyeong

Abstract
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¥á showed higher expression in patients with no lymphovascular invasion (p=0.014). HSP90¥â 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¥á might contribute more to the carcinogenesis of NSCLC than HSP90¥â, and GRP94 and isoform selectivity should be considered when HSP90 inhibitors are studied or utilized in the treatment of NSCLC.
KEYWORD
Heat shock protein 90¥á, Heat shock protein90¥â, Glucose related protein94, Non-small cell lung cancer
FullTexts / Linksout information
Listed journal information
ÇмúÁøÈïÀç´Ü(KCI)