Hsp90AB1 Protein is Overexpressed in Non-small Cell Lung Cancer Tissues ？and Associated with Poor Prognosis in Lung Adenocarcinoma Patients

Background and objective Heat shock protein 90 kDa alpha, class B member 1 (Hsp90AB1) is highly conserved ATP-dependent molecular chaperone, and over-expressed in a variety of tumor cells. Some molecules that play important roles in tumor development signaling pathways such as epidermal growth factor receptor (EGFR), human epidermal growth factor receptor-2 (HER2) are Hsp90AB1 client proteins. Hsp90AB1 interact with these client proteins and participate in a variety of pathophysiological processes of cells. The aim of this study is to detect the expression of Hsp90AB1 in non-small cell lung cancer (NSCLC) tissues, and explore its clinical significance. Methods The expression of Hsp90AB1 in 213 NSCLC tissues and 147 normal lung tissues was detected by tissue microarray and immunohistochemical staining method, and the relationship of Hsp90AB1 expression with clinicopathological parameters and prognosis of NSCLC patients were analyzed. Results The expression level of Hsp90AB1 in lung cancer tissues (positive rate of 54.0%) was significantly higher than that in normal lung tissue (positive rate of 0.0%, P<0.001). The positive expression rate of Hsp90AB1 in lung adenocarcinoma tissues (61.2%) was significantly higher than that in lung squamous cell carcinoma tissues (37.9%)(P=0.002), and its over-expression was associated with poor prognosis in lung adenocarcinoma patients (P=0.032). The expression level of Hsp90AB1 had no significant correlation with clinical stage, lymph node metastasis, pathological grade or other factors (P>0.05). Conclusion Hsp90AB1 protein was over-expressed in NSCLC tissues, and was associated with lung cancer pathological type and overall survival in lung adenocarcinoma patients.