Heat Shock Protein 70 and Ki-67 Expression in Intraepithelial Neoplasm and Squamous Cell Carcinoma of the Uterine Cervix

Doh, E H; Choi, S C; Yang, H S; Bae, C S; Yoon, H W; Sim, J C; Lee, J I; Kim, J R

Abstract

Heat shock protein (HSP) expressions is upregulated in some tumor cells. Furthermore, the 70-kda HSP (HSP70) is implicated in the degree of tumor differentiation, the rate of tumor proliferation and the magnitude of the antitumor immune reponse. Accordingly, the distribution and intensity of HSP 70 expression were assessed in normal squamous epithelium, squamous metaplasia and 32 cervical intraepithelial neoplasm (CIN, 14 CIN I , II and 18 CIN III) and 18 squamous cell carcinoma (SCC) of uterine cervix with Ki-67 cell proliferation associated antigen by avidin biotin complex immunohistochemisrty. Staining intesity was recorded in scoring index. Specific staining with anti-HSP 70 antibody was exclusively confined to the cytoplasm. HSP 70 was expressed in normal squamous epithelium (66.7%). Metaplastic squamous cells were completely negative. Rate of positive cases of HSP 70 expression were 35.9% in CIN I /II, 50% in CIN III, 89% in carcinomas (100% in keratinizing, 85% in nonkeratinizing) and scoring index of HSP 70 were 0.57 in CIN I /II, 0.61 in CIN III, 1.50 in carcinomas (2.00 in keratinizing, 1.31 in nonkeratinizing). The distribution and intensity of HSP 70 expression in keratinizing SCC was greater than that in nonkeratinizing SCC, although this result just failed to reach stastistical significance. Results of staining HSP 70 were correlated with distribution and rate of Ki-67 antigen expression but there was no significant regression coefficience between these groups. The expression and intensity of HSP 70 had no overlap between CIN and SCC, which can be proposed as a useful marker for the detection likely to be at risk of progression of CIN to SCC.