Dyregulation of chaperone proteins Hsp27, Hsp70 and Grp78 in hepatocellular carcinoma (Abstract)

Abstract

The purpose of this study is to establish differential protein expression profiles between hepatocellular carcinoma (HCC) and normal liver tissues by 2-D gel electrophoresis and MALDI-TOF. We aim to identify potentially useful tumor-associated markers that are dysregulated in HCC specimens. Fifty-two HCC surgical specimens and paired peritumor tissues were collected from patients underwent hepatectomy at Queen Mary Hospital, Pokfulam, Hong Kong, with approved protocol from the Institutional Ethics Committee. Cellular proteins were fractionated by differential extraction buffer system, and subjected to two-dimensional gel electrophoresis followed by MALDI-ToF analysis. Three chaperone heat shock proteins Hsp70, Hsp27 and GRP78 were found significantly dysregulated in 52 pairs of HCC tissues by proteomic analysis. These chaperon proteins are believed to play important roles in protein folding, transport and assembly as well as anti-apoptotic pathways in hepatocarcinogenesis. One-way ANOVA was used for statistical analysis, and p < 0.05 considered to be significant. Over expression of the chaperone proteins were confirmed by western blot. Clinical correlation of these chaperone proteins indicated their potential pathogenic roles in advanced tumor staging and metastasis, hinting for poor prognosis of patients with HCC. Supported by grants from the Research Grants Council of Hong Kong: HKU7320/02M; N_HKU718/03.