| HSPs(Heat shock proteins) are a group of proteins with important physiological functions and highly-conservative structures, which lies in all kinds of cells. The expression of heat-shock proteins(HSPs) is characteristic of all organisms in response to a variety of stresses, the response was called heat shock response(HSR).It will be largely expressed as a strategy to deal with adverse environmental changes such as ischemia,virus infections, oxidative injuries, tumors and a wide variety of other stressors. HSPs can be divided into several families including HSP100 families,HSP90 families,HSP70 families,HSP60 families, and HSPs of low molecular quanlity according molecular quality and the amino acid homogenousity. Among all the families of HSPs HSP70 is one of the mostly studied protein. It is regulated by the cell cycle in normal cells and exerts the function of "molecular chaperon".However,Hsp70 shows its excessive expression in tumor issues when stimulated by some materials such as mutant and abnormal proteins. The upregulation of HSP70 is related to the pathological classifications of cancers and the survival span with cured tumors in many malignant tumors. As for the importance of abnormal expression of HSP70 in tumor issues, on the one hand it regulates the reproduction of tumors; on the other hand, it can help tumors escape from the immune supervision. One of the most important mechanisms lies in its combination with the expreesions of some oncogenes and tumor-related proteins. It has been proven that HSP70 is combined with mutant p53 in the issues of oral cancers and ovary cancers. Thecompound of p53-HSP70 is probably involved in the access of malignance of some cells and then can be used as a factor to estimate the prognosis of corresponding cancers. In our lab, we have discovered the results that HSP70 and p53 not only upregulated in the hepatocellular carcinoma but they have a certain corelation in their expressions by immunohistochemistry, hybridization in situ and laser scan con-focal microscope(LSCM). We found that samples with p53 nuclei positive must coexist HSP70 nuclei positive, and both are expressed in the nuclei. Whether they develop a compound or not, however, it has not yet been reported. In our experiment, samples are stained by immunohistochemistry and 5 samples are selected which are both HSP70 and p53 positive to purify the whole cellular proteins. Then we first extract the proteins through immunoprecipitation, and then detect them by SDS-PAGE and western blot. Furthermore, 2 samples are used to extract the nuclei proteins and then detected by the same methods mentioned above. It indicates that there are p53 proteins in the samples immunoprecipitated by HSP70McAb in the extracts both from the whole cells and nucleis, and vice versa. We conclude that there exit p53-HSP70 proteins in the hepatocellular carcinoma which lie in the cell nuclears. The compound of p53-HSP70 proteins may be the basis of the regulation of p53 by HSP70. We think it important based on the experiment, on the one hand, it is the material basis of p53-HSP70 to regulate the functions of p53 in the movement of the hepatocellular carcinoma from the molecular level. On the other hand, there exits the mechanism of positive tumor immunology by p53-HSP70. It can be concluded that there will be an effective way to cure the hepatocellular carcinoma in the future through making massive proteins of p53-HSP70 by some methods such as extracted corresponding proteins directedly and expressions of mixed proteins by virtue of the combinational property of p53 with HSP70.
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