PMID: 7540234Jun 1, 1995Paper

Natural state of mutant p53 protein and heat shock protein 70 in breast cancer tissues

Laboratory Investigation; a Journal of Technical Methods and Pathology
K IwayaS Hirohashi

Abstract

Nuclear accumulation of p53 protein in breast cancer cells is generally accepted as a marker for the presence of p53 gene mutation and as an indicator of poor prognosis. Mutation in the p53 gene has been shown to cause conformational change in the p53 protein, which gives rise to a complex with heat shock protein 70 (hsp70). To clarify whether the p53 protein that accumulates in the nuclei of human cancer cells is bound to hsp70 in vivo, we compared the immunohistochemical localization of both p53 and hsp70 in 65 surgically resected cases of primary breast cancer. In four cases showing both nuclear accumulation of p53 protein and mutation of the p53 gene, identified by single-strand conformation polymorphism and direct sequence analysis, the presence of the p53-hsp70 complex was examined by coimmunoprecipitation assay. In 12 human cancer cell lines showing nuclear accumulation of the p53 protein, the presence of the p53-hsp70 complex was also examined by immunoprecipitation with two anti-p53 Ab after labeling with [35S]methionine. Among the 65 cases, p53 and hsp70 immunoreaction in cancer cell nuclei was detected immunohistochemically in 16 (25%) and 23 (35%) cases, respectively. The localizations of the two proteins were signi...Continue Reading

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