A Survey of relation to nuclear and cytoplasmic Hsp70 and P53 expression in breast cancer

Heat shock protein 70 (hsp70) is a chaperone that binds to mutant P53 and consequently could regulate its accumulation or localization. Nuclear accumulation of P53 protein is associated with a poorer clinical outcome in breast cancer patients. The aims of this study were to determine whether hsp70 was associated with nuclear accumulation of P53 and is there any relationship between hsp70 expression and P53 with clinicopathological factors of breast cancer.Subjects and Breast tumors of patients (n=47) were sent to Shafa pathology lab in province of Khouzestan/Iran were examined by immunohistochemistry for nuclear P53 and cytoplasmic or nuclear hsp70. The paraffin sections were stained with the P53 antibody (N1581, Dako) and the hsp70 antibody (ab47454, abcam). Hsp70 and P53 were scored statistically according to the nuclear and/or cytoplasmic content and the nuclear content respectively. There was no significant association between nuclear or cytoplasmic hsp70 staining and accumulation of P53. No significance association was found between nuclear hsp70 or P53 expression and clinicopathological factors of breast tumors. There was a correlation (P<0.001) between nuclear and cytoplasmic hsp70 expression. The cytoplasmic expression of hsp70 was moderately significant in relation to histological grade of breast tumors (P=0.049). In human breast cancer, nuclear accumulation of P53 was not associated with nuclear or cytoplasmic hsp70 levels, but cytoplasmic hsp70 level is correlated with nuclear hsp70 level and is related with histological grade of breast tumors.