Evgeniya V Kaigorodova
Tomsk Cancer Research Institute, Russian Federation
Title: The functional state of the chaperone Hsp27 as a molecular marker of lymph node metastases of breast cancer
Biography
Biography: Evgeniya V Kaigorodova
Abstract
Heat shock protein 27 kDa (Hsp27) is a chaperone of the sHsp (small heat shock protein). The common functions of sHsps are chaperone activity, inhibition of apoptosis, regulation of cell development, and cell differentiation, take part in signal transduction. Objective: To study the intracellular localization of phosphorylated features and non-phosphorylated forms of Hsp27in primary breast cancer cells and to evaluate their relationship with regional lymphatic metastasis. Material and Methods: Tumor biopsies of breast tissue were collected from 100 patients with a confirmed diagnosis of invasive carcinoma, nonspecific type, between the ages of 31-80 years. Immunohistochemistry was used to determine the intracellular localization of phosphorylated and non-phosphorylated forms of Hsp27. Results: The result of this study showed that biopsies from patients with lymph node metastasis exhibited significantly higher levels of phosphorylated forms of Hsp27 in the nucleus and cytoplasm compared with the group without lymph node metastasis. Analysis showed that the expression of phosphorylated forms of the chaperone Hsp27 correlates with the amount and percentage of lymph node metastases affected. Conclusion: The nuclear expression of phosphorylated and non-phosphorylated forms of the chaperone Hsp27 is a marker of tumor cells associated with lymphatic metastasis of breast cancer.