engleski

The role of heat shock 70 (HSP70) on cancer cell invasion-related activities.

INTRODUCTION: Breast cancer is one of the leading cause of cancer-related deaths in women worldwide and increasing rapidly in developing countries. Heat shock proteins (HSP) and heat shock factor 1 (HSF1), key factors in the heat shock response (HSR) have been implicated in the etiology of breast cancer. Available data indicate that extracellular HSP70 has a potent motogenic activity for fibroblasts, vascular and epithelial cells, and can induce angiogenesis and matrix remodelling, suggesting a possible role in cancer development and dissemination. In the present study, we investigated the potential role of HSP70 on migration and invasion capability of breast cancer cell line in vitro. MATERIAL AND METHODS: Breast cancer cell line MDA-MB-231 was used for in vitro model study to reflect in vivo immunophenotypic features of triple negative breast cancer. Stimulation with HSP70 was tested on cancer cells lines (PANC-1, MDA-MB-231, JAR) by migration and invasion assays. The gelatinase zymography method will be used to investigate the functional activity of matrix metalloproteases 2 and 9 (MMP-2 and-9) after the invasion assay. Double immunofluorescence of actin/tubulin was investigated on HSP70 stimulated breast cancer cell lines MDA-MB-231 . RESULTS: Extracellular HSP70 induce migration and invasion in a different human cancer cell line (PANC-1, MDA-MB-231, JAR) as well as remodel of extracellular matrix by MMP-2 and-9 upregulation. CONCLUSION: These results suggest that HSP70 may facilitate cancer cell extravasation and invasion, a crucial event for carcinogenesis. Modulating cancer cell migration and invasion as well as upregulation of MMP-2 and-9, HSP70 might promote and/or sustain a permissive microenvironment for cancer cell invasion and metastasis. Acknowledgement: The experiments were financed by the grant No. 19-171498

heat shock protein ; cancer cell

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