The role of membrane-associated heat shock protein Hsp70 in migration of glioblastoma cell

Background . Membrane-associated heat shock protein Hsp70 (mHsp70) is selectively expressed in tu mor, but not in normal cells. The mHsp70 functions are not fully understood. Objective : to study the role of mHsp70 in glioblastoma cell migration. Design and methods. mHsp70-positive rat glioma C6 and human glioblastoma U251 and T98G cell lines were used. Each cell line was sorted into two subpopulations: with high (mHsp70+) and low (mHsp70-) protein expression. The contribution of mHsp70 to migration was as sessed using a wound-healing assay, manual single-cell tracking, and the Transwell analysis. We also exam ined the effect of Hsp70 inhibitors PES and JG-98 on cell motility. To identify potential protein partners of mHsp70 that regulate cell motility, proteomic analysis of lipid rafts of T98G cells was performed. Results . mHsp70+ subpopulations have a higher mean speed (according to manual tracking) and lead to complete wound healing in a shorter period of time compared to mHsp70-. The use of PES and JG-98 inhibitors helps to reduce the speed of movement, as well as the number of invasive cells, with the greatest effect observed for mHsp70+ subpopulations. Proteomic analysis of T98G cells lipid rafts revealed a relationship between mHsp70 and proteins involved in cytoskeleton and extracellular matrix remodeling, adhesion and migration. Conclusion . mHsp70 is involved in glioblastoma cell migration and can be used as a target for malignant neoplasm therapy.