Scientific journal
Scientific Review. Biological science
ISSN 2500-3399
ПИ №ФС77-57454

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DEVELOPMENT OF THE METHOD FOR PURIFICATION OF HEAT SHOCK PROTEIN 90 (HSP90) FROM ANIMAL TISSUES

Snigireva A.V. 1 Vrublevskaya V.V. 1 Skarga Y.Y. 1 Evdokimovskaya Y.V. 1 Morenkov O.S. 1
1 Federal State Institution of Science Institute of Cell Biophysics Russian Academy of Sciences (142290
Heat shock protein 90 (Hsp90) is a molecular chaperone that plays an important role in functioning of cells under normal and stress conditions. Many of intracellular Hsp90 client proteins are associated with oncogenesis. In addition to intracellular Hsp90, extracellular Hsp90 that participates in the induction of antitumor immunity, stimulates migration and invasion of tumor cells is identified. Intracellular and extracellular Hsp90 are considered as perspective molecular targets for the development of antitumor drugs. Hsp90 from tumor cells have the potential as anti-tumor vaccines. Simple and efficient methods for purification of Hsp90 from animal and human cells and tissues are required to implement further investigation of Hsp90 and make the development on its basis for potential applications. This study describes a new simple and efficient method for purification of Hsp90 from tissues of various animal species, using thiophilic chromatography. The conditions for purification of Hsp90 on thiophilic gel during which the purity of Hsp90 reached up to 80 % were found. Further purification of Hsp90 by ion exchange chromatography yielded the purity of the Hsp90 more than 95 %. Hsp90 was functionally active and stimulated migration of human glioblastoma tumor cells A-172 and human fibrosarcoma cells HT1080 in vitro.