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Updated: Mar 28, 2026

Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections
Published on: March 8, 2024
Influence of encapsulated heat shock protein HSP70 on the basic functional properties of blood phagocytes
O Yu Kochetkova1,2, M M Yurinskaya3, M B Evgen'ev3,4
1Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Moscow oblast, Russia. o.y.kochetkova@gmail.com.
Abstract:
Microencapsulated heat shock proteins HSP 70 were studied in terms of their effects on neutrophil apoptosis, production of reactive oxygen species, and secretion of TNF-α by human neurtrophils and monocytes. Encapsulated HSP70 inhibited neutrophil apoptosis by 65% as compared to the effect of nonencapsulated HSP70; TNF-α production by the promonocytic THP-1 cells was similarly inhibited by the non-encapsulated and encapsulated HSP70. Thus, the polyelectrolyte micromolecules can be used as containers for effective delivery of HSP70 up to neutrophils and monocytes to correct the innate immunity functions.
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