Encapsulated Hsp70 decreases endotoxin-induced production of ROS and TNFα in human phagocytes

Cell Stress Chaperones. 2017 Jan;22(1):163-171. doi: 10.1007/s12192-016-0743-z. Epub 2016 Oct 26.

Abstract

Human heat shock protein Hsp70 was experimentally inserted into polyelectrolyte microcapsules. Encapsulated recombinant Hsp70 was studied in terms of its effects on neutrophil apoptosis, the production of reactive oxygen species, and the secretion of tumor necrosis factor alpha by promonocytic THP-1 cells. It was found that encapsulated Hsp70 effectively inhibits neutrophil apoptosis, unlike free exogenous protein used in solution. In THP-1 cells, encapsulated and free Hsp70 reduced LPS-induced tumor necrosis factor alpha production with a similar efficiency. Encapsulated Hsp70 reduces LPS-induced reactive oxygen species production by neutrophils in the course of its release from the microcapsules but not as much as free Hsp70. Thus, the polyelectrolyte microcapsules can be used as containers for the effective delivery of Hsp70 to neutrophils and monocytes to significantly improve the functioning of the innate immune system.

Keywords: Human neutrophils; LPS; Polyelectrolyte microcapsules; ROS; Recombinant human Hsp70; TNFα.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cells, Cultured
  • HSP70 Heat-Shock Proteins / genetics
  • HSP70 Heat-Shock Proteins / metabolism*
  • Humans
  • Lipopolysaccharides / toxicity*
  • Microscopy, Confocal
  • Monocytes / cytology
  • Monocytes / drug effects
  • Monocytes / metabolism
  • Neutrophils / cytology
  • Neutrophils / drug effects
  • Neutrophils / metabolism
  • Phagocytes / drug effects*
  • Reactive Oxygen Species / metabolism*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / isolation & purification
  • Tumor Necrosis Factor-alpha / metabolism*

Substances

  • HSP70 Heat-Shock Proteins
  • Lipopolysaccharides
  • Reactive Oxygen Species
  • Recombinant Proteins
  • Tumor Necrosis Factor-alpha