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

Tytuł:: Encapsulated Hsp70 decreases endotoxin-induced production of ROS and TNFα in human phagocytes.
Autorzy:: Yurinskaya MM; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Str. 32, Moscow, Russian Federation, 119991.; Institute of Cell Biophysics, Russian Academy of Science, Institutskaya Str. 3, Pushchino, Moscow Region, Russian Federation, 142290.
Kochetkova OY; Institute of Cell Biophysics, Russian Academy of Science, Institutskaya Str. 3, Pushchino, Moscow Region, Russian Federation, 142290.; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Institutskaya Str. 3, Pushchino, Moscow Region, Russian Federation, 142290.
Shabarchina LI; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Institutskaya Str. 3, Pushchino, Moscow Region, Russian Federation, 142290.
Antonova OY; Institute of Cell Biophysics, Russian Academy of Science, Institutskaya Str. 3, Pushchino, Moscow Region, Russian Federation, 142290.
Suslikov AV; Hospital of the Pushchino Research Center, Institutskaya Str. 1, Pushchino, Moscow Region, Russian Federation, 142290.
Evgen'ev MB; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Str. 32, Moscow, Russian Federation, 119991. .; Institute of Cell Biophysics, Russian Academy of Science, Institutskaya Str. 3, Pushchino, Moscow Region, Russian Federation, 142290. .
Vinokurov MG; Institute of Cell Biophysics, Russian Academy of Science, Institutskaya Str. 3, Pushchino, Moscow Region, Russian Federation, 142290.
Źródło:: Cell stress & chaperones [Cell Stress Chaperones] 2017 Jan; Vol. 22 (1), pp. 163-171. Date of Electronic Publication: 2016 Oct 26.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Publication: 2024- : [New York] : Elsevier
Original Publication: New York : Churchill Livingstone, c1996-
MeSH Terms:: HSP70 Heat-Shock Proteins/*metabolism
Lipopolysaccharides/*toxicity
Phagocytes/*drug effects
Reactive Oxygen Species/*metabolism
Tumor Necrosis Factor-alpha/*metabolism
Cells, Cultured ; HSP70 Heat-Shock Proteins/genetics ; Humans ; Microscopy, Confocal ; Monocytes/cytology ; Monocytes/drug effects ; Monocytes/metabolism ; Neutrophils/cytology ; Neutrophils/drug effects ; Neutrophils/metabolism ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/isolation & purification
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Contributed Indexing:: Keywords: Human neutrophils; LPS; Polyelectrolyte microcapsules; ROS; Recombinant human Hsp70; TNFα
Substance Nomenclature:: 0 (HSP70 Heat-Shock Proteins)
0 (Lipopolysaccharides)
0 (Reactive Oxygen Species)
0 (Recombinant Proteins)
0 (Tumor Necrosis Factor-alpha)
Entry Date(s):: Date Created: 20161027 Date Completed: 20180117 Latest Revision: 20240209
Update Code:: 20240209
PubMed Central ID:: PMC5225061
DOI:: 10.1007/s12192-016-0743-z
PMID:: 27783274
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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.

Erratum in: Cell Stress Chaperones. 2017 Mar;22(2):317. (PMID: 28247072)

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