Effects of the Hydrogen Sulfide Donor GYY4137 and HSP70 Protein on the Activation of SH-SY5Y Cells by Lipopolysaccharide

• Published in: Molecular biology (New York) Vol. 54; no. 6; pp. 894 - 903
• Main Authors: Yurinskaya, M. M., Garbuz, D. G., Afanasiev, V. N., Evgen’ev, M. B., Vinokurov, M. G.
• Format: Journal Article
• Language: English
• Published: Moscow Pleiades Publishing 01.11.2020; Springer Nature B.V
• Subjects: Biochemistry; Biomedical and Life Sciences; Caveolin; Cell activation; Clathrin; Endocytosis; Heat shock proteins; Hsp70 protein; Human Genetics; Hydrogen; Hydrogen sulfide; IL-1β; Inflammation; Interleukin 6; Life Sciences; Lipopolysaccharides; Molecular Cell Biology; Neuroblastoma cells; Nitric oxide; Pinocytosis; Proteins; Reactive oxygen species; Tubulin; Tumor necrosis factor-α; GYY4137; SH-SY5Y; NO; Hsp70; reactive oxygen species; endocytosis; lipopolysaccharide
• ISSN: 0026-8933; 1608-3245
• DOI: 10.1134/S002689332006014X

The effects of exogenous recombinant human heat shock protein Hsp70 and hydrogen sulfide donor GYY4137 on the mechanisms of endocytosis of lipopolysaccharide (LPS) by human neuroblastoma cells SH-SY5Y were studied. Hsp70 and GYY4137 have been shown to significantly reduce LPS-induced production of inflammatory mediators by SH-SY5Y cells, including reactive oxygen species, nitric oxide, TNFα, IL-1β, and IL-6. Both the recombinant protein Hsp70 and the hydrogen sulfide donor GYY4137 exhibited significant protective effects; however, the combined use of these agents did not lead to a cumulative effect. It has been shown that pinocytosis, as well as clathrin-, caveolin-, tubulin- and receptor-dependent endocytosis were involved in protecting the cells by both the hydrogen sulfide donor and Hsp70 from LPS-induced production of reactive oxygen species and NO.