| Autor: |
Yurinskaya MM; Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino Scientific Center for Biological Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia., Garbuz DG; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia., Afanasiev VN; Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino Scientific Center for Biological Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia., Evgen'ev MB; Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino Scientific Center for Biological Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia.; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia.; Misha672001@yahoo.com., Vinokurov MG; Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino Scientific Center for Biological Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia. |
| Abstrakt: |
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-SY5Ywas 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. |
