Carbon monoxide inhibits the nuclear-cytoplasmic translocation of HMGB1 in an in vitro oxidative stress injury model of mouse renal tubular epithelial cells.
- Author:
Yu JIA
1
;
Lu WANG
1
;
Guang-Yuan ZHAO
1
;
Zhi-Qiang WANG
1
;
Song CHEN
1
;
Gang CHEN
2
Author Information
1. Institute of Organ Transplantation, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, 30030, China.
2. Institute of Organ Transplantation, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, 30030, China. gchen@tjh.tjmu.edu.cn.
- Publication Type:Journal Article
- Keywords:
HMGB1 protein;
acetylation;
carbon monoxide;
epithelial cell;
oxidative stress;
renal tubules
- MeSH:
Active Transport, Cell Nucleus;
drug effects;
Animals;
Carbon Monoxide;
pharmacology;
Cell Nucleus;
metabolism;
Cells, Cultured;
Epithelial Cells;
drug effects;
metabolism;
HMGB1 Protein;
metabolism;
Kidney Tubules;
cytology;
Mice;
Organometallic Compounds;
pharmacology;
Oxidative Stress
- From:
Journal of Huazhong University of Science and Technology (Medical Sciences)
2016;36(6):791-795
- CountryChina
- Language:English
-
Abstract:
Carbon monoxide (CO), as a vital small molecule in signaling pathways, is found to be involved in ischemia-reperfusion injury (IRI) in renal transplantation. CO-releasing molecule-2 (CORM-2), a CO-releasing molecule, is a type of metal carbonyl complexes which can quickly release CO in vivo. In this study, an in vitro oxidative stress injury model was established to examine the effect of CORM-2 pretreatment on the nuclear-cytoplasmic translocation of high mobility group box 1 protein (HMGB1) in mouse primary renal proximal tubular epithelial cells (RPTECs). Immunofluorescence staining showed that HMGB1 in the medium- and CORM-2-treated groups was predominantly localized in the nucleus of the cells, whereas higher amounts of HMGB1 translocated to the cytoplasm in the HO- and inactive CORM-2 (iCORM-2)-treated groups. Western blotting of HMGB1 showed that the total amounts of cytoplasmic HMGB1 in the HO-treated (0.59±0.27) and iCORM-2-treated (0.57±0.22) groups were markedly higher than those in the medium-treated (0.19±0.05) and CORM-2-treated (0.21±0.10) groups (P<0.05). Co-immunoprecipitation showed that the levels of acetylated HMGB1 in the HO-treated (642.98±57.25) and iCORM-2-treated (342.11±131.25) groups were markedly increased as compared with the medium-treated (78.72±74.17) and CORM-2-treated (71.42±53.35) groups (P<0.05), and no significant difference was observed between the medium-treated and CORM-2-treated groups (P>0.05). In conclusion, our study demonstrated that in the in vitro oxidative stress injury model of primary RPTECs, CORM-2 can significantly inhibit the nuclear-cytoplasmic translocation of HMGB1, which is probably associated with the prevention of HMGB1 acetylation.
