Acknowledgement
This research was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (2020R1A6A1A 03044512 and 2020R1I1A3060716).
References
- Xiong Y, Uys JD, Tew KD and Townsend DM (2011) S-glutathionylation: from molecular mechanisms to health outcomes. Antioxid Redox Signal 15, 233-270 https://doi.org/10.1089/ars.2010.3540
- Mieyal JJ, Gallogly MM, Qanungo S, Sabens EA and Shelton MD (2008) Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid Redox Signal 10, 1941-1988 https://doi.org/10.1089/ars.2008.2089
- Musaogullari A and Chai YC (2020) Redox regulation by protein S-glutathionylation: from molecular mechanisms to implications in health and disease. Int J Mol Sci 21, 8113 https://doi.org/10.3390/ijms21218113
- Couvertier SM, Zhou Y and Weerapana E (2014) Chemical-proteomic strategies to investigate cysteine posttranslational modifications. Biochim Biophys Acta 1844, 2315-2330 https://doi.org/10.1016/j.bbapap.2014.09.024
- Yang J, Carroll KS and Liebler DC (2016) The expanding landscape of the thiol redox proteome. Mol Cell Proteomics 15, 1-11 https://doi.org/10.1074/mcp.O115.056051
- Zhang J, Ye ZW, Singh S, Townsend DM and Tew KD (2018) An evolving understanding of the S-glutathionylation cycle in pathways of redox regulation. Free Radic Biol Med 120, 204-216 https://doi.org/10.1016/j.freeradbiomed.2018.03.038
- Comini MA (2016) Measurement and meaning of cellular thiol: disufhide redox status. Free Radic Res 50, 246-271 https://doi.org/10.3109/10715762.2015.1110241
- Montano SJ, Lu J, Gustafsson TN and Holmgren A (2014) Activity assays of mammalian thioredoxin and thioredoxin reductase: fluorescent disulfide substrates, mechanisms, and use with tissue samples. Anal Biochem 449, 139-146 https://doi.org/10.1016/j.ab.2013.12.025
- Coppo L, Montano SJ, Padilla AC and Holmgren A (2016) Determination of glutaredoxin enzyme activity and protein S-glutathionylation using fluorescent eosin-glutathione. Anal Biochem 499, 24-33 https://doi.org/10.1016/j.ab.2016.01.012
- Velu CS, Niture SK, Doneanu CE, Pattabiraman N and Srivenugopal KS (2007) Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress. Biochemistry 46, 7765-7780 https://doi.org/10.1021/bi700425y
- Marino SM and Gladyshev VN (2010) Cysteine function governs its conservation and degeneration and restricts its utilization on protein surfaces. J Mol Biol 404, 902-916 https://doi.org/10.1016/j.jmb.2010.09.027
- Bechtel TJ and Weerapana E (2017) From structure to redox: the diverse functional roles of disulfides and implications in disease. Proteomics 17, 1600391 https://doi.org/10.1002/pmic.201600391
- Bujacz A (2012) Structures of bovine, equine and leporine serum albumin. Acta Crystallogr D Biol Crystallogr 68, 1278-1289 https://doi.org/10.1107/S0907444912027047
- Fischer G (2000) Chemical aspects of peptide bond isomerisation. Chem Soc Rev 29, 119-127 https://doi.org/10.1039/a803742f
- Xiao Z, La Fontaine S, Bush AI and Wedd AG (2019) Molecular mechanisms of glutaredoxin enzymes: versatile hubs for thiol-disulfide exchange between protein thiols and glutathione. J Mol Biol 431, 158-177 https://doi.org/10.1016/j.jmb.2018.12.006
- Castro JP, Grune T and Speckmann B (2016) The two faces of reactive oxygen species (ROS) in adipocyte function and dysfunction. Biol Chem 397, 709-724 https://doi.org/10.1515/hsz-2015-0305
- Lee H, Lee YJ, Choi H, Ko EH and Kim JW (2009) Reactive oxygen species facilitate adipocyte differentiation by accelerating mitotic clonal expansion. J Biol Chem 284, 10601-10609 https://doi.org/10.1074/jbc.M808742200
- Watanabe Y, Watanabe K, Fujioka D et al (2020) Protein S-glutathionylation stimulate adipogenesis by stabilizing C/EBPbeta in 3T3L1 cells. FASEB J 34, 5827-5837 https://doi.org/10.1096/fj.201902575r
- Qiang L and Farmer SR (2006) C/EBPalpha-dependent induction of glutathione S-transferase zeta/maleylacetoacetate isomerase (GSTzeta/MAAI) expression during the differentiation of mouse fibroblasts into adipocytes. Biochem Biophys Res Commun 340, 845-851 https://doi.org/10.1016/j.bbrc.2005.12.067
- Jowsey IR, Smith SA and Hayes JD (2003) Expression of the murine glutathione S-transferase alpha3 (GSTA3) subunit is markedly induced during adipocyte differentiation: activation of the GSTA3 gene promoter by the pro-adipogenic eicosanoid 15-deoxy-Delta12,14-prostaglandin J2. Biochem Biophys Res Commun 312, 1226-1235 https://doi.org/10.1016/j.bbrc.2003.11.068
- Byun Y, Rahman S, Hwang S, Park J, Go S and Kim J (2019) Highly sensitive and straightforward methods for the detection of cyanide using profluorescent glutathionylcobalamin. Spectrochim Acta A Mol Biomol Spectrosc 221, 117151 https://doi.org/10.1016/j.saa.2019.117151
- Raturi A and Mutus B (2007) Characterization of redox state and reductase activity of protein disulfide isomerase under different redox environments using a sensitive fluorescent assay. Free Radic Biol Med 43, 62-70 https://doi.org/10.1016/j.freeradbiomed.2007.03.025
- Go S, Park J, Rahman S, Jin J, Choi I and Kim J (2021) Adipogenic function of tetranectin mediated by enhancing mitotic clonal expansion via ERK signaling. BMB Rep 54, 374-379 https://doi.org/10.5483/BMBRep.2021.54.7.024
- Muller G, Wied S, Jung C and Over S (2008) Hydrogen peroxide-induced translocation of glycolipid-anchored (c)AMP-hydrolases to lipid droplets mediates inhibition of lipolysis in rat adipocytes. Br J Pharmacol 154, 901-913 https://doi.org/10.1038/bjp.2008.146
- Park TJ, Park A, Kim J et al (2021) Myonectin inhibits adipogenesis in 3T3-L1 preadipocytes by regulating p38 MAPK pathway. BMB Rep 54, 124-129 https://doi.org/10.5483/BMBRep.2021.54.2.262