Cited by 36

The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.

Role of Glutaredoxin-1 and Glutathionylation in Cardiovascular Diseases

Burns, Mannix, Rizvi, Syed Husain Mustafa, Tsukahara, Yuko, Pimentel, David R., Luptak, Ivan, Hamburg, Naomi M., Matsui, Reiko, Bachschmid, Markus M.·2020·International Journal of Molecular Sciences

Abstract

Cardiovascular diseases are the leading cause of death worldwide, and as rates continue to increase, discovering mechanisms and therapeutic targets become increasingly important. An underlying cause of most cardiovascular diseases is believed to be excess reactive oxygen or nitrogen species. Glutathione, the most abundant cellular antioxidant, plays an important role in the body’s reaction to oxidative stress by forming reversible disulfide bridges with a variety of proteins, termed glutathionylation (GSylation). GSylation can alter the activity, function, and structure of proteins, making it a major regulator of cellular processes. Glutathione-protein mixed disulfide bonds are regulated by glutaredoxins (Glrxs), thioltransferase members of the thioredoxin family. Glrxs reduce GSylated proteins and make them available for another redox signaling cycle. Glrxs and GSylation play an important role in cardiovascular diseases, such as myocardial ischemia and reperfusion, cardiac hypertrophy, peripheral arterial disease, and atherosclerosis. This review primarily concerns the role of GSylation and Glrxs, particularly glutaredoxin-1 (Glrx), in cardiovascular diseases and the potential of Glrx as therapeutic agents.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/ijms21186803

Cites

9 of 9 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 125

  1. Agha, 2017, The rising prevalence of obesity, Int. J. Surg. Oncol., 2, e17, 10.1097/IJ9.0000000000000017 · DOI
  2. Sturm, 2013, Morbid obesity rates continue to rise rapidly in the United States, Int. J. Obes., 37, 889, 10.1038/ijo.2012.159 · DOI
  3. Pagidipati, 2013, Estimating Deaths from Cardiovascular Disease: A Review of Global Methodologies of Mortality Measurement, Circulation, 127, 749, 10.1161/CIRCULATIONAHA.112.128413 · DOI
  4. 2014, Oxidative Stress in Cardiovascular Disease, Int. J. Mol. Sci., 15, 6002, 10.3390/ijms15046002 · DOI
  5. Elahi, 2009, Oxidative Stress as a Mediator of Cardiovascular Disease, Oxidative Med. Cell. Longev., 2, 259, 10.4161/oxim.2.5.9441 · DOI
  6. Mashamaite, 2015, The glutaredoxin mono- and di-thiol mechanisms for deglutathionylation are functionally equivalent: Implications for redox systems biology, Biosci. Rep., 35, e00173, 10.1042/BSR20140157 · DOI
  7. Miller, 2016, Upregulation of Glutaredoxin-1 Activates Microglia and Promotes Neurodegeneration: Implications for Parkinson’s Disease, Antioxid. Redox Signal., 25, 967, 10.1089/ars.2015.6598 · DOI
  8. Kenchappa, 2004, Estrogen and neuroprotection: Higher constitutive expression of glutaredoxin in female mice offers protection against MPTP-mediated neurodegeneration, FASEB J., 18, 1102, 10.1096/fj.03-1075fje · DOI
  9. Durgadoss, 2012, Redox modification of Akt mediated by the dopaminergic neurotoxin MPTP, in mouse midbrain, leads to down-regulation of pAkt, FASEB J., 26, 1473, 10.1096/fj.11-194100 · DOI
  10. Lou, 2003, Redox regulation in the lens, Prog. Retin. Eye Res., 22, 657, 10.1016/S1350-9462(03)00050-8 · DOI
  11. Liu, 2015, Glutaredoxin 1 (Grx1) Protects Human Retinal Pigment Epithelial Cells From Oxidative Damage by Preventing AKT Glutathionylation, Investig. Ophthalmol. Vis. Sci., 56, 2821, 10.1167/iovs.14-15876 · DOI
  12. Shelton, 2007, Glutaredoxin regulates nuclear factor kappa-B and intercellular adhesion molecule in Müller cells: Model of diabetic retinopathy, J. Biol. Chem., 282, 12467, 10.1074/jbc.M610863200 · DOI
  13. Shao, 2014, A redox-resistant sirtuin-1 mutant protects against hepatic metabolic and oxidant stress, J. Biol. Chem., 289, 7293, 10.1074/jbc.M113.520403 · DOI
  14. Zee, 2010, Redox regulation of sirtuin-1 by S-glutathiolation, Antioxid. Redox Signal., 13, 1023, 10.1089/ars.2010.3251 · DOI
  15. Shao, 2017, Glutaredoxin-1 Deficiency Causes Fatty Liver and Dyslipidemia by Inhibiting Sirtuin-1, Antioxid. Redox Signal., 27, 313, 10.1089/ars.2016.6716 · DOI
  16. Anathy, 2018, Reducing protein oxidation reverses lung fibrosis, Nat. Med., 24, 1128, 10.1038/s41591-018-0090-y · DOI
  17. Anathy, 2014, Glutaredoxin-1 attenuates S-glutathionylation of the death receptor fas and decreases resolution of Pseudomonas aeruginosa pneumonia, Am. J. Respir. Crit. Care Med., 189, 463, 10.1164/rccm.201310-1905OC · DOI
  18. Lekli, 2010, Functional recovery of diabetic mouse hearts by glutaredoxin-1 gene therapy: Role of Akt-FoxO-signaling network, Gene Ther., 17, 478, 10.1038/gt.2010.9 · DOI
  19. Inadomi, 2012, Overexpression of glutaredoxin protects cardiomyocytes against nitric oxide-induced apoptosis with suppressing the S-nitrosylation of proteins and nuclear translocation of GAPDH, Biochem. Biophys. Res. Commun., 425, 656, 10.1016/j.bbrc.2012.07.118 · DOI
  20. Matsui, 2017, Redox regulation of ischemic limb neovascularization—What we have learned from animal studies, Redox Biol., 12, 1011, 10.1016/j.redox.2017.04.040 · DOI
  21. Watanabe, 2016, Glutathione adducts induced by ischemia and deletion of glutaredoxin-1 stabilize HIF-1α and improve limb revascularization, Proc. Natl. Acad. Sci. USA, 113, 6011, 10.1073/pnas.1524198113 · DOI
  22. Murdoch, 2014, Glutaredoxin-1 up-regulation induces soluble vascular endothelial growth factor receptor 1, attenuating post-ischemia limb revascularization, J. Biol. Chem., 289, 8633, 10.1074/jbc.M113.517219 · DOI
  23. Meister, 1988, Glutathione metabolism and its selective modification, J. Biol. Chem., 263, 17205, 10.1016/S0021-9258(19)77815-6 · DOI
  24. Lu, 2009, Regulation of glutathione synthesis, Mol. Asp. Med., 30, 42, 10.1016/j.mam.2008.05.005 · DOI
  25. Halliwell, B., and Gutteridge, J.M.C. (2015). Free Radicals in Biology and Medicine, Oxford University Press. · DOI · Paper page
  26. Meister, 1992, Biosynthesis and functions of glutathione, an essential biofactor, J. Nutr. Sci. Vitaminol., 38, 1, 10.3177/jnsv.38.Special_1 · DOI
  27. Dagnell, 2019, Bicarbonate is essential for protein-tyrosine phosphatase 1B (PTP1B) oxidation and cellular signaling through EGF-triggered phosphorylation cascades, J. Biol. Chem., 294, 12330, 10.1074/jbc.RA119.009001 · DOI
  28. Bergman, 1994, S-thiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment, Eur. J. Biochem., 221, 1033, 10.1111/j.1432-1033.1994.tb18821.x · DOI
  29. Niture, 2005, S-thiolation mimicry: Quantitative and kinetic analysis of redox status of protein cysteines by glutathione-affinity chromatography, Arch. Biochem. Biophys., 444, 174, 10.1016/j.abb.2005.10.013 · DOI
  30. Coles, 2009, S-Nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and S-thiolation, Biochemistry, 48, 645, 10.1021/bi801805h · DOI
  31. Mohr, 1999, Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase, J. Biol. Chem., 274, 9427, 10.1074/jbc.274.14.9427 · DOI
  32. Giustarini, 2005, S-nitrosation versus S-glutathionylation of protein sulfhydryl groups by S-nitrosoglutathione, Antioxid. Redox Signal., 7, 930, 10.1089/ars.2005.7.930 · DOI
  33. Sies, 1997, Oxidative stress: Oxidants and antioxidants, Exp. Physiol., 82, 291, 10.1113/expphysiol.1997.sp004024 · DOI
  34. Valko, 2007, Free radicals and antioxidants in normal physiological functions and human disease, Int. J. Biochem. Cell Biol., 39, 44, 10.1016/j.biocel.2006.07.001 · DOI · Paper page
  35. Di Meo, S., Reed, T.T., Venditti, P., and Victor, V.M. (2016). Role of ROS and RNS Sources in Physiological and Pathological Conditions. Oxid. Med. Cell. Longev., 2016. · DOI
  36. Tousoulis, 2012, The Role of Nitric Oxide on Endothelial Function, Curr. Vasc. Pharmacol., 10, 4, 10.2174/157016112798829760 · DOI · Paper page
  37. Donald, 1996, The vascular biology of nitric oxide and its role in atherogenesis, Annu. Rev. Med., 47, 365, 10.1146/annurev.med.47.1.365 · DOI
  38. Li, 2000, The role of cellular glutathione peroxidase redox regulation in the suppression of tumor cell growth by manganese superoxide dismutase, Cancer Res., 60, 3927
  39. Ho, 2007, Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia, Free Radic. Biol. Med., 43, 1299, 10.1016/j.freeradbiomed.2007.07.025 · DOI
  40. Schafer, 2001, Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple, Free Radic. Biol. Med., 30, 1191, 10.1016/S0891-5849(01)00480-4 · DOI · Paper page
  41. Rebrin, 2004, Comparison of thiol redox state of mitochondria and homogenates of various tissues between two strains of mice with different longevities, Exp. Gerontol., 39, 1513, 10.1016/j.exger.2004.08.014 · DOI
  42. Zitka, 2012, Redox status expressed as GSH:GSSG ratio as a marker for oxidative stress in paediatric tumour patients, Oncol. Lett., 4, 1247, 10.3892/ol.2012.931 · DOI · Paper page
  43. Rossi, 2007, S-glutathionylation in protein redox regulation, Free Radic. Biol. Med., 43, 883, 10.1016/j.freeradbiomed.2007.06.014 · DOI
  44. Ravichandran, 1994, S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes, J. Biol. Chem., 269, 25010, 10.1016/S0021-9258(17)31491-6 · DOI
  45. Fratelli, 2002, Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes, Proc. Natl. Acad. Sci. USA, 99, 3505, 10.1073/pnas.052592699 · DOI
  46. Xiong, 2011, S-glutathionylation: From molecular mechanisms to health outcomes, Antioxid. Redox Signal., 15, 233, 10.1089/ars.2010.3540 · DOI · Paper page
  47. Pastore, 2013, Protein glutathionylation in cardiovascular diseases, Int. J. Mol. Sci., 14, 20845, 10.3390/ijms141020845 · DOI
  48. VanHecke, 2019, Proteomic Identification of Protein Glutathionylation in Cardiomyocytes, J. Proteome Res., 18, 1806, 10.1021/acs.jproteome.8b00986 · DOI
  49. Lillig, 2008, Glutaredoxin systems, Biochim. Biophys. Acta, 1780, 1304, 10.1016/j.bbagen.2008.06.003 · DOI
  50. Eklund, 1984, Conformational and functional similarities between glutaredoxin and thioredoxins, EMBO J., 3, 1443, 10.1002/j.1460-2075.1984.tb01994.x · DOI
  51. Mieyal, 2008, Molecular mechanisms and clinical implications of reversible protein S-glutathionylation, Antioxid. Redox Signal., 10, 1941, 10.1089/ars.2008.2089 · DOI · Paper page
  52. Cheng, 2011, A mammalian monothiol glutaredoxin, Grx3, is critical for cell cycle progression during embryogenesis, FEBS J., 278, 2525, 10.1111/j.1742-4658.2011.08178.x · DOI
  53. Sagemark, 2007, Redox properties and evolution of human glutaredoxins, Proteins Struct. Funct. Bioinform., 68, 879, 10.1002/prot.21416 · DOI
  54. Herrero, 2007, Monothiol glutaredoxins: A common domain for multiple functions, Cell. Mol. Life Sci., 64, 1518, 10.1007/s00018-007-6554-8 · DOI
  55. Pimentel, 2006, Strain-stimulated hypertrophy in cardiac myocytes is mediated by reactive oxygen species-dependent Ras S-glutathiolation, J. Mol. Cell. Cardiol., 41, 613, 10.1016/j.yjmcc.2006.05.009 · DOI
  56. Han, 2016, The redox mechanism for vascular barrier dysfunction associated with metabolic disorders: Glutathionylation of Rac1 in endothelial cells, Redox Biol., 9, 306, 10.1016/j.redox.2016.09.003 · DOI
  57. Wang, 2007, Glutaredoxin Mediates Akt and eNOS Activation by Flow in a Glutathione Reductase-Dependent Manner, Arterioscler. Thromb. Vasc. Biol., 27, 1283, 10.1161/ATVBAHA.107.144659 · DOI · Paper page
  58. Mailloux, 2014, Glutaredoxin-2 is required to control oxidative phosphorylation in cardiac muscle by mediating deglutathionylation reactions, J. Biol. Chem., 289, 14812, 10.1074/jbc.M114.550574 · DOI
  59. Kanaan, 2018, Glutaredoxin-2 controls cardiac mitochondrial dynamics and energetics in mice, and protects against human cardiac pathologies, Redox Biol., 14, 509, 10.1016/j.redox.2017.10.019 · DOI
  60. Donelson, 2019, Cardiac-specific ablation of glutaredoxin 3 leads to cardiac hypertrophy and heart failure, Physiol. Rep., 7, e14071, 10.14814/phy2.14071 · DOI
  61. Frey, 2016, A Glutaredoxin·BolA Complex Serves as an Iron-Sulfur Cluster Chaperone for the Cytosolic Cluster Assembly Machinery, J. Biol. Chem., 291, 22344, 10.1074/jbc.M116.744946 · DOI
  62. Johansson, 2011, The crystal structure of human GLRX5: Iron-sulfur cluster co-ordination, tetrameric assembly and monomer activity, Biochem. J., 433, 303, 10.1042/BJ20101286 · DOI
  63. Haunhorst, 2010, Characterization of the human monothiol glutaredoxin 3 (PICOT) as iron–sulfur protein, Biochem. Biophys. Res. Commun., 394, 372, 10.1016/j.bbrc.2010.03.016 · DOI
  64. Ye, 2010, Human Iron−Sulfur Cluster Assembly, Cellular Iron Homeostasis, and Disease, Biochemistry, 49, 4945, 10.1021/bi1004798 · DOI
  65. Rouault, 2012, Biogenesis of iron-sulfur clusters in mammalian cells: New insights and relevance to human disease, Dis. Model. Mech., 5, 155, 10.1242/dmm.009019 · DOI
  66. Matsui, 2020, Redox Regulation via Glutaredoxin-1 and Protein S-Glutathionylation, Antioxid. Redox Signal., 32, 677, 10.1089/ars.2019.7963 · DOI
  67. Pai, 2007, What is the functional significance of the unique location of glutaredoxin 1 (GRx1) in the intermembrane space of mitochondria?, Antioxid. Redox Signal., 9, 2027, 10.1089/ars.2007.1642 · DOI
  68. Lind, 1998, Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: Catalysis by glutaredoxin, Biochem. Biophys. Res. Commun., 247, 481, 10.1006/bbrc.1998.8695 · DOI
  69. Klatt, 2001, Glutathionylation of the p50 subunit of NF-kappaB: A mechanism for redox-induced inhibition of DNA binding, Biochemistry, 40, 14134, 10.1021/bi011459o · DOI
  70. Barrett, 1999, Regulation of PTP1B via glutathionylation of the active site cysteine 215, Biochemistry, 38, 6699, 10.1021/bi990240v · DOI
  71. Klatt, 1999, Redox regulation of c-Jun DNA binding by reversible S-glutathiolation, FASEB J., 13, 1481, 10.1096/fasebj.13.12.1481 · DOI
  72. Reddy, 2000, Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue, Biochem. J., 347, 821, 10.1042/bj3470821 · DOI
  73. Wang, 2001, Reversible glutathionylation regulates actin polymerization in A431 cells, J. Biol. Chem., 276, 47763, 10.1074/jbc.C100415200 · DOI
  74. Davis, 1997, Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro, J. Biol. Chem., 272, 25935, 10.1074/jbc.272.41.25935 · DOI
  75. Murata, 2003, Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt, J. Biol. Chem., 278, 50226, 10.1074/jbc.M310171200 · DOI
  76. Adachi, 2004, S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide, Nat. Med., 10, 1200, 10.1038/nm1119 · DOI
  77. Eaton, 2002, Glyceraldehyde phosphate dehydrogenase oxidation during cardiac ischemia and reperfusion, J. Mol. Cell. Cardiol., 34, 1549, 10.1006/jmcc.2002.2108 · DOI
  78. Gallogly, 2009, Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation, Antioxid. Redox Signal., 11, 1059, 10.1089/ars.2008.2291 · DOI
  79. Anathy, 2009, Redox amplification of apoptosis by caspase-dependent cleavage of glutaredoxin 1 and S-glutathionylation of Fas, J. Cell Biol., 184, 241, 10.1083/jcb.200807019 · DOI
  80. Song, 2002, Role of glutaredoxin in metabolic oxidative stress. Glutaredoxin as a sensor of oxidative stress mediated by H2O2, J. Biol. Chem., 277, 46566, 10.1074/jbc.M206826200 · DOI
  81. Song, 2003, Differential role of glutaredoxin and thioredoxin in metabolic oxidative stress-induced activation of apoptosis signal-regulating kinase 1, Biochem. J., 373, 845, 10.1042/bj20030275 · DOI
  82. Adluri, R.S., Thirunavukkarasu, M., Zhan, L., Dunna, N.R., Akita, Y., Selvaraju, V., Otani, H., Sanchez, J.A., Ho, Y.-S., and Maulik, N. (2012). Glutaredoxin-1 overexpression enhances neovascularization and diminishes ventricular remodeling in chronic myocardial infarction. PLoS ONE, 7. · DOI
  83. Chen, 2006, Decline of contractility during ischemia-reperfusion injury: Actin glutathionylation and its effect on allosteric interaction with tropomyosin, Am. J. Physiol. Cell Physiol., 290, C719, 10.1152/ajpcell.00419.2005 · DOI
  84. Rizvi, 2019, S-glutathionylation of Glyceraldehyde 3-Phosphate Dehydrogenase Regulates Sirtuin-1 Function through Trans-glutathionylation: Implication of Glutaredoxin-1, Free Radic. Biol. Med., 145, S37, 10.1016/j.freeradbiomed.2019.10.094 · DOI
  85. Travasso, 2017, Localized redox relays as a privileged mode of cytoplasmic hydrogen peroxide signaling, Redox Biol., 12, 233, 10.1016/j.redox.2017.01.003 · DOI
  86. Petrushanko, 2012, S-Glutathionylation of the Na,K-ATPase Catalytic α Subunit Is a Determinant of the Enzyme Redox Sensitivity, J. Biol. Chem., 287, 32195, 10.1074/jbc.M112.391094 · DOI
  87. Poluektov, 2019, Glutathione-related substances maintain cardiomyocyte contractile function in hypoxic conditions, Sci. Rep., 9, 4872, 10.1038/s41598-019-41266-2 · DOI
  88. Zweier, 2011, S-glutathionylation reshapes our understanding of endothelial nitric oxide synthase uncoupling and nitric oxide/reactive oxygen species-mediated signaling, Antioxid. Redox Signal., 14, 1769, 10.1089/ars.2011.3904 · DOI
  89. Rochette, 2013, Nitric oxide synthase inhibition and oxidative stress in cardiovascular diseases: Possible therapeutic targets?, Pharmacol. Ther., 140, 239, 10.1016/j.pharmthera.2013.07.004 · DOI · Paper page
  90. Evangelista, 2012, Redox regulation of SERCA2 is required for vascular endothelial growth factor-induced signaling and endothelial cell migration, Antioxid. Redox Signal., 17, 1099, 10.1089/ars.2011.4022 · DOI
  91. Ying, 2008, Cysteine-674 oxidation and degradation of sarcoplasmic reticulum Ca(2+) ATPase in diabetic pig aorta, Free Radic. Biol. Med., 45, 756, 10.1016/j.freeradbiomed.2008.05.029 · DOI
  92. Berenji, 2005, Does load-induced ventricular hypertrophy progress to systolic heart failure?, Am. J. Physiol. Heart Circ. Physiol., 289, H8, 10.1152/ajpheart.01303.2004 · DOI
  93. Haider, 1998, Increased left ventricular mass and hypertrophy are associated with increased risk for sudden death, J. Am. Coll. Cardiol., 32, 1454, 10.1016/S0735-1097(98)00407-0 · DOI
  94. Heineke, 2006, Regulation of cardiac hypertrophy by intracellular signalling pathways, Nat. Rev. Mol. Cell Biol., 7, 589, 10.1038/nrm1983 · DOI
  95. Bachschmid, 2010, Attenuated cardiovascular hypertrophy and oxidant generation in response to angiotensin II infusion in glutaredoxin-1 knockout mice, Free Radic. Biol. Med., 49, 1221, 10.1016/j.freeradbiomed.2010.07.005 · DOI
  96. Jeong, 2008, PICOT Attenuates Cardiac Hypertrophy by Disrupting Calcineurin–NFAT Signaling, Circ. Res., 102, 711, 10.1161/CIRCRESAHA.107.165985 · DOI
  97. Lusis, 2000, Atherosclerosis, Nature, 407, 233, 10.1038/35025203 · DOI
  98. Ross, 1976, Hyperlipidemia and atherosclerosis, Science, 193, 1094, 10.1126/science.822515 · DOI
  99. Wouters, 2005, Understanding hyperlipidemia and atherosclerosis: Lessons from genetically modified apoe and ldlr mice, Clin. Chem. Lab. Med., 43, 470, 10.1515/CCLM.2005.085 · DOI · Paper page
  100. Griendling, 2003, Oxidative stress and cardiovascular injury: Part II: Animal and human studies, Circulation, 108, 2034, 10.1161/01.CIR.0000093661.90582.c4 · DOI
  101. Fukai, 1998, Vascular expression of extracellular superoxide dismutase in atherosclerosis, J. Clin. Investig., 101, 2101, 10.1172/JCI2105 · DOI
  102. Shukla, 2014, FoxO proteins’ nuclear retention and BH3-only protein Bim induction evoke mitochondrial dysfunction-mediated apoptosis in berberine-treated HepG2 cells, Free Radic. Biol. Med., 76, 185, 10.1016/j.freeradbiomed.2014.07.039 · DOI
  103. Lei, 2003, JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis, Proc. Natl. Acad. Sci. USA, 100, 2432, 10.1073/pnas.0438011100 · DOI · Paper page
  104. Nigro, 2011, Flow shear stress and atherosclerosis: A matter of site specificity, Antioxid. Redox Signal., 15, 1405, 10.1089/ars.2010.3679 · DOI
  105. Li, 2017, Glutaredoxin 1 mediates the protective effect of steady laminar flow on endothelial cells against oxidative stress-induced apoptosis via inhibiting Bim, Sci. Rep., 7, 15539, 10.1038/s41598-017-15672-3 · DOI
  106. Piemonte, 2008, Protein glutathionylation increases in the liver of patients with non-alcoholic fatty liver disease, J. Gastroenterol. Hepatol., 23, e457, 10.1111/j.1440-1746.2007.05070.x · DOI
  107. Watanabe, 2020, Protein S-glutathionylation stimulate adipogenesis by stabilizing C/EBPβ in 3T3L1 cells, FASEB J., 34, 5827, 10.1096/fj.201902575R · DOI
  108. Mylonis, I., Simos, G., and Paraskeva, E. (2019). Hypoxia-Inducible Factors and the Regulation of Lipid Metabolism. Cells, 8. · DOI · Paper page
  109. Ban, 2014, Regulation of obesity and insulin resistance by hypoxia-inducible factors, Hypoxia (Auckl.), 2, 171
  110. Krishnan, 2009, Activation of a HIF1alpha-PPARgamma axis underlies the integration of glycolytic and lipid anabolic pathways in pathologic cardiac hypertrophy, Cell Metab., 9, 512, 10.1016/j.cmet.2009.05.005 · DOI
  111. Reinbothe, 2009, Glutaredoxin-1 mediates NADPH-dependent stimulation of calcium-dependent insulin secretion, Mol. Endocrinol., 23, 893, 10.1210/me.2008-0306 · DOI
  112. Klaus, A., Zorman, S., Berthier, A., Polge, C., Ramirez, S., Michelland, S., Sève, M., Vertommen, D., Rider, M., and Lentze, N. (2013). Glutathione S-transferases interact with AMP-activated protein kinase: Evidence for S-glutathionylation and activation in vitro. PLoS ONE, 8. · DOI
  113. Velu, 2007, Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress, Biochemistry, 46, 7765, 10.1021/bi700425y · DOI
  114. Chen, 2019, Cardiac Specific Knockout of p53 Decreases ER Stress-Induced Mitochondrial Damage, Front. Cardiovasc. Med., 6, 10, 10.3389/fcvm.2019.00010 · DOI
  115. Wohua, 2019, Glutaredoxin 2 (GRX2) deficiency exacerbates high fat diet (HFD)-induced insulin resistance, inflammation and mitochondrial dysfunction in brain injury: A mechanism involving GSK-3β, Biomed. Pharmacother., 118, 108940, 10.1016/j.biopha.2019.108940 · DOI
  116. Young, 2019, Deletion of the Glutaredoxin-2 Gene Protects Mice from Diet-Induced Weight Gain, Which Correlates with Increased Mitochondrial Respiration and Proton Leaks in Skeletal Muscle, Antioxid. Redox Signal., 31, 1272, 10.1089/ars.2018.7715 · DOI
  117. Shimizu, 2004, Relationship Between Plasma Glutathione Levels and Cardiovascular Disease in a Defined Population, Stroke, 35, 2072, 10.1161/01.STR.0000138022.86509.2d · DOI
  118. Lagman, M., Ly, J., Saing, T., Kaur Singh, M., Vera Tudela, E., Morris, D., Chi, P.-T., Ochoa, C., Sathananthan, A., and Venketaraman, V. (2015). Investigating the causes for decreased levels of glutathione in individuals with type II diabetes. PLoS ONE, 10. · DOI
  119. Damy, T., Kirsch, M., Khouzami, L., Caramelle, P., Le Corvoisier, P., Roudot-Thoraval, F., Dubois-Randé, J.-L., Hittinger, L., Pavoine, C., and Pecker, F. (2009). Glutathione deficiency in cardiac patients is related to the functional status and structural cardiac abnormalities. PLoS ONE, 4. · DOI
  120. Oliva, 2003, Antioxidant activities and oxidative stress byproducts in human hypertension, Hypertension, 41, 1096, 10.1161/01.HYP.0000068370.21009.38 · DOI
  121. Shahid, 2018, The SNP rs10911021 is associated with oxidative stress in coronary heart disease patients from Pakistan, Lipids Health Dis., 17, 6, 10.1186/s12944-017-0654-8 · DOI
  122. Okuda, 2001, Expression of glutaredoxin in human coronary arteries: Its potential role in antioxidant protection against atherosclerosis, Arterioscler. Thromb. Vasc. Biol., 21, 1483, 10.1161/hq0901.095550 · DOI
  123. Nakamura, 1998, Measurements of plasma glutaredoxin and thioredoxin in healthy volunteers and during open-heart surgery, Free Radic. Biol. Med., 24, 1176, 10.1016/S0891-5849(97)00429-2 · DOI
  124. 2019, Genome editing: A perspective on the application of CRISPR/Cas9 to study human diseases (Review), Int. J. Mol. Med., 43, 1559
  125. Ahsan, 2009, Redox regulation of cell survival by the thioredoxin superfamily: An implication of redox gene therapy in the heart, Antioxid. Redox Signal., 11, 2741, 10.1089/ars.2009.2683 · DOI

Cited by

Sorted by citations

Metadata

Authors
Burns, M., Rizvi, S. H. M., Tsukahara, Y., Pimentel, D. R., Luptak, I., Hamburg, N. M., Matsui, R., & Bachschmid, M. M.
Affiliations
  • Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine, 650 Albany St., Boston, MA 02118, USA
  • Cardiology, Whitaker Cardiovascular Institute, Boston University School of Medicine, 650 Albany St., Boston, MA 02118, USA
Venue
International Journal of Molecular Sciences
Publisher
MDPI AG
Published
2020-09-16
Volume
21
Issue
18
Pages
6803
ISSN
1422-0067
Cited by
36
References
9
Language
en
Funders
  • National Institutes of Health (R01 HL133013, R01 D K103750, R03 AG 051857, 1UL1TR001430)
  • American Heart Association (16GRNT27660006)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review