CoChat
Sign Up
Cited by 94Sulfur Compounds in BiologyRedox biology and oxidative stressGlutathione Transferases and Polymorphisms

Cellular Compartmentalization, Glutathione Transport and Its Relevance in Some Pathologies

Open access
Vázquez-Meza, Héctor, Vilchis-Landeros, María Magdalena, Vázquez-Carrada, Melissa, Uribe-Ramírez, Daniel, Matuz-Mares, Deyamira·2023·Antioxidants
DOI 10.3390/antiox12040834PMC PMC10135322
Open this paper in CoChat — free accountOpen PDF

Abstract

Reduced glutathione (GSH) is the most abundant non-protein endogenous thiol. It is a ubiquitous molecule produced in most organs, but its synthesis is predominantly in the liver, the tissue in charge of storing and distributing it. GSH is involved in the detoxification of free radicals, peroxides and xenobiotics (drugs, pollutants, carcinogens, etc.), protects biological membranes from lipid peroxidation, and is an important regulator of cell homeostasis, since it participates in signaling redox, regulation of the synthesis and degradation of proteins (S-glutathionylation), signal transduction, various apoptotic processes, gene expression, cell proliferation, DNA and RNA synthesis, etc. GSH transport is a vital step in cellular homeostasis supported by the liver through providing extrahepatic organs (such as the kidney, lung, intestine, and brain, among others) with the said antioxidant. The wide range of functions within the cell in which glutathione is involved shows that glutathione’s role in cellular homeostasis goes beyond being a simple antioxidant agent; therefore, the importance of this tripeptide needs to be reassessed from a broader metabolic perspective.

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/antiox12040834

Cites

8 of 8 references verified0 citation errors · 0 not checkable

Statistics

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?

  • Cultured astrocytes from murine brain contain higher specific GSH contents than cultured neurons.

    “Cultured astrocytes from murine brain have frequently been reported to contain higher specific GSH contents than cultured neurons (Dringen, Kussmaul, et al. 1999; Dringen et al. 2005; Vázquez‐Meza et al. 2023).”

    From Glutathione Metabolism of the Brain—The Role of Astrocytes (2025) · cites this paper as Vázquez‐Meza et al. 2023

    Section 2 says GSH content differs among mammalian cells, and Section 6.2 discusses neuronal and brain GSH, but neither passage compares astrocytes with neurons. Searches for astrocytes, cultured neurons, and higher GSH content found no passage reporting the claimed comparison in murine brain cultures. (LLM, conf=0.70)

    Experimental — accuracy not yet measured

Self-check

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

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

Cites

Flagged first, then by citations

Research works printed but not linked: 197

  1. [1]Jelic M.D. Mandic A.D. Maricic S.M. Srdjenovic B.U. Oxidative stress and its role in cancer J. Cancer Res. Ther. 2021 17 22 28 10.4103/jcrt.JCRT_862_16 33723127 · DOI
  2. [2]Klaunig J.E. Oxidative stress and cancer Curr. Pharm. Des. 2018 24 4771 4778 10.2174/1381612825666190215121712 30767733 · DOI
  3. [3]Radi E. Formichi P. Battisti C. Federico A. Apoptosis and oxidative stress in neurodegenerative diseases J. Alzheimers Dis. 2014 42 (Suppl. S3) S125 S152 10.3233/JAD-132738 25056458 · DOI
  4. [4]Singh A. Kukreti R. Saso L. Kukreti S. Oxidative stress: A key modulator in neurodegenerative diseases Molecules 2019 24 1583 10.3390/molecules24081583 31013638 PMC6514564 · DOI
  5. [5]Chen Z. Tian R. She Z. Cai J. Li H. Role of oxidative stress in the pathogenesis of nonalcoholic fatty liver disease Free Radic. Biol. Med. 2020 152 116 141 10.1016/j.freeradbiomed.2020.02.025 32156524 · DOI
  6. [6]Seen S. Chronic liver disease and oxidative stress—A narrative review Expert Rev. Gastroenterol. Hepatol. 2021 15 1021 1035 10.1080/17474124.2021.1949289 34176419 · DOI
  7. [7]Peoples J.N. Saraf A. Ghazal N. Pham T.T. Kwong J.Q. Mitochondrial dysfunction and oxidative stress in heart disease Exp. Mol. Med. 2019 51 1 13 10.1038/s12276-019-0355-7 PMC6923355 31857574 · DOI · Paper page
  8. [8]van der Pol A. van Gilst W.H. Voors A.A. van der Meer P. Treating oxidative stress in heart failure: Past, present and future Eur. J. Heart Fail 2019 21 425 435 10.1002/ejhf.1320 30338885 PMC6607515 · DOI
  9. [9]Ornatowski W. Lu Q. Yegambaram M. Garcia A.E. Zemskov E.A. Maltepe E. Fineman J.R. Wang T. Black S.M. Complex interplay between autophagy and oxidative stress in the development of pulmonary disease Redox Biol. 2020 36 101679 10.1016/j.redox.2020.101679 32818797 PMC7451718 · DOI
  10. [10]Wiegman C.H. Li F. Ryffel B. Togbe D. Chung K.F. Oxidative stress in ozone-induced chronic lung inflammation and emphysema: A facet of chronic obstructive pulmonary disease Front. Immunol. 2020 11 1957 10.3389/fimmu.2020.01957 32983127 PMC7492639 · DOI
  11. [11]Flemming N.B. Gallo L.A. Forbes J.M. Mitochondrial dysfunction and signaling in diabetic kidney disease: Oxidative stress and beyond Semin. Nephrol. 2018 38 101 110 10.1016/j.semnephrol.2018.01.001 29602393 · DOI
  12. [12]Small D.M. Coombes J.S. Bennett N. Johnson D.W. Gobe G.C. Oxidative stress, anti-oxidant therapies and chronic kidney disease Nephrology 2012 17 311 321 10.1111/j.1440-1797.2012.01572.x 22288610 · DOI
  13. [13]Arazi H. Eghbali E. Suzuki K. Creatine supplementation, physical exercise and oxidative stress markers: A review of the mechanisms and effectiveness Nutrients 2021 13 869 10.3390/nu13030869 33800880 PMC8000194 · DOI · Paper page
  14. [15]Kruk J. Aboul-Enein B.H. Duchnik E. Exercise-induced oxidative stress and melatonin supplementation: Current evidence J. Physiol. Sci. 2021 71 27 10.1186/s12576-021-00812-2 34470608 PMC8409271 · DOI
  15. [16]Rodriguez M.L. Perez S. Mena-Molla S. Desco M.C. Ortega A.L. Oxidative stress and microvascular alterations in diabetic retinopathy: Future therapies Oxid. Med. Cell. Longev. 2019 2019 4940825 10.1155/2019/4940825 31814880 PMC6878793 · DOI
  16. [17]Lambeth J.D. NOX enzymes and the biology of reactive oxygen Nat. Rev. Immunol. 2004 4 181 189 10.1038/nri1312 15039755 · DOI · Paper page
  17. [18]Matuz-Mares D. Vazquez-Meza H. Vilchis-Landeros M.M. NOX as a therapeutic target in liver disease Antioxidants 2022 11 2038 10.3390/antiox11102038 36290761 PMC9598239 · DOI
  18. [19]Balaban R.S. Nemoto S. Finkel T. Mitochondria, oxidants, and aging Cell 2005 120 483 495 10.1016/j.cell.2005.02.001 15734681 · DOI · Paper page
  19. [20]Matuz-Mares D. Riveros-Rosas H. Vilchis-Landeros M.M. Vazquez-Meza H. Glutathione participation in the prevention of cardiovascular diseases Antioxidants 2021 10 1220 10.3390/antiox10081220 34439468 PMC8389000 · DOI
  20. [21]Meister A. On the discovery of glutathione Trends Biochem. Sci. 1988 13 185 188 10.1016/0968-0004(88)90148-X 3076280 · DOI
  21. [22]Townsend D.M. Tew K.D. Tapiero H. The importance of glutathione in human disease Biomed. Pharmacother. 2003 57 145 155 10.1016/S0753-3322(03)00043-X 12818476 PMC6522248 · DOI
  22. [23]Meister A. Anderson M.E. Glutathione Annu. Rev. Biochem. 1983 52 711 760 10.1146/annurev.bi.52.070183.003431 6137189 · DOI
  23. [24]Wang L. Wang L. Xia T. Bian G. Dong L. Tang Z. Wang F. A highly sensitive assay for spectrofluorimetric determination of reduced glutathione using organic nano-probes Spectrochim. Acta A Mol. Biomol. Spectrosc. 2005 61 2533 2538 10.1016/j.saa.2004.07.041 16043045 · DOI
  24. [25]Birben E. Sahiner U.M. Sackesen C. Erzurum S. Kalayci O. Oxidative stress and antioxidant defense World Allergy Organ. J. 2012 5 9 19 10.1097/WOX.0b013e3182439613 23268465 PMC3488923 · DOI
  25. [26]Scire A. Cianfruglia L. Minnelli C. Bartolini D. Torquato P. Principato G. Galli F. Armeni T. Glutathione compartmentalization and its role in glutathionylation and other regulatory processes of cellular pathways Biofactors 2019 45 152 168 10.1002/biof.1476 30561781 · DOI
  26. [27]Diaz Vivancos P. Wolff T. Markovic J. Pallardo F.V. Foyer C.H. A nuclear glutathione cycle within the cell cycle Biochem. J. 2010 431 169 178 10.1042/BJ20100409 20874710 · DOI
  27. [28]Jobbagy S. Vitturi D.A. Salvatore S.R. Turell L. Pires M.F. Kansanen E. Batthyany C. Lancaster J.R. Jr. Freeman B.A. Schopfer F.J. Electrophiles modulate glutathione reductase activity via alkylation and upregulation of glutathione biosynthesis Redox Biol. 2019 21 101050 10.1016/j.redox.2018.11.008 30654300 PMC6348771 · DOI
  28. [29]Wu G. Fang Y.Z. Yang S. Lupton J.R. Turner N.D. Glutathione metabolism and its implications for health J. Nutr. 2004 134 489 492 10.1093/jn/134.3.489 14988435 · DOI · Paper page
  29. [30]Bachhawat A.K. Yadav S. The glutathione cycle: Glutathione metabolism beyond the gamma-glutamyl cycle IUBMB Life 2018 70 585 592 10.1002/iub.1756 29667297 · DOI
  30. [31]Lu S.C. Glutathione synthesis Biochim. Biophys. Acta 2013 1830 3143 3153 10.1016/j.bbagen.2012.09.008 22995213 PMC3549305 · DOI
  31. [32]Chakravarthi S. Jessop C.E. Bulleid N.J. The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress EMBO Rep. 2006 7 271 275 10.1038/sj.embor.7400645 16607396 PMC1456887 · DOI
  32. [33]Kojer K. Bien M. Gangel H. Morgan B. Dick T.P. Riemer J. Glutathione redox potential in the mitochondrial intermembrane space is linked to the cytosol and impacts the Mia40 redox state EMBO J 2012 31 3169 3182 10.1038/emboj.2012.165 22705944 PMC3400016 · DOI
  33. [34]Chen Z. Putt D.A. Lash L.H. Enrichment and functional reconstitution of glutathione transport activity from rabbit kidney mitochondria: Further evidence for the role of the dicarboxylate and 2-oxoglutarate carriers in mitochondrial glutathione transport Arch. Biochem. Biophys. 2000 373 193 202 10.1006/abbi.1999.1527 10620338 · DOI
  34. [35]Armeni T. Cianfruglia L. Piva F. Urbanelli L. Luisa Caniglia M. Pugnaloni A. Principato G. S-D-Lactoylglutathione can be an alternative supply of mitochondrial glutathione Free Radic. Biol. Med. 2014 67 451 459 10.1016/j.freeradbiomed.2013.12.005 24333633 · DOI
  35. [36]Martensson J. Lai J.C. Meister A. High-affinity transport of glutathione is part of a multicomponent system essential for mitochondrial function Proc. Natl. Acad. Sci. USA 1990 87 7185 7189 10.1073/pnas.87.18.7185 2402500 PMC54708 · DOI
  36. [37]Chakravarthi S. Bulleid N.J. Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway J. Biol. Chem. 2004 279 39872 39879 10.1074/jbc.M406912200 15254031 · DOI
  37. [38]Ponsero A.J. Igbaria A. Darch M.A. Miled S. Outten C.E. Winther J.R. Palais G. D’Autreaux B. Delaunay-Moisan A. Toledano M.B. Endoplasmic reticulum transport of glutathione by Sec61 is regulated by Ero1 and Bip Mol. Cell 2017 67 962 973.e5 10.1016/j.molcel.2017.08.012 28918898 PMC5772773 · DOI
  38. [39]Noctor G. Queval G. Mhamdi A. Chaouch S. Foyer C.H. Glutathione Arab. Book 2011 9 e0142 10.1199/tab.0142 PMC3267239 22303267 · DOI
  39. [40]Voehringer D.W. McConkey D.J. McDonnell T.J. Brisbay S. Meyn R.E. Bcl-2 expression causes redistribution of glutathione to the nucleus Proc. Natl. Acad. Sci. USA 1998 95 2956 2960 10.1073/pnas.95.6.2956 9501197 PMC19676 · DOI
  40. [41]Zimmermann A.K. Loucks F.A. Schroeder E.K. Bouchard R.J. Tyler K.L. Linseman D.A. Glutathione binding to the Bcl-2 homology-3 domain groove: A molecular basis for Bcl-2 antioxidant function at mitochondria J. Biol. Chem. 2007 282 29296 29304 10.1074/jbc.M702853200 17690097 PMC2386251 · DOI
  41. [42]Blanco R.A. Ziegler T.R. Carlson B.A. Cheng P.Y. Park Y. Cotsonis G.A. Accardi C.J. Jones D.P. Diurnal variation in glutathione and cysteine redox states in human plasma Am. J. Clin. Nutr. 2007 86 1016 1023 10.1093/ajcn/86.4.1016 17921379 · DOI
  42. [44]Kondo T. Yoshida K. Urata Y. Goto S. Gasa S. Taniguchi N. gamma-Glutamylcysteine synthetase and active transport of glutathione S-conjugate are responsive to heat shock in K562 erythroid cells J. Biol. Chem. 1993 268 20366 20372 10.1016/S0021-9258(20)80737-6 8104187 · DOI
  43. [45]Urata Y. Yamamoto H. Goto S. Tsushima H. Akazawa S. Yamashita S. Nagataki S. Kondo T. Long exposure to high glucose concentration impairs the responsive expression of gamma-glutamylcysteine synthetase by interleukin-1beta and tumor necrosis factor-alpha in mouse endothelial cells J. Biol. Chem. 1996 271 15146 15152 10.1074/jbc.271.25.15146 8662965 · DOI
  44. [46]Woods J.S. Ellis M.E. Up-regulation of glutathione synthesis in rat kidney by methyl mercury. Relationship to mercury-induced oxidative stress Biochem. Pharmacol. 1995 50 1719 1724 10.1016/0006-2952(95)02075-6 7503776 · DOI
  45. [47]Dringen R. Brandmann M. Hohnholt M.C. Blumrich E.M. Glutathione-dependent detoxification processes in astrocytes Neurochem. Res. 2015 40 2570 2582 10.1007/s11064-014-1481-1 25428182 · DOI
  46. [48]McBean G.J. Cysteine, glutathione, and thiol redox balance in astrocytes Antioxidants 2017 6 62 10.3390/antiox6030062 28771170 PMC5618090 · DOI
  47. [49]Asanuma M. Miyazaki I. Glutathione and related molecules in parkinsonism Int. J. Mol. Sci. 2021 22 8689 10.3390/ijms22168689 34445395 PMC8395390 · DOI · Paper page
  48. [50]Sedlak T.W. Paul B.D. Parker G.M. Hester L.D. Snowman A.M. Taniguchi Y. Kamiya A. Snyder S.H. Sawa A. The glutathione cycle shapes synaptic glutamate activity Proc. Natl. Acad. Sci. USA 2019 116 2701 2706 10.1073/pnas.1817885116 30692251 PMC6377501 · DOI
  49. [51]Chen Y. Dong H. Thompson D.C. Shertzer H.G. Nebert D.W. Vasiliou V. Glutathione defense mechanism in liver injury: Insights from animal models Food Chem. Toxicol. 2013 60 38 44 10.1016/j.fct.2013.07.008 23856494 PMC3801188 · DOI
  50. [52]Gad S.C. Glutathione Encyclopedia of Toxicology 3rd ed. Wexler P. Academic Press Cambridge, MA, USA 2014 751 10.1016/B978-0-12-386454-3.00850-2 · DOI
  51. [53]Garcia-Ruiz C. Morales A. Ballesta A. Rodes J. Kaplowitz N. Fernandez-Checa J.C. Effect of chronic ethanol feeding on glutathione and functional integrity of mitochondria in periportal and perivenous rat hepatocytes J. Clin. Investig. 1994 94 193 201 10.1172/JCI117306 8040260 PMC296297 · DOI
  52. [54]Griffith O.W. Meister A. Origin and turnover of mitochondrial glutathione Proc. Natl. Acad. Sci. USA 1985 82 4668 4672 10.1073/pnas.82.14.4668 3860816 PMC390447 · DOI
  53. [55]Giustarini D. Milzani A. Dalle-Donne I. Rossi R. Red blood cells as a physiological source of glutathione for extracellular fluids Blood Cells Mol. Dis. 2008 40 174 179 10.1016/j.bcmd.2007.09.001 17964197 · DOI
  54. [56]Swietek K. Juszczyk J. Reduced glutathione concentration in erythrocytes of patients with acute and chronic viral hepatitis J. Viral Hepat. 1997 4 139 141 10.1111/j.1365-2893.1997.tb00217.x 9097271 · DOI
  55. [57]van ‘t Erve T.J. Wagner B.A. Ryckman K.K. Raife T.J. Buettner G.R. The concentration of glutathione in human erythrocytes is a heritable trait Free Radic. Biol. Med. 2013 65 742 749 10.1016/j.freeradbiomed.2013.08.002 23938402 PMC3859832 · DOI
  56. [58]Cantin A.M. North S.L. Hubbard R.C. Crystal R.G. Normal alveolar epithelial lining fluid contains high levels of glutathione J. Appl. Physiol. 1987 63 152 157 10.1152/jappl.1987.63.1.152 3040659 · DOI
  57. [59]Jean J.C. Liu Y. Brown L.A. Marc R.E. Klings E. Joyce-Brady M. Gamma-glutamyl transferase deficiency results in lung oxidant stress in normoxia Am. J. Physiol. Lung Cell. Mol. Physiol. 2002 283 L766 L776 10.1152/ajplung.00250.2000 12225953 · DOI
  58. [60]van Klaveren R.J. Demedts M. Nemery B. Cellular glutathione turnover in vitro, with emphasis on type II pneumocytes Eur. Respir. J. 1997 10 1392 1400 10.1183/09031936.97.10061392 9192948 · DOI
  59. [61]Li S. Li X. Rozanski G.J. Regulation of glutathione in cardiac myocytes J. Mol. Cell Cardiol. 2003 35 1145 1152 10.1016/S0022-2828(03)00230-X 12967637 · DOI
  60. [63]Vazquez-Meza H. de Pina M.Z. Pardo J.P. Riveros-Rosas H. Villalobos-Molina R. Pina E. Non-steroidal anti-inflammatory drugs activate NADPH oxidase in adipocytes and raise the H2O2 pool to prevent cAMP-stimulated protein kinase a activation and inhibit lipolysis BMC Biochem. 2013 14 13 10.1186/1471-2091-14-13 23718778 PMC3671242 · DOI
  61. [64]Kalinina E. Novichkova M. Glutathione in protein redox modulation through S-glutathionylation and S-nitrosylation Molecules 2021 26 435 10.3390/molecules26020435 33467703 PMC7838997 · DOI
  62. [65]Rashdan N.A. Shrestha B. Pattillo C.B. S-glutathionylation, friend or foe in cardiovascular health and disease Redox Biol. 2020 37 101693 10.1016/j.redox.2020.101693 32912836 PMC7767732 · DOI
  63. [66]Benhar M. Oxidants, Antioxidants and thiol redox switches in the control of regulated cell death pathways Antioxidants 2020 9 309 10.3390/antiox9040309 32290499 PMC7222211 · DOI
  64. [67]Zhang J. Ye Z.W. Singh S. Townsend D.M. Tew K.D. An evolving understanding of the S-glutathionylation cycle in pathways of redox regulation Free Radic. Biol. Med. 2018 120 204 216 10.1016/j.freeradbiomed.2018.03.038 29578070 PMC5940525 · DOI
  65. [68]Cha S.J. Kim H. Choi H.J. Lee S. Kim K. Protein glutathionylation in the pathogenesis of neurodegenerative diseases Oxid. Med. Cell. Longev. 2017 2017 2818565 10.1155/2017/2818565 29456785 PMC5804111 · DOI
  66. [69]Guaita-Esteruelas S. Guma J. Masana L. Borras J. The peritumoural adipose tissue microenvironment and cancer. The roles of fatty acid binding protein 4 and fatty acid binding protein 5 Mol. Cell. Endocrinol. 2018 462 107 118 10.1016/j.mce.2017.02.002 28163102 · DOI
  67. [70]Lermant A. Murdoch C.E. Cysteine glutathionylation acts as a redox switch in endothelial cells Antioxidants 2019 8 315 10.3390/antiox8080315 31426416 PMC6720164 · DOI
  68. [71]Mailloux R.J. Protein S-glutathionylation reactions as a global inhibitor of cell metabolism for the desensitization of hydrogen peroxide signals Redox Biol. 2020 32 101472 10.1016/j.redox.2020.101472 32171726 PMC7076094 · DOI
  69. [72]Aesif S.W. Anathy V. Kuipers I. Guala A.S. Reiss J.N. Ho Y.S. Janssen-Heininger Y.M. Ablation of glutaredoxin-1 attenuates lipopolysaccharide-induced lung inflammation and alveolar macrophage activation Am. J. Respir. Cell Mol. Biol. 2011 44 491 499 10.1165/rcmb.2009-0136OC 20539014 PMC3095922 · DOI
  70. [73]Gorelenkova Miller O. Behring J.B. Siedlak S.L. Jiang S. Matsui R. Bachschmid M.M. Zhu X. Mieyal J.J. Upregulation of glutaredoxin-1 activates microglia and promotes neurodegeneration: Implications for Parkinson’s disease Antioxid. Redox Signal. 2016 25 967 982 10.1089/ars.2015.6598 27224303 PMC5175443 · DOI
  71. [74]Sakai J. Li J. Subramanian K.K. Mondal S. Bajrami B. Hattori H. Jia Y. Dickinson B.C. Zhong J. Ye K. Reactive oxygen species-induced actin glutathionylation controls actin dynamics in neutrophils Immunity 2012 37 1037 1049 10.1016/j.immuni.2012.08.017 23159440 PMC3525814 · DOI
  72. [75]Barinova K.V. Serebryakova M.V. Eldarov M.A. Kulikova A.A. Mitkevich V.A. Muronetz V.I. Schmalhausen E.V. S-glutathionylation of human glyceraldehyde-3-phosphate dehydrogenase and possible role of Cys152-Cys156 disulfide bridge in the active site of the protein Biochim. Biophys. Acta Gen. Subj. 2020 1864 129560 10.1016/j.bbagen.2020.129560 32061786 · DOI
  73. [76]Bachhawat A.K. Thakur A. Kaur J. Zulkifli M. Glutathione transporters Biochim. Biophys. Acta 2013 1830 3154 3164 10.1016/j.bbagen.2012.11.018 23206830 · DOI
  74. [77]Couto N. Wood J. Barber J. The role of glutathione reductase and related enzymes on cellular redox homoeostasis network Free Radic. Biol. Med. 2016 95 27 42 10.1016/j.freeradbiomed.2016.02.028 26923386 · DOI
  75. [78]Zhang Z. Liu F. Chen J. Conformational changes of CFTR upon phosphorylation and ATP binding Cell 2017 170 483 491.e8 10.1016/j.cell.2017.06.041 28735752 · DOI
  76. [79]Cole S.P. Deeley R.G. Transport of glutathione and glutathione conjugates by MRP1 Trends Pharmacol. Sci. 2006 27 438 446 10.1016/j.tips.2006.06.008 16820223 · DOI
  77. [80]Homolya L. Varadi A. Sarkadi B. Multidrug resistance-associated proteins: Export pumps for conjugates with glutathione, glucuronate or sulfate Biofactors 2003 17 103 114 10.1002/biof.5520170111 12897433 · DOI
  78. [81]Baiceanu E. Nguyen K.A. Gonzalez-Lobato L. Nasr R. Baubichon-Cortay H. Loghin F. Le Borgne M. Chow L. Boumendjel A. Peuchmaur M. 2-Indolylmethylenebenzofuranones as first effective inhibitors of ABCC2 Eur. J. Med. Chem. 2016 122 408 418 10.1016/j.ejmech.2016.06.039 27393949 · DOI
  79. [82]Ballatori N. Krance S.M. Marchan R. Hammond C.L. Plasma membrane glutathione transporters and their roles in cell physiology and pathophysiology Mol. Asp. Med. 2009 30 13 28 10.1016/j.mam.2008.08.004 18786560 PMC2716123 · DOI
  80. [83]Baiceanu E. Crisan G. Loghin F. Falson P. Modulators of the human ABCC2: Hope from natural sources? Future Med. Chem. 2015 7 2041 2063 10.4155/fmc.15.131 26496229 · DOI
  81. [84]Brechbuhl H.M. Gould N. Kachadourian R. Riekhof W.R. Voelker D.R. Day B.J. Glutathione transport is a unique function of the ATP-binding cassette protein ABCG2 J. Biol. Chem. 2010 285 16582 16587 10.1074/jbc.M109.090506 20332504 PMC2878084 · DOI
  82. [85]Johnson Z.L. Chen J. Structural basis of substrate recognition by the multidrug resistance protein MRP1 Cell 2017 168 1075 1085.e9 10.1016/j.cell.2017.01.041 28238471 · DOI · Paper page
  83. [86]Juan-Carlos P.M. Perla-Lidia P.P. Stephanie-Talia M.M. Monica-Griselda A.M. Luz-Maria T.E. ABC transporter superfamily. An updated overview, relevance in cancer multidrug resistance and perspectives with personalized medicine Mol. Biol. Rep. 2021 48 1883 1901 10.1007/s11033-021-06155-w 33616835 · DOI
  84. [87]Nasr R. Lorendeau D. Khonkarn R. Dury L. Peres B. Boumendjel A. Cortay J.C. Falson P. Chaptal V. Baubichon-Cortay H. Molecular analysis of the massive GSH transport mechanism mediated by the human Multidrug Resistant Protein 1/ABCC1 Sci. Rep. 2020 10 7616 10.1038/s41598-020-64400-x 32377003 PMC7203140 · DOI
  85. [88]Lorendeau D. Dury L. Genoux-Bastide E. Lecerf-Schmidt F. Simoes-Pires C. Carrupt P.A. Terreux R. Magnard S. Di Pietro A. Boumendjel A. Collateral sensitivity of resistant MRP1-overexpressing cells to flavonoids and derivatives through GSH efflux Biochem. Pharmacol. 2014 90 235 245 10.1016/j.bcp.2014.05.017 24875445 · DOI
  86. [90]Chen Z.S. Tiwari A.K. Multidrug resistance proteins (MRPs/ABCCs) in cancer chemotherapy and genetic diseases FEBS J. 2011 278 3226 3245 10.1111/j.1742-4658.2011.08235.x 21740521 PMC3168698 · DOI · Paper page
  87. [91]Ito K. Olsen S.L. Qiu W. Deeley R.G. Cole S.P. Mutation of a single conserved tryptophan in multidrug resistance protein 1 (MRP1/ABCC1) results in loss of drug resistance and selective loss of organic anion transport J. Biol. Chem. 2001 276 15616 15624 10.1074/jbc.M011246200 11278867 · DOI
  88. [92]Cheepala S. Hulot J.S. Morgan J.A. Sassi Y. Zhang W. Naren A.P. Schuetz J.D. Cyclic nucleotide compartmentalization: Contributions of phosphodiesterases and ATP-binding cassette transporters Annu. Rev. Pharmacol. Toxicol. 2013 53 231 253 10.1146/annurev-pharmtox-010611-134609 23072381 PMC4303346 · DOI
  89. [93]Decouture B. Dreano E. Belleville-Rolland T. Kuci O. Dizier B. Bazaa A. Coqueran B. Lompre A.M. Denis C.V. Hulot J.S. Impaired platelet activation and cAMP homeostasis in MRP4-deficient mice Blood 2015 126 1823 1830 10.1182/blood-2015-02-631044 26316625 PMC4626663 · DOI
  90. [94]Jedlitschky G. Greinacher A. Kroemer H.K. Transporters in human platelets: Physiologic function and impact for pharmacotherapy Blood 2012 119 3394 3402 10.1182/blood-2011-09-336933 22337717 · DOI
  91. [95]Jedlitschky G. Tirschmann K. Lubenow L.E. Nieuwenhuis H.K. Akkerman J.W. Greinacher A. Kroemer H.K. The nucleotide transporter MRP4 (ABCC4) is highly expressed in human platelets and present in dense granules, indicating a role in mediator storage Blood 2004 104 3603 3610 10.1182/blood-2003-12-4330 15297306 · DOI
  92. [96]Zhang Y.K. Wang Y.J. Gupta P. Chen Z.S. Multidrug resistance proteins (MRPs) and cancer therapy AAPS J. 2015 17 802 812 10.1208/s12248-015-9757-1 25840885 PMC4476997 · DOI
  93. [97]Sampath J. Adachi M. Hatse S. Naesens L. Balzarini J. Flatley R.M. Matherly L.H. Schuetz J.D. Role of MRP4 and MRP5 in biology and chemotherapy AAPS PharmSci 2002 4 E14 10.1208/ps040314 12423063 PMC2751353 · DOI
  94. [98]Hu X. Plomp A. Wijnholds J. Ten Brink J. van Soest S. van den Born L.I. Leys A. Peek R. de Jong P.T. Bergen A.A. ABCC6/MRP6 mutations: Further insight into the molecular pathology of pseudoxanthoma elasticum Eur. J. Hum. Genet. 2003 11 215 224 10.1038/sj.ejhg.5200953 12673275 · DOI
  95. [99]Sodani K. Patel A. Kathawala R.J. Chen Z.S. Multidrug resistance associated proteins in multidrug resistance Chin. J. Cancer 2012 31 58 72 10.5732/cjc.011.10329 22098952 PMC3777468 · DOI
  96. [100]Belinsky M.G. Chen Z.S. Shchaveleva I. Zeng H. Kruh G.D. Characterization of the drug resistance and transport properties of multidrug resistance protein 6 (MRP6, ABCC6) Cancer Res. 2002 62 6172 6177 12414644
  97. [101]Roy U. Barber P. Tse-Dinh Y.C. Batrakova E.V. Mondal D. Nair M. Role of MRP transporters in regulating antimicrobial drug inefficacy and oxidative stress-induced pathogenesis during HIV-1 and TB infections Front. Microbiol. 2015 6 948 10.3389/fmicb.2015.00948 26441882 PMC4585023 · DOI
  98. [102]Hopper-Borge E. Xu X. Shen T. Shi Z. Chen Z.S. Kruh G.D. Human multidrug resistance protein 7 (ABCC10) is a resistance factor for nucleoside analogues and epothilone B Cancer Res. 2009 69 178 184 10.1158/0008-5472.CAN-08-1420 19118001 PMC2745904 · DOI
  99. [103]Guo Y. Kotova E. Chen Z.S. Lee K. Hopper-Borge E. Belinsky M.G. Kruh G.D. MRP8, ATP-binding cassette C11 (ABCC11), is a cyclic nucleotide efflux pump and a resistance factor for fluoropyrimidines 2′,3′-dideoxycytidine and 9′-(2′-phosphonylmethoxyethyl)adenine J. Biol. Chem. 2003 278 29509 29514 10.1074/jbc.M304059200 12764137 · DOI
  100. [104]Yang A.K. Zhou Z.W. Wei M.Q. Liu J.P. Zhou S.F. Modulators of multidrug resistance associated proteins in the management of anticancer and antimicrobial drug resistance and the treatment of inflammatory diseases Curr. Top. Med. Chem. 2010 10 1732 1756 10.2174/156802610792928040 20645920 · DOI
  101. [105]Zhou S.F. Wang L.L. Di Y.M. Xue C.C. Duan W. Li C.G. Li Y. Substrates and inhibitors of human multidrug resistance associated proteins and the implications in drug development Curr. Med. Chem. 2008 15 1981 2039 10.2174/092986708785132870 18691054 · DOI
  102. [106]Chambers I.G. Kumar P. Lichtenberg J. Wang P. Yu J. Phillips J.D. Kane M.A. Bodine D. Hamza I. MRP5 and MRP9 play a concerted role in male reproduction and mitochondrial function Proc. Natl. Acad. Sci. USA 2022 119 e2111617119 10.1073/pnas.2111617119 35121660 PMC8832985 · DOI
  103. [107]Borst P. Evers R. Kool M. Wijnholds J. A family of drug transporters: The multidrug resistance-associated proteins J. Natl. Cancer Inst. 2000 92 1295 1302 10.1093/jnci/92.16.1295 10944550 · DOI · Paper page
  104. [108]Leslie E.M. Deeley R.G. Cole S.P. Toxicological relevance of the multidrug resistance protein 1, MRP1 (ABCC1) and related transporters Toxicology 2001 167 3 23 10.1016/S0300-483X(01)00454-1 11557126 · DOI · Paper page
  105. [109]Konig J. Nies A.T. Cui Y. Leier I. Keppler D. Conjugate export pumps of the multidrug resistance protein (MRP) family: Localization, substrate specificity, and MRP2-mediated drug resistance Biochim. Biophys. Acta 1999 1461 377 394 10.1016/S0005-2736(99)00169-8 10581368 · DOI
  106. [110]Linsdell P. Hanrahan J.W. Glutathione permeability of CFTR Am. J. Physiol. 1998 275 C323 C326 10.1152/ajpcell.1998.275.1.C323 9688865 · DOI
  107. [111]Borst P. de Wolf C. van de Wetering K. Multidrug resistance-associated proteins 3, 4, and 5 Pflugers Arch. 2007 453 661 673 10.1007/s00424-006-0054-9 16586096 · DOI
  108. [112]Rius M. Nies A.T. Hummel-Eisenbeiss J. Jedlitschky G. Keppler D. Cotransport of reduced glutathione with bile salts by MRP4 (ABCC4) localized to the basolateral hepatocyte membrane Hepatology 2003 38 374 384 10.1053/jhep.2003.50331 12883481 · DOI
  109. [113]Zelcer N. Reid G. Wielinga P. Kuil A. van der Heijden I. Schuetz J.D. Borst P. Steroid and bile acid conjugates are substrates of human multidrug-resistance protein (MRP) 4 (ATP-binding cassette C4) Biochem. J. 2003 371 361 367 10.1042/bj20021886 12523936 PMC1223295 · DOI
  110. [114]Wijnholds J. Mol C.A. van Deemter L. de Haas M. Scheffer G.L. Baas F. Beijnen J.H. Scheper R.J. Hatse S. De Clercq E. Multidrug-resistance protein 5 is a multispecific organic anion transporter able to transport nucleotide analogs Proc. Natl. Acad. Sci. USA 2000 97 7476 7481 10.1073/pnas.120159197 10840050 PMC16570 · DOI
  111. [115]Ilias A. Urban Z. Seidl T.L. Le Saux O. Sinko E. Boyd C.D. Sarkadi B. Varadi A. Loss of ATP-dependent transport activity in pseudoxanthoma elasticum-associated mutants of human ABCC6 (MRP6) J. Biol. Chem. 2002 277 16860 16867 10.1074/jbc.M110918200 11880368 · DOI
  112. [116]Kruh G.D. Guo Y. Hopper-Borge E. Belinsky M.G. Chen Z.S. ABCC10, ABCC11, and ABCC12 Pflugers Arch. 2007 453 675 684 10.1007/s00424-006-0114-1 16868766 · DOI
  113. [117]Ono N. Van der Heijden I. Scheffer G.L. Van de Wetering K. Van Deemter E. De Haas M. Boerke A. Gadella B.M. De Rooij D.G. Neefjes J.J. Multidrug resistance-associated protein 9 (ABCC12) is present in mouse and boar sperm Biochem. J. 2007 406 31 40 10.1042/BJ20070292 17472575 PMC1948986 · DOI
  114. [118]Li B. Umapathy A. Tran L.U. Donaldson P.J. Lim J.C. Molecular identification and cellular localisation of GSH synthesis, uptake, efflux and degradation pathways in the rat ciliary body Histochem. Cell Biol. 2013 139 559 571 10.1007/s00418-012-1049-6 23229863 · DOI
  115. [120]Dalle-Donne I. Garavaglia M.L. Colombo G. Astori E. Lionetti M.C. La Porta C.A.M. Santucci A. Rossi R. Giustarini D. Milzani A. Cigarette smoke and glutathione: Focus on in vitro cell models Toxicol. In Vitro 2020 65 104818 10.1016/j.tiv.2020.104818 32135238 · DOI
  116. [121]Cantin A.M. Hanrahan J.W. Bilodeau G. Ellis L. Dupuis A. Liao J. Zielenski J. Durie P. Cystic fibrosis transmembrane conductance regulator function is suppressed in cigarette smokers Am. J. Respir. Crit. Care Med. 2006 173 1139 1144 10.1164/rccm.200508-1330OC 16497995 · DOI
  117. [122]Gould N.S. Min E. Martin R.J. Day B.J. CFTR is the primary known apical glutathione transporter involved in cigarette smoke-induced adaptive responses in the lung Free Radic. Biol. Med. 2012 52 1201 1206 10.1016/j.freeradbiomed.2012.01.001 22266045 PMC3920665 · DOI
  118. [123]Gadsby D.C. Nairn A.C. Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis Physiol. Rev. 1999 79 S77 S107 10.1152/physrev.1999.79.1.S77 9922377 · DOI
  119. [124]Wang W. Oliva C. Li G. Holmgren A. Lillig C.H. Kirk K.L. Reversible silencing of CFTR chloride channels by glutathionylation J. Gen. Physiol. 2005 125 127 141 10.1085/jgp.200409115 15657297 PMC2217496 · DOI
  120. [125]Huang K.P. Huang F.L. Glutathionylation of proteins by glutathione disulfide S-oxide Biochem. Pharmacol. 2002 64 1049 1056 10.1016/S0006-2952(02)01175-9 12213604 · DOI
  121. [126]Jetter A. Kullak-Ublick G.A. Drugs and hepatic transporters: A review Pharmacol. Res. 2020 154 104234 10.1016/j.phrs.2019.04.018 31004787 · DOI
  122. [127]Granados J.C. Nigam A.K. Bush K.T. Jamshidi N. Nigam S.K. A key role for the transporter OAT1 in systemic lipid metabolism J. Biol. Chem. 2021 296 100603 10.1016/j.jbc.2021.100603 33785360 PMC8102404 · DOI
  123. [128]Roth M. Obaidat A. Hagenbuch B. OATPs, OATs and OCTs: The organic anion and cation transporters of the SLCO and SLC22A gene superfamilies Br. J. Pharmacol. 2012 165 1260 1287 10.1111/j.1476-5381.2011.01724.x 22013971 PMC3372714 · DOI
  124. [129]Lash L.H. Renal membrane transport of glutathione in toxicology and disease Vet. Pathol. 2011 48 408 419 10.1177/0300985810375811 20656901 · DOI
  125. [130]Hagenbuch B. Meier P.J. The superfamily of organic anion transporting polypeptides Biochim. Biophys. Acta 2003 1609 1 18 10.1016/S0005-2736(02)00633-8 12507753 · DOI
  126. [131]Brenner S. Klameth L. Riha J. Scholm M. Hamilton G. Bajna E. Ausch C. Reiner A. Jager W. Thalhammer T. Specific expression of OATPs in primary small cell lung cancer (SCLC) cells as novel biomarkers for diagnosis and therapy Cancer Lett. 2015 356 517 524 10.1016/j.canlet.2014.09.025 25301452 · DOI
  127. [132]van de Steeg E. Stranecky V. Hartmannova H. Noskova L. Hrebicek M. Wagenaar E. van Esch A. de Waart D.R. Oude Elferink R.P. Kenworthy K.E. Complete OATP1B1 and OATP1B3 deficiency causes human Rotor syndrome by interrupting conjugated bilirubin reuptake into the liver J. Clin. Investig. 2012 122 519 528 10.1172/JCI59526 22232210 PMC3266790 · DOI
  128. [133]Lomaestro B.M. Malone M. Glutathione in health and disease: Pharmacotherapeutic issues Ann. Pharmacother. 1995 29 1263 1273 10.1177/106002809502901213 8672832 · DOI
  129. [134]Pastore A. Federici G. Bertini E. Piemonte F. Analysis of glutathione: Implication in redox and detoxification Clin. Chim. Acta 2003 333 19 39 10.1016/S0009-8981(03)00200-6 12809732 · DOI
  130. [136]Minich D.M. Brown B.I. A review of dietary (phyto)nutrients for glutathione support Nutrients 2019 11 2073 10.3390/nu11092073 31484368 PMC6770193 · DOI
  131. [137]Bajic V.P. Van Neste C. Obradovic M. Zafirovic S. Radak D. Bajic V.B. Essack M. Isenovic E.R. Glutathione “Redox Homeostasis” and its relation to cardiovascular disease Oxid. Med. Cell. Longev. 2019 2019 5028181 10.1155/2019/5028181 31210841 PMC6532282 · DOI
  132. [138]Hudson V.M. Rethinking cystic fibrosis pathology: The critical role of abnormal reduced glutathione (GSH) transport caused by CFTR mutation Free Radic. Biol. Med. 2001 30 1440 1461 10.1016/S0891-5849(01)00530-5 11390189 · DOI
  133. [139]Cantin A.M. White T.B. Cross C.E. Forman H.J. Sokol R.J. Borowitz D. Antioxidants in cystic fibrosis. Conclusions from the CF antioxidant workshop, Bethesda, Maryland, November 11-12, 2003 Free Radic. Biol. Med. 2007 42 15 31 10.1016/j.freeradbiomed.2006.09.022 17157190 PMC2696206 · DOI
  134. [140]Cross C.E. Halliwell B. Borish E.T. Pryor W.A. Ames B.N. Saul R.L. McCord J.M. Harman D. Oxygen radicals and human disease Ann. Intern. Med. 1987 107 526 545 10.7326/0003-4819-107-4-526 3307585 · DOI · Paper page
  135. [142]Anderson M.E. Luo J.L. Glutathione therapy: From prodrugs to genes Semin. Liver Dis. 1998 18 415 424 10.1055/s-2007-1007174 9875558 · DOI
  136. [143]Atmaca G. Antioxidant effects of sulfur-containing amino acids Yonsei Med. J. 2004 45 776 788 10.3349/ymj.2004.45.5.776 15515186 · DOI
  137. [145]Masubuchi Y. Nakayama J. Sadakata Y. Protective effects of exogenous glutathione and related thiol compounds against drug-induced liver injury Biol. Pharm. Bull. 2011 34 366 370 10.1248/bpb.34.366 21372386 · DOI
  138. [146]Sochman J. N-acetylcysteine in acute cardiology: 10 years later: What do we know and what would we like to know?! J. Am. Coll. Cardiol. 2002 39 1422 1428 10.1016/S0735-1097(02)01797-7 11985902 · DOI
  139. [147]Vendemiale G. Altomare E. Trizio T. Le Grazie C. Di Padova C. Salerno M.T. Carrieri V. Albano O. Effects of oral S-adenosyl-L-methionine on hepatic glutathione in patients with liver disease Scand. J. Gastroenterol. 1989 24 407 415 10.3109/00365528909093067 2781235 · DOI
  140. [148]Herzenberg L.A. De Rosa S.C. Dubs J.G. Roederer M. Anderson M.T. Ela S.W. Deresinski S.C. Herzenberg L.A. Glutathione deficiency is associated with impaired survival in HIV disease Proc. Natl. Acad. Sci. USA 1997 94 1967 1972 10.1073/pnas.94.5.1967 9050888 PMC20026 · DOI
  141. [149]Kovacs V. Gasz B. Balatonyi B. Jaromi L. Kisfali P. Borsiczky B. Jancso G. Marczin N. Szabados S. Melegh B. Polymorphisms in glutathione S-transferase are risk factors for perioperative acute myocardial infarction after cardiac surgery: A preliminary study Mol. Cell Biochem. 2014 389 79 84 10.1007/s11010-013-1929-7 24435850 · DOI
  142. [150]Lagman M. Ly J. Saing T. Kaur Singh M. Vera Tudela E. Morris D. Chi P.T. Ochoa C. Sathananthan A. Venketaraman V. Investigating the causes for decreased levels of glutathione in individuals with type II diabetes PLoS ONE 2015 10 e0118436 10.1371/journal.pone.0118436 25790445 PMC4366217 · DOI
  143. [151]Silvagno F. Vernone A. Pescarmona G.P. The role of glutathione in protecting against the severe inflammatory response triggered by COVID-19 Antioxidants 2020 9 624 10.3390/antiox9070624 32708578 PMC7402141 · DOI
  144. [152]Yang J. Song P. Zhou G. A study on the correlations of MRP-1 expression with the pathogenesis and prognosis of colorectal cancer J. BUON 2019 24 84 90 30941955
  145. [153]Innis S.M. Davidson A.G. Melynk S. James S.J. Choline-related supplements improve abnormal plasma methionine-homocysteine metabolites and glutathione status in children with cystic fibrosis Am. J. Clin. Nutr. 2007 85 702 708 10.1093/ajcn/85.3.702 17344490 · DOI
  146. [154]Jones D.P. Carlson J.L. Mody V.C. Cai J. Lynn M.J. Sternberg P. Redox state of glutathione in human plasma Free Radic. Biol. Med. 2000 28 625 635 10.1016/S0891-5849(99)00275-0 10719244 · DOI
  147. [155]Giustarini D. Dalle-Donne I. Colombo R. Milzani A. Rossi R. Interference of plasmatic reduced glutathione and hemolysis on glutathione disulfide levels in human blood Free Radic. Res. 2004 38 1101 1106 10.1080/10715760400008854 15512798 · DOI
  148. [156]Preville X. Salvemini F. Giraud S. Chaufour S. Paul C. Stepien G. Ursini M.V. Arrigo A.P. Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery Exp. Cell Res. 1999 247 61 78 10.1006/excr.1998.4347 10047448 · DOI
  149. [157]Swamy S.M. Rajasekaran N.S. Thannickal V.J. Nuclear factor-erythroid-2-related factor 2 in aging and lung fibrosis Am. J. Pathol. 2016 186 1712 1723 10.1016/j.ajpath.2016.02.022 27338106 PMC4929397 · DOI
  150. [158]Brewer A.C. Murray T.V. Arno M. Zhang M. Anilkumar N.P. Mann G.E. Shah A.M. Nox4 regulates Nrf2 and glutathione redox in cardiomyocytes in vivo Free Radic. Biol. Med. 2011 51 205 215 10.1016/j.freeradbiomed.2011.04.022 21554947 PMC3112490 · DOI
  151. [159]Rosenblat M. Volkova N. Coleman R. Aviram M. Anti-oxidant and anti-atherogenic properties of liposomal glutathione: Studies in vitro, and in the atherosclerotic apolipoprotein E-deficient mice Atherosclerosis 2007 195 e61 e68 10.1016/j.atherosclerosis.2007.05.012 17588583 · DOI
  152. [160]Lin C.C. Yin M.C. Hsu C.C. Lin M.P. Effect of five cysteine-containing compounds on three lipogenic enzymes in Balb/cA mice consuming a high saturated fat diet Lipids 2004 39 843 848 10.1007/s11745-004-1305-4 15669759 · DOI
  153. [161]Callegari A. Liu Y. White C.C. Chait A. Gough P. Raines E.W. Cox D. Kavanagh T.J. Rosenfeld M.E. Gain and loss of function for glutathione synthesis: Impact on advanced atherosclerosis in apolipoprotein E-deficient mice Arterioscler. Thromb. Vasc. Biol. 2011 31 2473 2482 10.1161/ATVBAHA.111.229765 21868708 PMC3415243 · DOI
  154. [162]Lewis P. Stefanovic N. Pete J. Calkin A.C. Giunti S. Thallas-Bonke V. Jandeleit-Dahm K.A. Allen T.J. Kola I. Cooper M.E. Lack of the antioxidant enzyme glutathione peroxidase-1 accelerates atherosclerosis in diabetic apolipoprotein E-deficient mice Circulation 2007 115 2178 2187 10.1161/CIRCULATIONAHA.106.664250 17420349 · DOI
  155. [163]Matouskova P. Hanouskova B. Skalova L. MicroRNAs as potential regulators of glutathione peroxidases expression and their role in obesity and related pathologies Int. J. Mol. Sci. 2018 19 1199 10.3390/ijms19041199 29662007 PMC5979329 · DOI
  156. [164]Shimizu H. Kiyohara Y. Kato I. Kitazono T. Tanizaki Y. Kubo M. Ueno H. Ibayashi S. Fujishima M. Iida M. Relationship between plasma glutathione levels and cardiovascular disease in a defined population: The Hisayama study Stroke 2004 35 2072 2077 10.1161/01.STR.0000138022.86509.2d 15256685 · DOI
  157. [165]Rybka J. Kupczyk D. Kedziora-Kornatowska K. Motyl J. Czuczejko J. Szewczyk-Golec K. Kozakiewicz M. Pawluk H. Carvalho L.A. Kedziora J. Glutathione-related antioxidant defense system in elderly patients treated for hypertension Cardiovasc. Toxicol. 2011 11 1 9 10.1007/s12012-010-9096-5 21140238 PMC3035775 · DOI
  158. [166]Damy T. Kirsch M. Khouzami L. Caramelle P. Le Corvoisier P. Roudot-Thoraval F. Dubois-Rande J.L. Hittinger L. Pavoine C. Pecker F. Glutathione deficiency in cardiac patients is related to the functional status and structural cardiac abnormalities PLoS ONE 2009 4 e4871 10.1371/journal.pone.0004871 19319187 PMC2655715 · DOI
  159. [167]De Mattia G. Bravi M.C. Laurenti O. Cassone-Faldetta M. Proietti A. De Luca O. Armiento A. Ferri C. Reduction of oxidative stress by oral N-acetyl-L-cysteine treatment decreases plasma soluble vascular cell adhesion molecule-1 concentrations in non-obese, non-dyslipidaemic, normotensive, patients with non-insulin-dependent diabetes Diabetologia 1998 41 1392 1396 10.1007/s001250051082 9833950 · DOI
  160. [168]Allen J. Bradley R.D. Effects of oral glutathione supplementation on systemic oxidative stress biomarkers in human volunteers J. Altern. Complement. Med. 2011 17 827 833 10.1089/acm.2010.0716 21875351 PMC3162377 · DOI
  161. [169]Pizzorno J. Glutathione! Integr. Med. 2014 13 8 12 PMC4684116 26770075
  162. [170]Buonocore D. Grosini M. Giardina S. Michelotti A. Carrabetta M. Seneci A. Verri M. Dossena M. Marzatico F. Bioavailability study of an innovative orobuccal formulation of glutathione Oxid. Med. Cell. Longev. 2016 2016 3286365 10.1155/2016/3286365 26649136 PMC4663342 · DOI
  163. [171]Schmitt B. Vicenzi M. Garrel C. Denis F.M. Effects of N-acetylcysteine, oral glutathione (GSH) and a novel sublingual form of GSH on oxidative stress markers: A comparative crossover study Redox Biol. 2015 6 198 205 10.1016/j.redox.2015.07.012 26262996 PMC4536296 · DOI
  164. [173]Chen X.Q. Mobley W.C. Alzheimer disease pathogenesis: Insights from molecular and cellular biology studies of oligomeric Abeta and Tau species Front. Neurosci. 2019 13 659 10.3389/fnins.2019.00659 31293377 PMC6598402 · DOI
  165. [174]Li N. Gao X. Zheng L. Huang Q. Zeng F. Chen H. Farag M.A. Zhao C. Advances in fucoxanthin chemistry and management of neurodegenerative diseases Phytomedicine 2022 105 154352 10.1016/j.phymed.2022.154352 35917771 · DOI
  166. [175]Aoyama K. Glutathione in the brain Int. J. Mol. Sci. 2021 22 5010 10.3390/ijms22095010 34065042 PMC8125908 · DOI
  167. [176]Dong X.X. Wang Y. Qin Z.H. Molecular mechanisms of excitotoxicity and their relevance to pathogenesis of neurodegenerative diseases Acta Pharmacol. Sin. 2009 30 379 387 10.1038/aps.2009.24 19343058 PMC4002277 · DOI · Paper page
  168. [177]Zhang K. Zhu S. Li J. Jiang T. Feng L. Pei J. Targeting autophagy using small-molecule compounds to improve potential therapy of Parkinson’s disease Acta Pharm. Sin. 2021 11 3015 3034 10.1016/j.apsb.2021.02.016 PMC8546670 34729301 · DOI
  169. [178]Bjorklund G. Peana M. Maes M. Dadar M. Severin B. The glutathione system in Parkinson’s disease and its progression Neurosci. Biobehav. Rev. 2021 120 470 478 10.1016/j.neubiorev.2020.10.004 33068556 · DOI · Paper page
  170. [179]Grad L.I. Rouleau G.A. Ravits J. Cashman N.R. Clinical spectrum of Amyotrophic Lateral Sclerosis (ALS) Cold Spring Harb. Perspect. Med. 2017 7 a024117 10.1101/cshperspect.a024117 28003278 PMC5538408 · DOI
  171. [180]Park H.R. Yang E.J. Oxidative stress as a therapeutic target in amyotrophic lateral sclerosis: Opportunities and limitations Diagnostics 2021 11 1546 10.3390/diagnostics11091546 34573888 PMC8465946 · DOI
  172. [181]Weiduschat N. Mao X. Hupf J. Armstrong N. Kang G. Lange D.J. Mitsumoto H. Shungu D.C. Motor cortex glutathione deficit in ALS measured in vivo with the J-editing technique Neurosci. Lett. 2014 570 102 107 10.1016/j.neulet.2014.04.020 24769125 · DOI
  173. [182]Andronesi O.C. Nicholson K. Jafari-Khouzani K. Bogner W. Wang J. Chan J. Macklin E.A. Levine-Weinberg M. Breen C. Schwarzschild M.A. Imaging neurochemistry and brain structure tracks clinical decline and mechanisms of ALS in patients Front. Neurol. 2020 11 590573 10.3389/fneur.2020.590573 33343494 PMC7744722 · DOI
  174. [183]Palaiogeorgou A.M. Papakonstantinou E. Golfinopoulou R. Sigala M. Mitsis T. Papageorgiou L. Diakou I. Pierouli K. Dragoumani K. Spandidos D.A. Recent approaches on Huntington’s disease (Review) Biomed. Rep. 2023 18 5 10.3892/br.2022.1587 36544856 PMC9756286 · DOI
  175. [184]Johri A. Beal M.F. Antioxidants in Huntington’s disease Biochim. Biophys. Acta. 2012 1822 664 674 10.1016/j.bbadis.2011.11.014 22138129 PMC3303936 · DOI
  176. [185]Bahmani M. Zargaran A. Rafieian-Kopaei M. Saki K. Ethnobotanical study of medicinal plants used in the management of diabetes mellitus in the Urmia, Northwest Iran Asian Pac. J. Trop. Med. 2014 7 (Suppl. S1) S348 S354 10.1016/S1995-7645(14)60257-1 25312149 · DOI
  177. [186]Rolo A.P. Palmeira C.M. Diabetes and mitochondrial function: Role of hyperglycemia and oxidative stress Toxicol. Appl. Pharmacol. 2006 212 167 178 10.1016/j.taap.2006.01.003 16490224 · DOI · Paper page
  178. [187]Bajaj S. Khan A. Antioxidants and diabetes Indian J. Endocrinol. Metab. 2012 16 S267 S271 10.4103/2230-8210.104057 23565396 PMC3603044 · DOI
  179. [188]Hurrle S. Hsu W.H. The etiology of oxidative stress in insulin resistance Biomed. J. 2017 40 257 262 10.1016/j.bj.2017.06.007 29179880 PMC6138814 · DOI
  180. [189]Søndergård S.D. Cintin I. Kuhlman A.B. Morville T.H. Bergmann M.L. Kjær L.K. Poulsen H.E. Giustarini D. Rossi R. Dela F. The effects of 3 weeks of oral glutathione supplementation on whole body insulin sensitivity in obese males with and without type 2 diabetes: A randomized trial Appl. Physiol. Nutr. Metab. 2021 46 1133 1142 10.1139/apnm-2020-1099 33740389 · DOI
  181. [190]Lutchmansingh F.K. Hsu J.W. Bennett F.I. Badaloo A.V. McFarlane-Anderson N. Gordon-Strachan G.M. Wright-Pascoe R.A. Jahoor F. Boyne M.S. Glutathione metabolism in type 2 diabetes and its relationship with microvascular complications and glycemia PLoS ONE 2018 13 e0198626 10.1371/journal.pone.0198626 29879181 PMC5991679 · DOI
  182. [191]de Souza D.N. de Souza E.M.N. da Silva Pedrosa M. Nogueira F.N. Simoes A. Nicolau J. Effect of tungstate administration on the lipid peroxidation and antioxidant parameters in salivary glands of STZ-induced diabetic rats Biol. Trace Elem. Res. 2021 199 1525 1533 10.1007/s12011-020-02273-x 32596802 · DOI
  183. [192]Zhang J. Bai J. Zhou Q. Hu Y. Wang Q. Yang L. Chen H. An H. Zhou C. Wang Y. Glutathione prevents high glucose-induced pancreatic fibrosis by suppressing pancreatic stellate cell activation via the ROS/TGFbeta/SMAD pathway Cell Death Dis. 2022 13 440 10.1038/s41419-022-04894-7 35523788 PMC9076672 · DOI
  184. [193]Kong H. Chandel N.S. Regulation of redox balance in cancer and T cells J. Biol. Chem. 2018 293 7499 7507 10.1074/jbc.TM117.000257 29282291 PMC5961053 · DOI
  185. [194]He F. Ru X. Wen T. NRF2, a Transcription factor for stress response and beyond Int. J. Mol. Sci. 2020 21 4777 10.3390/ijms21134777 32640524 PMC7369905 · DOI · Paper page
  186. [195]Traverso N. Ricciarelli R. Nitti M. Marengo B. Furfaro A.L. Pronzato M.A. Marinari U.M. Domenicotti C. Role of glutathione in cancer progression and chemoresistance Oxid. Med. Cell. Longev. 2013 2013 972913 10.1155/2013/972913 23766865 PMC3673338 · DOI · Paper page
  187. [197]Grant C. Rahman F. Piekarz R. Peer C. Frye R. Robey R.W. Gardner E.R. Figg W.D. Bates S.E. Romidepsin: A new therapy for cutaneous T-cell lymphoma and a potential therapy for solid tumors Expert Rev. Anticancer Ther. 2010 10 997 1008 10.1586/era.10.88 20645688 PMC6361116 · DOI
  188. [198]Navya P.N. Kaphle A. Srinivas S.P. Bhargava S.K. Rotello V.M. Daima H.K. Current trends and challenges in cancer management and therapy using designer nanomaterials Nano Converg. 2019 6 23 10.1186/s40580-019-0193-2 31304563 PMC6626766 · DOI
  189. [199]Asantewaa G. Harris I.S. Glutathione and its precursors in cancer Curr. Opin. Biotechnol. 2021 68 292 299 10.1016/j.copbio.2021.03.001 33819793 · DOI
  190. [200]Elshorbagy A.K. Jerneren F. Scudamore C.L. McMurray F. Cater H. Hough T. Cox R. Refsum H. Exploring the lean phenotype of glutathione-depleted mice: Thiol, amino acid and fatty acid profiles PLoS ONE 2016 11 e0163214 10.1371/journal.pone.0163214 27788147 PMC5082875 · DOI
  191. [201]Ringel A.E. Drijvers J.M. Baker G.J. Catozzi A. Garcia-Canaveras J.C. Gassaway B.M. Miller B.C. Juneja V.R. Nguyen T.H. Joshi S. Obesity shapes metabolism in the tumor microenvironment to suppress anti-tumor immunity Cell 2020 183 1848 1866.e26 10.1016/j.cell.2020.11.009 33301708 PMC8064125 · DOI · Paper page
  192. [202]Rashida Gnanaprakasam J.N. Wu R. Wang R. Metabolic Reprogramming in modulating T cell reactive oxygen species generation and antioxidant capacity Front. Immunol. 2018 9 1075 10.3389/fimmu.2018.01075 29868027 PMC5964129 · DOI
  193. [203]Labarrere C.A. Kassab G.S. Glutathione: A Samsonian life-sustaining small molecule that protects against oxidative stress, ageing and damaging inflammation Front. Nutr. 2022 9 1007816 10.3389/fnut.2022.1007816 36386929 PMC9664149 · DOI
  194. [204]Muhammad Y. Kani Y.A. Iliya S. Muhammad J.B. Binji A. El-Fulaty Ahmad A. Kabir M.B. Umar Bindawa K. Ahmed A. Deficiency of antioxidants and increased oxidative stress in COVID-19 patients: A cross-sectional comparative study in Jigawa, Northwestern Nigeria SAGE Open Med. 2021 9 2050312121991246 10.1177/2050312121991246 33614035 PMC7871282 · DOI
  195. [205]Kumar P. Osahon O. Vides D.B. Hanania N. Minard C.G. Sekhar R.V. Severe glutathione deficiency, oxidative stress and oxidant damage in adults hospitalized with COVID-19: Implications for GlyNAC (Glycine and N-Acetylcysteine) supplementation Antioxidants 2021 11 50 10.3390/antiox11010050 35052554 PMC8773164 · DOI
  196. [206]Darenskaya M. Rychkova L.V. Semenova N.V. Petrova A. Kolesnikov S.I. Kudeyarova E. Brichagina A. Kolesnikova L. Children and adolescents with COVID-19: Reduced, oxidized glutathione and their ratio level Free. Radic. Biol. Med. 2022 180 s42 10.1016/j.freeradbiomed.2021.12.090 · DOI
  197. [207]Tsermpini E.E. Glamoclija U. Ulucan-Karnak F. Redensek Trampuz S. Dolzan V. Molecular mechanisms related to responses to oxidative stress and antioxidative therapies in COVID-19: A systematic review Antioxidants 2022 11 1609 10.3390/antiox11081609 36009328 PMC9405444 · DOI

Cited by

Sorted by citations

Authors
Vázquez-Meza, H., Vilchis-Landeros, M. M., Vázquez-Carrada, M., Uribe-Ramírez, D., & Matuz-Mares, D.
Affiliations
  • Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, Avenida Universidad 3000, Cd. Universitaria, Coyoacán, Mexico City 04510, Mexico
  • Instituto Politécnico Nacional (MX)
ORCID
Venue
Antioxidants
Publisher
MDPI AG
Published
2023-03-29
Volume
12
Issue
4
Pages
834
ISSN
2076-3921 (ISSN-L)
DOI
10.3390/antiox12040834
PMC
PMC10135322
OpenAlex
W4361267990
Cited by
94
References
8
Citations by year
2026: 35 · 2025: 30 · 2024: 23 · 2023: 6
FWCI
2.17
Type
journal article
Language
en
Open access
Licence
Locations
  • Antioxidants (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • PAPIIT-UNAM (IN-218821)
  • Research Division of the Medical School, UNAM (IN-218821)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
Keywords
glutathione, glutathione transport, cellular compartmentalization, cellular homeostasis, antioxidant function, detoxification, redox signaling, S-glutathionylation, lipid peroxidation, liver, extracellular glutathione

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