The antioxidant system of the respiratory tract. The intracellular antioxidant protection in the respiratory tract (part 5)

А.E. Abaturov, A.P. Volosovets, T.P. Borysova

Abstract


The literature review presents the current data about the glutaredoxin system in the functioning of the intracellular antioxidant protection in the respiratory tract. The paper dwells upon the details of glutaredoxin-dependent oxidation reaction.


Keywords


antioxidant system; respiratory tract; intracellular antioxidant protection; review

References


Abaturov AE, Volosovets AP, Borysova TP. The Antioxidant System of the Respiratory Tract the Intracellular Antioxidant Protection in the Respiratory Tract (Part 2). Zdorov’e rebenka. 2016;6(74):121-7. doi: 10.22141/2224-0551.6.74.2016.82144. (in Russian).

Kalinina EV, Chernov NN, Saprin AN. Part tio peroxide and glutaredoxins in cellular redox-dependent processes. Uspehi biologicheskoy himii. 2008;48:319-31. (in Russian).

Asmis R, Wang Y, Xu L, Kisgati M, Begley JG, Mieyal JJ. A novel thiol oxidation-based mechanism for adriamycin-induced cell injury in human macrophages. FASEB J. 2005 Nov;19(13):1866-8. doi: 10.1096/fj.04-2991fje. Epub 2005 Sep 13.

Aesif SW, Anathy V, Kuipers I, Guala AS, Reiss JN, Ho YS, Janssen-Heininger YM. Ablation of glutaredoxin-1 attenuates lipopolysaccharide-induced lung inflammation and alveolar macrophage activation. Am J Respir Cell Mol Biol. 2011 Apr;44(4):491-9. doi: 10.1165/rcmb.2009-0136OC. Epub 2010 Jun 10.

Reynaert NL, van der Vliet A, Guala AS, et al. Dynamic redox control of NF-kappa B through glutaredoxin-regulated S-glutathionylation of inhibitory kappa B kinase beta. Proc Natl Acad Sci USA. 2006 Aug 29;103(35):13086-91. doi: 10.1073/pnas.0603290103. Epub 2006 Aug 17.

Peltoniemi M, Kaarteenaho-Wiik R, Säily M, et al. Expression of glutaredoxin is highly cell specific in human lung and is decreased by transforming growth factor-beta in vitro and in interstitial lung diseases in vivo. Hum Pathol. 2004 Aug;35(8):1000-7. PMID: 15297967.

Rouhier N, Couturier J, Johnson MK, Jacquot JP. Glutaredoxins: roles in iron homeostasis. Trends Biochem Sci. 2010 Jan;35(1):43-52. doi: 10.1016/j.tibs.2009.08.005. Epub 2009 Oct 5.

Chung S, Sundar IK, Yao H, Ho YS, Rahman I. Glutaredoxin 1 regulates cigarette smoke-mediated lung inflammation through differential modulation of I{kappa}B kinases in mice: impact on histone acetylation. Am J Physiol Lung Cell Mol Physiol. 2010 Aug;299(2):192-203. doi: 10.1152/ajplung.00426.2009. Epub 2010 May 14.

Yang SR, Valvo S, Yao H, et al. IKK alpha causes chromatin modification on pro-inflammatory genes by cigarette smoke in mouse lung. Am J Respir Cell Mol Biol. 2008 Jun;38(6):689-98. doi: 10.1165/rcmb.2007-0379OC. Epub 2008 Jan 31.

Lillig CH, Berndt C, Holmgren A. Glutaredoxin systems. Biochim Biophys Acta. 2008 Nov;1780(11):1304-17. doi: 10.1016/j.bbagen.2008.06.003. Epub 2008 Jun 18.

Mieyal JJ, Gallogly MM, Qanungo S, Sabens EA, Shelton MD. Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid Redox Signal. 2008 Nov;10(11):1941-88. doi: 10.1089/ars.2008.2089.

Prasad VR, Tripathi BN, Sethumadhavan R. Distinct role of non-covalent interactions to the function and structural stability of glutaredoxins: a multifunctional redox protein. Int J Bioinform Res Appl. 2010;6(3):241-59. doi: 10.1504/IJBRA.2010.034073.

Ahsan MK, Lekli I, Ray D, Yodoi J, Das DK. Redox regulation of cell survival by the thioredoxin superfamily: an implication of redox gene therapy in the heart. Antioxid Redox Signal. 2009 Nov;11(11):2741-58. doi: 10.1089/ARS.2009.2683.

Johansson C, Kavanagh KL, Gileadi O, Oppermann U. Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria. J Biol Chem. 2007 Feb 2;282(5):3077-82. doi: 10.1074/jbc.M608179200. Epub 2006 Nov 22.

Reynaert NL, Wouters EF, Janssen-Heininger YM. Modulation of glutaredoxin-1 expression in a mouse model of allergic airway disease. Am J Respir Cell Mol Biol. 2007 Feb;36(2):147-51. doi: 10.1165/rcmb.2006-0259RC. Epub 2006 Sep 15.

Shelton MD, Mieyal JJ. Regulation by reversible S-glutathionylation: molecular targets implicated in inflammatory diseases. Mol Cells. 2008 May 31;25(3):332-46. Epub 2008 May 16. PMCID: PMC3367451.

Johansson C, Roos AK, Montano SJ, et al. The crystal structure of human GLRX5: iron-sulfur cluster co-ordination, tetrameric assembly and monomer activity. Biochem J. 2011 Jan 15;433(2):303-11. doi: 10.1042/BJ20101286.

Holmgren A, Johansson C, Berndt C, Lönn ME, Hudemann C, Lillig CH. Thiol redox control via thioredoxin and glutaredoxin systems. Biochem Soc Trans. 2005 Dec;33(Pt 6):1375-7. doi: 10.1042/BST20051375.




DOI: https://doi.org/10.22141/2224-0551.12.1.2017.95035

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