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    GLRX2 glutaredoxin 2 [ Homo sapiens (human) ]

    Gene ID: 51022, updated on 2-May-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Glutaredoxin 2 Protein (Grx2) as an Independent Prognostic Factor Associated with the Survival of Colon Adenocarcinoma Patients.

    Glutaredoxin 2 Protein (Grx2) as an Independent Prognostic Factor Associated with the Survival of Colon Adenocarcinoma Patients.
    Brzozowa-Zasada M, Piecuch A, Bajdak-Rusinek K, Gołąbek K, Michalski M, Janelt K, Matysiak N., Free PMC Article

    02/28/2024
    By sensing the overall cellular redox conditions, mitochondrial Grx2 dimers become active monomers upon oxidative stress induced by sodium selenite with the consequent release of the iron-sulfur cluster, leading to activation of the intrinsic apoptotic pathway.

    Dimers of glutaredoxin 2 as mitochondrial redox sensors in selenite-induced oxidative stress.
    Scalcon V, Tonolo F, Folda A, Bindoli A, Rigobello MP.

    05/30/2020
    GRX2 is important in the control of cardiac mitochondrial structure and function, and protects against human cardiac pathologies.

    Glutaredoxin-2 controls cardiac mitochondrial dynamics and energetics in mice, and protects against human cardiac pathologies.
    Kanaan GN, Ichim B, Gharibeh L, Maharsy W, Patten DA, Xuan JY, Reunov A, Marshall P, Veinot J, Menzies K, Nemer M, Harper ME., Free PMC Article

    07/21/2018
    Study shows that Grx2 detoxifies *NO in mature oligodendrocytes and oligodendroglial precursor cellsvia the formation of dinitrosyl-iron-complexes, inhibiting the formation of harmful peroxynitrite and reducing subsequent oligodendroglial damage. Findings link inorganic biochemistry to neuroinflammation and identify glutaredoxin 2 as a protective factor against neuroinflammation-mediated myelin damage.

    Iron-sulfur glutaredoxin 2 protects oligodendrocytes against damage induced by nitric oxide release from activated microglia.
    Lepka K, Volbracht K, Bill E, Schneider R, Rios N, Hildebrandt T, Ingwersen J, Prozorovski T, Lillig CH, van Horssen J, Steinman L, Hartung HP, Radi R, Holmgren A, Aktas O, Berndt C.

    04/14/2018
    Grx2 and Trx1 contribute significantly to neuronal integrity and could be clinically relevant in neuronal damage following perinatal asphyxia and other neuronal disorders.

    Thioredoxin 1 and glutaredoxin 2 contribute to maintain the phenotype and integrity of neurons following perinatal asphyxia.
    Romero JI, Hanschmann EM, Gellert M, Eitner S, Holubiec MI, Blanco-Calvo E, Lillig CH, Capani F.

    09/5/2015
    The Grx2 system could help to keep Trx2/1 reduced during an oxidative stress, thereby contributing to the anti-apoptotic signaling.

    Glutaredoxin 2 reduces both thioredoxin 2 and thioredoxin 1 and protects cells from apoptosis induced by auranofin and 4-hydroxynonenal.
    Zhang H, Du Y, Zhang X, Lu J, Holmgren A., Free PMC Article

    04/25/2015
    These results suggest that Grx2a plays proliferative and anti-apoptotic roles under serum deprivation.

    Glutaredoxin 2a, a mitochondrial isoform, plays a protective role in a human cell line under serum deprivation.
    Kim SJ, Jung HJ, Choi H, Lim CJ.

    08/14/2013
    Grx2 thiol redox regulation is essential for vertebrate embryonic development

    Vertebrate-specific glutaredoxin is essential for brain development.
    Bräutigam L, Schütte LD, Godoy JR, Prozorovski T, Gellert M, Hauptmann G, Holmgren A, Lillig CH, Berndt C., Free PMC Article

    03/10/2012
    Exchange of [2Fe-2S] centers between glutaredoxin 2 and the cluster scaffold protein ISU, supports a direct link for glutaredoxin 2 and glutathione involvement in ISU promoted Fe-S cluster biosynthesis.

    Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange.
    Qi W, Cowan JA.

    08/13/2011
    Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3.

    Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3.
    Hanschmann EM, Lönn ME, Schütte LD, Funke M, Godoy JR, Eitner S, Hudemann C, Lillig CH., Free PMC Article

    01/29/2011
    Observational study of gene-disease association. (HuGE Navigator)

    Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
    Hendrickson SL, Lautenberger JA, Chinn LW, Malasky M, Sezgin E, Kingsley LA, Goedert JJ, Kirk GD, Gomperts ED, Buchbinder SP, Troyer JL, O'Brien SJ., Free PMC Article

    12/5/2010
    Studies indicate that the mechanism of Grx2 protection against H(2)O(2)-induced apoptosis is likely associated with its ability to preserve complex I.

    Glutaredoxin 2 prevents H(2)O(2)-induced cell apoptosis by protecting complex I activity in the mitochondria.
    Wu H, Xing K, Lou MF., Free PMC Article

    10/30/2010
    cluster signal of Grx2 is stable at positive potentials up to 0.5 V but that cluster destruction occurs readily when oxidative pulses in excess of this value are applied

    Oxidative disassembly of the [2Fe-2S] cluster of human Grx2 and redox regulation in the mitochondria.
    Mitra S, Elliott SJ.

    01/21/2010
    Grx1 and Grx2 exhibit key catalytic similarities, including selectivity for protein-SSG substrates and a nucleophilic, double-displacement, monothiol mechanism exhibiting a strong commitment to catalysis.

    Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: implications for intracellular roles.
    Gallogly MM, Starke DW, Leonberg AK, Ospina SM, Mieyal JJ., Free PMC Article

    01/21/2010
    Grx2 is constitutively expressed in both neuron and glia in mouse and human brain including the neurons in human substantia nigra.

    Constitutive expression and functional characterization of mitochondrial glutaredoxin (Grx2) in mouse and human brain.
    Karunakaran S, Saeed U, Ramakrishnan S, Koumar RC, Ravindranath V.

    01/21/2010
    Human Grx2 is found to be a conserved feature within the deuterostomes and appears to be the only additional conserved intramolecular disulfide within the glutaredoxins.

    Redox properties and evolution of human glutaredoxins.
    Sagemark J, Elgán TH, Bürglin TR, Johansson C, Holmgren A, Berndt KD.

    01/21/2010
    characterization of Grx2 as an iron-sulfur center-containing member of the thioredoxin fold protein family

    Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor.
    Lillig CH, Berndt C, Vergnolle O, Lönn ME, Hudemann C, Bill E, Holmgren A., Free PMC Article

    01/21/2010
    Eficence of an iron-sulfur cluster in which binding of the cluster inactivates the protein by sequestering active site residues and where loss of the cluster through changes in subcellular redox status creates a catalytically active protein.

    Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria.
    Johansson C, Kavanagh KL, Gileadi O, Oppermann U.

    01/21/2010
    results suggest an important role for glutaredoxin 2 in protection and recovery from oxidative stress

    Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase.
    Johansson C, Lillig CH, Holmgren A.

    01/21/2010
    The iron-sulfur cluster is complexed by the two N-terminal active site thiols of two Grx2 monomers and two molecules of glutathione that are bound noncovalently to the proteins and in equilibrium with glutathione in solution.

    How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2?
    Berndt C, Hudemann C, Hanschmann EM, Axelsson R, Holmgren A, Lillig CH.

    01/21/2010
    Lung cells can synthesize Grx2 mRNA and protein.

    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.
    Peltoniemi M, Kaarteenaho-Wiik R, Säily M, Sormunen R, Pääkkö P, Holmgren A, Soini Y, Kinnula VL.

    01/21/2010
    Grx2 has a novel function as a peroxidase, accepting electrons both from GSH and TR. This unique property may play a role in protecting the mitochondria from oxidative damage.

    Mitochondrial thioltransferase (glutaredoxin 2) has GSH-dependent and thioredoxin reductase-dependent peroxidase activities in vitro and in lens epithelial cells.
    Fernando MR, Lechner JM, Löfgren S, Gladyshev VN, Lou MF.

    01/21/2010
    Grx1 and Grx2 were present in placenta extracts and in cell lysates prepared from tumor cell lines; however, the levels of Grx1 were at least 20 times higher than those of Grx2; Grx2 was not detected in plasma from healthy blood donors

    Cellular and plasma levels of human glutaredoxin 1 and 2 detected by sensitive ELISA systems.
    Lundberg M, Fernandes AP, Kumar S, Holmgren A.

    01/21/2010
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