Thioltransferases

Wells, William W.; Yang, Yanfeng; Deits, Thomas L.; Gan, Zhong-Ru

doi:10.1002/9780470123126.ch4

Cited by 49 publications

(38 citation statements)

References 177 publications

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“…These thiol functions typically catalyse thiol-disulfide exchange reactions, but some glutaredoxins are also capable of simultaneously binding iron and glutathione, forming [2Fe-2S] clusters which are shared between two subunits of a homodimer (Fig. 8) (Wells et al 1993;Mesecke et al 2008). These [2Fe-2S] clusters can be transferred to a range of acceptor proteins (Rouhier et al 2009;Li et al 2009;Qi and Cowan 2011) and are reported to be responsible for the channelling of iron to the mitochondrion (Lillig et al 2008;Rouhier et al 2009).…”

Section: Resultsmentioning

confidence: 93%

“…Glutathione facilitates cytoplasmic iron/sulphur cluster assembly (Sipos et al 2002, Sharma et al 2010. Glutaredoxins are widely distributed; being found in virus particles, bacteria, yeast, plants and mammals (Wells et al 1993). They are small proteins which possess a GSH binding site and a redox active thiol function, both of which are located on the surface of the protein.…”

Section: Resultsmentioning

confidence: 99%

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Glutathione: a key component of the cytoplasmic labile iron pool

2011

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The cytoplasmic labile iron pool supplies iron to the mitochondrion for heme and iron sulfur cluster synthesis and to many cytoplasmic enzymes, thereby controlling numerous metabolic reactions. Surprisingly the chemical nature of this pool has never been convincingly characterised. Here we provide evidence for iron(II)glutathione being the dominant component of this pool. We report for the first time the affinity constant for the glutathione-iron(II) interaction and use this value to study the cytoplasmic speciation of iron(II). The formation of this complex is a major determinant of the electrode potential of the cytoplasmic ferrous iron pool, a means of selecting between iron(II) and manganese(II) and it provides a substrate for glutaredoxin/iron clusters at the dimer interface of glutaredoxins involved in the synthesis of Fe-S cluster proteins.

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Section: Resultsmentioning

confidence: 93%

Section: Resultsmentioning

confidence: 99%

Glutathione: a key component of the cytoplasmic labile iron pool

2011

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“…Two glutaredoxin (Glrx) genes have been characterized in mammals. The Glrx1 gene encodes the cytosolic enzyme Grx1 [23]. The second Glrx (Glrx2) gene encodes two proteins as a result of alteration of RNA splicing.…”

Section: Introductionmentioning

confidence: 99%

Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia

Xiong

et al. 2007

Free Radical Biology and Medicine

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To understand the physiological function of glutaredoxin, a thiotransferase catalyzing the reduction of mixed disulfides of protein and glutathione (protein-SSG), we generated a line of knockout mice deficient in the cytosolic glutaredoxin 1 (Grx1). To our surprise, mice deficient in Grx1 were not more susceptible to acute oxidative insults in models of heart and lung injury induced by ischemia/ reperfusion and hyperoxia, respectively; suggesting that changes in S-glutathionylation status of cytosolic proteins are not the major cause of such tissue injury. On the other hand, mouse embryonic fibroblasts (MEFs) isolated from Grx1-deficient mice displayed an increased vulnerability to diquat and paraquat, but they were not more susceptible to cell death induced by hydrogen peroxide (H 2 O 2 ) and diamide. A deficiency in Grx1 also sensitized MEFs to protein S-glutathionylation in response to H 2 O 2 treatment and retarded deglatuthionylation of the S-glutathionylated proteins, especially evident for an unspecified protein of approximately 44 kDa. Additional experiments showed that MEFs lacking Grx1 were more tolerant to apoptosis induced by tumor necrosis factor α plus actinomycin D. These findings suggest that different oxidants may damage the cells via distinct mechanisms in which Grx1-dependent de-glutathionylation may or may not be protective, and Grx1 may exert its function on specific target proteins.

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“…This group includes thioltransferase (glutaredoxin [GRX]), thioredoxin (TRX), and protein disulfide isomerase (437). Whereas TRX and protein disulfide isomerase have broad substrate specificities (289), GRX specifically reduces GSHcontaining mixed disulfides with greater efficiency than TRX (153,289).…”

Section: Catalasementioning

confidence: 99%

Reactive Oxygen Species in the Regulation of Synaptic Plasticity and Memory

Massaad

Klann

2011

Antioxidants & Redox Signaling

495

350

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The brain is a metabolically active organ exhibiting high oxygen consumption and robust production of reactive oxygen species (ROS). The large amounts of ROS are kept in check by an elaborate network of antioxidants, which sometimes fail and lead to neuronal oxidative stress. Thus, ROS are typically categorized as neurotoxic molecules and typically exert their detrimental effects via oxidation of essential macromolecules such as enzymes and cytoskeletal proteins. Most importantly, excessive ROS are associated with decreased performance in cognitive function. However, at physiological concentrations, ROS are involved in functional changes necessary for synaptic plasticity and hence, for normal cognitive function. The fine line of role reversal of ROS from good molecules to bad molecules is far from being fully understood. This review focuses on identifying the multiple sources of ROS in the mammalian nervous system and on presenting evidence for the critical and essential role of ROS in synaptic plasticity and memory. The review also shows that the inability to restrain either age-or pathology-related increases in ROS levels leads to opposite, detrimental effects that are involved in impairments in synaptic plasticity and memory function.

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Thioltransferases

Cited by 49 publications

References 177 publications

Glutathione: a key component of the cytoplasmic labile iron pool

Glutathione: a key component of the cytoplasmic labile iron pool

Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia

Reactive Oxygen Species in the Regulation of Synaptic Plasticity and Memory

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