ライフサイエンスコーパス: GSSG

1 GSSG adsorbed on native, -NH2-functionalized, and -SO3H-

2 GSSG export by MRP1 leads to a perturbation of endotheli

3 GSSG is likely to bind via the carboxylate groups of one

4 GSSG levels were, however, similar between all study gro

5 GSSG oxidizes copper-coordinating cysteines of Atox1 wit

6 analogues of the analytes ((310)GSH and (616)GSSG), along with N-ethylmaleimide (NEM), and treated wi

7 of glutathione biosynthesis and accumulated GSSG in the mitochondria.

8 ance-associated protein-1 (MRP-1), an active GSSG efflux mechanism, showed 2-fold increased activity

9 phenic acid, glutathione sulphinic acid, and GSSG are rather reaction intermediates.

10 yledons and older leaves yellowed early, and GSSG, the oxidized form of glutathione, accumulated in t

11 Our results portray the role of GSH and GSSG as markers of oxidative stress in live organisms un

12 We used quantitative GSH and GSSG biosensors to monitor glutathione import into the E

13 Fasting plasma GSH and GSSG concentrations were measured to calculate the GSH/G

14 as calculated to be -171 mV based on GSH and GSSG concentrations.

15 These data demonstrate that GSH and GSSG contamination must be accounted for when determinin

16 iciency of photosystem II, decreased GSH and GSSG contents, and the ratio of GSH to GSSG.

17 rat liver samples demonstrated that GSH and GSSG coprecipitated with proteins similar to the range f

18 de was used for the determination of GSH and GSSG in rat urine and plasma samples, intoxicated or not

19 by day 56; concomitantly, levels of GSH and GSSG increased in both cytosol and mitochondria.

20 The lowest detection for GSH and GSSG is 0.103 nM in a 96-well plate.

21 ing is shown to occur when the total GSH and GSSG is close to 1 mM, whereas pool sizes below 0.9 mM r

22 For GSH and GSSG measurement, the sample was spiked with isotopicall

23 is based on the masking of GSH in a GSH and GSSG mixture via a 1,4-addition reaction with p-benzoqui

24 -dependent chemical modifications on GSH and GSSG that are caused by dielectric barrier discharge und

25 2.1% to 7.9%, and accuracy values of GSH and GSSG were 96% and 105%, respectively.

26 the detection of total glutathione (GSH and GSSG).

27 t of intracellular concentrations of GSH and GSSG, and the calculation of Eh using the Nernst equatio

28 h for reliable detection of cellular GSH and GSSG.

29 Measurements of Cys, CySS, GSH, and GSSG were used with the Nernst equation to calculate the

30 ited by 45 and 98% the formation of GSNO and GSSG, respectively.

31 formation of GAPDH-SSG, compared to GSNO and GSSG.

32 likely depends on ER glutathione import and GSSG export.

33 hearts showed more normal levels of mRNA and GSSG.

34 ctrocatalytic activity for GSH oxidation and GSSG reduction, enabling the simultaneous detection of b

35 nucleotide disulfide oxidoreductase, Trx and GSSG reductase (TGR), that exhibits specificity for both

36 ell as products of oxidative stress (such as GSSG and 4-HNE) generated by these enzymes, induced neut

37 lfoxide, dimethylformamide, and methanol, at GSSG concentrations as low as 1.5 mM.

38 N-Acetyl cysteine attenuated GSSG elevation and diamide-induced apoptosis.

39 t associations between As exposure and blood GSSG or plasma Cys.

40 The orientation of particle bound GSSG was assessed by the release of glutathione after re

41 ects of the composition of the redox buffer, GSSG and GSH, on folding has not been extensively invest

42 h a 3-fold stimulation of ATPase activity by GSSG.

43 Inhibition of the Na,K-ATPase by GSSG did not occur in the presence of ATP at concentrati

44 ys-264 were specifically glutathionylated by GSSG.

45 e conclude that the inactivation of GmPTP by GSSG is regulated at two levels.

46 as in both cases enhanced by H2O2 but not by GSSG, indicating that the intermediate sulfenylation is

47 The currents were also suppressed by GSSG and the thiol oxidants pyridine disulfides (PDSs),

48 e to inactivate the enzyme when thiolated by GSSG or alkylated with iodoacetamide.

49 We found that GRx catalyzes GSSG formation in the presence of GS-thiyl radical gener

50 althy murine aortic endothelial (MAE) cells, GSSG/GSH was over twice as high in EOMA cells.

51 GPX1-/- than in WT cells, and corresponding GSSG accumulation occurred only in the latter.

52 ssential role of the DmTrx system in cycling GSSG/GSH and maintaining the intracellular redox homeost

53 Consistent with the location of Cys158, GSSG inhibited the channel only when the channel was ope

54 wer glutathione (GSH)/glutathione disulfate (GSSG) ratio was associated with the decreased activity,

55 lutathione (GSH), and glutathione disulfide (GSSG) and calculated E(h) according to the Nernst equati

56 e of GSH oxidation to glutathione disulfide (GSSG) and decrease of the GSH/GSSG ratio.

57 conditions, 0.125 mM glutathione disulfide (GSSG) and no glutathione (GSH), the folding pathway of B

58 transporters of GSH, glutathione disulfide (GSSG) and/or GSH conjugates (GS-X).

59 after the addition of glutathione disulfide (GSSG) but not GSH.

60 lectively transported glutathione disulfide (GSSG) but not reduced glutathione in agreement with a 3-

61 m of the reduction of glutathione disulfide (GSSG) by the reduced a domain of human protein disulfide

62 The glutathione disulfide (GSSG) formed can be recycled to GSH by glutathione reduc

63 yzes the reduction of glutathione disulfide (GSSG) into reduced glutathione (GSH).

64 In healthy cells, glutathione disulfide (GSSG) is rapidly reduced back to glutathione (GSH) by gl

65 glutathione (GSH) and glutathione disulfide (GSSG) levels were measured by high-performance liquid ch

66 al disulfides such as glutathione disulfide (GSSG) oxidize MT with concomitant release of zinc, while

67 ) or a mixture of GSH/glutathione disulfide (GSSG) potentiated platelet aggregation.

68 ced glutathione (GSH)/glutathione disulfide (GSSG) ratio.

69 rs, glutathione (GSH)/glutathione disulfide (GSSG) ratios, and activation of stress-response transcri

70 Glutathione disulfide (GSSG) reductase (GR) activity was not altered.

71 yzes the reduction of glutathione disulfide (GSSG) to reduced glutathione (GSH) with the accompanying

72 Glutathione disulfide (GSSG) was not transported in either Cyd(+) or Cyd(-) str

73 ion of divalent anion glutathione disulfide (GSSG) was undetectable.

74 glutathione (GSH) and glutathione disulfide (GSSG) were measured by HPLC.

75 on of glutathione and glutathione disulfide (GSSG), which was used for the determination of PSSG in b

76 of the model peptide glutathione disulfide (GSSG).

77 ecies, thus producing glutathione disulfide (GSSG).

78 nificant increases in glutathione disulfide (GSSG)/glutathione (GSH), a marker of oxidative stress, c

79 ng and liver GSH and oxidized GSH disulfide (GSSG) levels were measured on days 0 and 5 and glutathio

80 reduced glutathione (GSH) to its disulfide (GSSG) and promotes the formation of protein-glutathione

81 ed glutathione [GSH], glutathione disulfide [GSSG], and total glutathione [tGSH]) and plasma von Will

82 lutathione (GSH) and glutathione disulphide (GSSG) forms the most important redox buffer in organisms

83 assay, glutathione (GSH) levels by the DTNB-GSSG reductase method, apoptosis, reactive oxygen specie

84 ameters indicative of oxidative stress (i.e. GSSG and steady-state levels of oxygen-centered radicals

85 and is not directly influenced by endogenous GSSG reductase activity.

86 idative stress by metabolizing extracellular GSSG, while GGT2 might be important in transporting glut

87 We find GSSG, S-oxidised glutathione species, and S-nitrosogluta

88 The Michaelis constants (K(m)) for GSSG and beta-NADPH were found to be 40 +/- 11 and 4.4 +

89 on limits of 100 muM for GSH and 8.3 muM for GSSG, respectively.

90 O2 production on the reduction potential for GSSG/2GSH exists between -150 and -300 mV.

91 orrelated with decreases in NADPH supply for GSSG reduction.

92 A hyperactive MRP-1 system for GSSG efflux acts as a critical survival factor for these

93 ioxidant thiol, its oxidized disulfide form (GSSG), and their redox state (E(h) GSH/GSSG), and 2) cys

94 d glutathione (GSH), over its oxidized form (GSSG), and glutathione reductase (GR) in human serum.

95 uced glutathione (GSH) to its oxidized form (GSSG).

96 n that regenerates the free enzyme and forms GSSG.

97 e GSH synthesis and regeneration of GSH from GSSG.

98 yme involved in the regeneration of GSH from GSSG.

99 ne (GSH) and oxidized disulfide glutathione (GSSG) in cell extracts and isolated mitochondria as a me

100 resence of the oxidized form of glutathione (GSSG), except in the presence of the enzyme glutathione

101 P6), reduced (GSH) and oxidised glutathione (GSSG) contents, antioxidant and reducing capacity and Ma

102 lpha after 4 hours and oxidized glutathione (GSSG) after 8 hours indicated development of oxidative s

103 well as the amount of oxidized glutathione (GSSG) and 4-hydroxynonenal (4-HNE) in airway-lining flui

104 ed a rapid increase in oxidized glutathione (GSSG) and a loss of mitochondrial cytochrome c in 15-30

105 Determinations of oxidized glutathione (GSSG) and reduced glutathione (GSH) were performed in mo

106 tracellularly [altered oxidized glutathione (GSSG) and reduced glutathione levels and ratio; increase

107 hibition was seen with oxidized glutathione (GSSG) and thiol-modulating reagents.

108 Glutathione (GSH) and oxidized glutathione (GSSG) control cellular function and efficiency of antica

109 MT-2 with an excess of oxidized glutathione (GSSG) increased metal donation fourfold, whereas reduced

110 of the Na,K-ATPase to oxidized glutathione (GSSG) resulted in an increase in the number of S-glutath

111 lyzes the reduction of oxidized glutathione (GSSG) to GSH in the presence of beta-NADPH (beta-nicotin

112 increased recycling of oxidized glutathione (GSSG) to reduced glutathione (GSH), which is due to the

113 glutathione (GSH) and oxidized glutathione (GSSG) were linear over more than four orders of magnitud

114 glutathione (GSH) and oxidized glutathione (GSSG) were measured by HPLC.

115 from the formation of oxidized glutathione (GSSG) within the interior of the vesicle, the appearance

116 s of reduced (GSH) and oxidized glutathione (GSSG), and it enables the calculation of the GSH:GSSG ra

117 levels, via increased oxidized glutathione (GSSG), induce isoform-specific S-glutathionylation of 6-

118 had elevated levels of oxidized glutathione (GSSG), resulting in a dramatic change in the ELF redox s

119 ted by the presence of oxidized glutathione (GSSG).

120 fully reactivated with oxidized glutathione (GSSG).

121 significantly elevated oxidized glutathione (GSSG).

122 entrapped GSH to form oxidized glutathione (GSSG).

123 of increased levels of oxidized glutathione (GSSG).

124 8 h, without change in oxidized glutathione (GSSG); no effect was seen in pure glial cultures.

125 ed glutathione (GSH)]/[oxidized glutathione (GSSG)] ratio was significantly decreased, whereas the di

126 the sum of oxidized and reduced glutathione (GSSG and GSH) can be measured with essentially no additi

127 he ratio of oxidised to reduced glutathione (GSSG/GSH).

128 of responses to applied reduced glutathione, GSSG and MRP1 inhibitors (indomethacin, MK571) further s

129 tripeptide glutathione (gamma-glu-cys-gly) (GSSG) is shown to produce transparent, thermoreversible

130 Oxidized GSH (GSSG) can be recycled to GSH by the GSH reductase or exp

131 ADPH via Trx reductase (TR) or oxidized GSH (GSSG) reductase and further supply electrons for deoxyri

132 subcellular redox state using oxidized GSH (GSSG) reductase localization mutants.

133 SH adducts with cell-permeable oxidized GSH (GSSG-ethyl ester) or 2-acetylamino-3-[4-(2-acetylamino-2

134 lity of the total glutathione content (GSH + GSSG) and GSH in saliva is significantly greater than in

135 Using HPLC-BDD and -UV, hepatic GSH, GSSG, and GSH/GSSG from mice (r=0.64-0.94) and rats (r=0

136 d in families that have a known role in GSH, GSSG, and/or GS-X transport was employed to help identif

137 ndividing cells had lower intracellular GSH, GSSG, and GSH/GSSG and a more oxidized redox potential (

138 Blood glutathione levels (GSH, GSSG, and tGSH) were lower (P < 0.001, P = 0.039, and P

139 in- and between-day precision values of GSH, GSSG, and GSH/GSSG were 2.1% to 7.9%, and accuracy value

140 Concentrations of GSH, GSSG, Cys, and CySS were measured using HPLC.

141 Exposure of complex I to oxidized GSH, GSSG, resulted in specific S-glutathiolation at the 51 k

142 d hepatic DNA oxidation damage, aberrant GSH/GSSG profiles, and altered activation patterns for AP-1.

143 ater extent in the autism LCLs, although GSH/GSSG and ATP concentrations were similarly decreased in

144 s had lower intracellular GSH, GSSG, and GSH/GSSG and a more oxidized redox potential (E(h)).

145 HPLC-BDD and -UV, hepatic GSH, GSSG, and GSH/GSSG from mice (r=0.64-0.94) and rats (r=0.79-0.92) were

146 and p66(shc), coupled with low AGER1 and GSH/GSSG levels, insulin resistance, marked myocardial and r

147 tively by DCF fluorescence intensity and GSH/GSSG ratio, and promoted ERK1/2 phosphorylation (P<0.001

148 Cys/CySS and GSH/GSSG redox states in human plasma undergo diurnal variat

149 E(h) of Cys/CySS and GSH/GSSG was -120 to -20 and -200 to -50 mV, respectively.

150 n-day precision values of GSH, GSSG, and GSH/GSSG were 2.1% to 7.9%, and accuracy values of GSH and G

151 tial and intracellular levels of GSH and GSH/GSSG.

152 dox status was systematically clamped at GSH/GSSG ratios ranging from 300:1 to 20:1.

153 in human breast cancer cells attenuated GSH/GSSG, total GSH, nuclear factor erythroid 2-related fact

154 Reliable detection of cellular GSH/GSSG is challenging due to their ultralow concentration

155 ce a progressive decline in the cellular GSH/GSSG ratio, in parallel with a linear increase in newly

156 The glutathione redox couple, GSH/GSSG, oscillated in parallel with DeltaPsi(m) and the NA

157 ine whether the redox state of GSH, Cys, GSH/GSSG, or Cys/CySS undergoes diurnal variation in healthy

158 ed apoptosis associated with a decreased GSH/GSSG ratio, augmented nuclear factor erythroid-related f

159 creases the HSP-FRET ratio and decreases GSH/GSSG, indicating an increase in oxidant stress.

160 lasma glutathione/glutathione disulfide (GSH/GSSG) and cysteine/cystine (Cys/CySS) couples are oxidiz

161 t the glutathione/glutathione disulfide (GSH/GSSG) pair controls the copper transport pathway by regu

162 lular glutathione/glutathione disulfide (GSH/GSSG) potential at the redox boundary between cellular d

163 Elevated GSH/GSSG ratio (especially in mitochondria), decreased LPO a

164 ne beta-synthase (CBS) promotes elevated GSH/GSSG.

165 CML levels, via Nrf2 pathway, enhancing GSH/GSSG ratio, heme oxygenase-1 and glyoxalase 1 in liver t

166 atio of reduced to oxidized glutathione (GSH/GSSG) as well as a pro-oxidizing shift in the calculated

167 educed glutathione/oxidized glutathione (GSH/GSSG) ratio and oxidative damage of mitochondrial DNA (m

168 atio of reduced to oxidized glutathione (GSH/GSSG), chlorophyll content, photosynthesis and related g

169 atio of reduced to oxidized glutathione (GSH/GSSG), in a well-controlled study of twins.

170 rements of reduced/oxidized glutathione (GSH/GSSG), to assess cytosolic redox responses in cultured p

171 atio of reduced to oxidized glutathione (GSH/GSSG).

172 racellular vitamin C, glutathione (GSH), GSH/GSSG, and NAD(P)H/NAD(P)+ ratios, as well as oxidant app

173 1), CySS (r = 0.18, p = 0.049), and E(h) GSH/GSSG (r = 0.34, p < 0.0002) correlated with IMT.

174 E(h) GSH/GSSG predicted IMT in a manner that was both independent

175 ional risk factors and hs-CRP, only E(h) GSH/GSSG remained an independent predictor of IMT.

176 Glutathione redox state (E(h) GSH/GSSG), an in vivo measure of intracellular oxidative str

177 form (GSSG), and their redox state (E(h) GSH/GSSG), and 2) cysteine (Cys), an important extracellular

178 et score was associated with a 7% higher GSH/GSSG ratio (P = 0.03) after adjustment for energy intake

179 ed with a 10% (95% CI: 2.7, 18.0) higher GSH/GSSG ratio in the twin with the higher score than in the

180 ant decrease in intracellular GSH and in GSH/GSSG ratios.

181 in cardiomyocytes and that intermediate GSH/GSSG ratios cause reversible DeltaPsi(m) depolarization,

182 accompanied by an increase in intraislet GSH/GSSG ratio (control, 7.1 +/- 0.1; 10 ng/ml IL-1 beta, 8.

183 long-term caloric restriction, had lower GSH/GSSG ratios and higher protein-mixed disulfides than age

184 dox couples (NADH/NAD(+), NADPH/NADP(+), GSH/GSSG, Trx(SH)(2)/TrxSS).

185 The ratio of GSH/GSSG has been used as an indicator of oxidative stress.

186 With a ratio of GSH/GSSG of 5/1, similar to that of blood, the addition of G

187 glutathione/glutathione-disulfide ratio (GSH/GSSG) and/or the reduced/oxidized thioredoxin ratio.

188 ered glutathione reduced/oxidized ratio (GSH/GSSG) similar to MDs, human myopathies, and neurogenic a

189 ed the cellular glutathione redox ratio (GSH/GSSG).

190 and reduced/oxidized glutathione ratios (GSH/GSSG) and increased cell sensitivity to oxidative stress

191 Carbon monoxide (CO) reduced GSH/GSSG in three breast cancer cell lines by inhibiting CBS

192 The results indicate that GSH/GSSG redox status governs the sequential opening of mito

193 iently oxidized (>90 mV) relative to the GSH/GSSG (-250 mV) and thioredoxin (Trx1, -280 mV) redox cou

194 The calculated redox states of the GSH/GSSG and Cys/CySS couples varied in association with the

195 0, whereas the respective values for the GSH/GSSG couple occurred at 0330 and 1330.

196 al resulted in a greater decrease in the GSH/GSSG ratio and increase in free radical generation in au

197 vely old mice (17 months), increased the GSH/GSSG ratio and redox potential at 19 months in the same

198 mitant increase in the total GSH and the GSH/GSSG ratio was also observed; the NAD(P)H/NAD(P)+ ratio

199 akfast reduced plasma GSH levels and the GSH/GSSG ratio, increased protein carbonyl levels, and induc

200 act dose and with minimal decline in the GSH/GSSG ratio, whereas MAP kinase activation required a hig

201 levated oxidative stress detected by the GSH/GSSG ratio.

202 were the levels of NADPH, NADH, and the GSH/GSSG ratio.

203 ntrations were measured to calculate the GSH/GSSG ratio.

204 one disulfide (GSSG) and decrease of the GSH/GSSG ratio.

205 However, the GSH/GSSG redox pair can efficiently couple with the MT/thion

206 The results indicated that the GSH/GSSG redox ratio was decreased and percentage oxidized g

207 er was retained; however, decreasing the GSH/GSSG to 50:1 irreversibly depolarized DeltaPsi(m) and in

208 uction of GSSG to GSH to maintain a high GSH:GSSG ratio.

209 alone sufficient to reduce intracellular GSH:GSSG ratio and cause eNOS S-glutathionylation.

210 ant proteins showed that as the ratio of GSH:GSSG decreased significant S-glutathionylation occurred

211 izes the in vitro underestimation of the GSH:GSSG ratio arising from the degradation of GSH and forma

212 ), and it enables the calculation of the GSH:GSSG ratios in human plasma and saliva samples.

213 O] ratio and to be independent of the [GSH]/[GSSG] ratio.

214 xidizing glutathione redox potential, E(hc) (GSSG/2GSH), respectively.

215 hich is reflected by low GSH levels and high GSSG levels and significant glutathionylation of mitocho

216 thiol redox switch), and a +10 mV change in GSSG/2GSH reduction potential.

217 thiol redox switches, and a -25 mV change in GSSG/2GSH reduction potential.

218 dative stress without significant changes in GSSG/GSH ratios indicates that assays of ubiquitination

219 he brain regions examined, and elevations in GSSG amount that were most pronounced in the striatum an

220 alpha and GSH with a significant increase in GSSG and in pro-fibrogenic transforming growth factor be

221 25% GSH reduction, and a 5-fold increase in GSSG in 20 min.

222 th decreases in GSH and Cys and increases in GSSG and CySS (i.e., a more oxidized environment).

223 TNF-alpha levels after 4 hours and increased GSSG after 8 hours of reperfusion, AdvBcl-2-treated hear

224 oxygen tensions decreased GSNO and increased GSSG formation.

225 extracellular oxidants but not intracellular GSSG.

226 trapeptide serves a role of a protein-linked GSSG and shuttles electrons from the disulfide center wi

227 of the pentose phosphate pathway maintained GSSG elevation and accelerated cell apoptosis.

228 ative stress shown by elevated mitochondrial GSSG/GSH and protein carbonyls.

229 lds more efficiently in the presence of 5 mM GSSG and 5 mM GSH than it does under traditional conditi

230 However, with 5 mM GSSG and 5 mM GSH the formation of the double mixed disu

231 he use of [(13)C2,(5)N]GSH and [(13)C4,(5)N2]GSSG validated these results and demonstrated that the r

232 dant enzyme glutathione reductase (GR; NADPH+GSSG+H(+) <==> NADP(+)+2 GSH) has become an attractive d

233 GSH but not GSSG also inhibited rhinovirus-induced ICAM-1 promoter a

234 d with a progressive increase in GSx but not GSSG in the culture medium.

235 s, compared with in the cytosol, the nuclear GSSG/GSH ratio was 5-fold higher.

236 ibition as well as knockdown trapped nuclear GSSG, causing cell death of EOMA.

237 Addition of GSSG or 4-HNE to Amb a 1 challenge material boosted alle

238 1, similar to that of blood, the addition of GSSG potentiated the stimulatory effect as compared to G

239 The addition of GSSG to platelets generated sulfhydryls in the beta subu

240 ry efficient, even at high concentrations of GSSG or GSH.

241 d with the addition of low concentrations of GSSG to the GSH.

242 -NDH) decreased in parallel as the dosage of GSSG increased.

243 ve a heavy oxidant burden by rapid efflux of GSSG, which is lethal if trapped within the cell.

244 llatory shear also caused a robust export of GSSG that was prevented by the MRP1 inhibitor MK571 and

245 RP1) and use this as their major exporter of GSSG.

246 from the degradation of GSH and formation of GSSG.

247 The fractions of GSSG were 0.2-2.2% (RBC and blood) and 15-47% (saliva) o

248 Disulfide loading of cells by inhibition of GSSG reductase (bischoloronitrosourea) or thioredoxin re

249 y by cytosolic and mitochondrial isoforms of GSSG reductase.

250 miao accumulates high levels of GSSG and exhibits increased glutathione oxidation.

251 e proteins in the presence of high levels of GSSG in conditions of oxidative stress.

252 olated from old donors had a higher ratio of GSSG to GSH.

253 storation of GSH levels through reduction of GSSG and deglutathionylation of mitochondrial proteins.

254 e used to observe the enzymatic reduction of GSSG to GSH in real time.

255 The enzyme catalyzes the reduction of GSSG to GSH to maintain a high GSH:GSSG ratio.

256 tional GSH biosynthesis and the reduction of GSSG.

257 and converts the gamma-glutamyl residues of GSSG to 5-hydroxybutyrolactam.

258 direct incorporation of biotinylated GSH or GSSG into the purified recombinant p53 protein was obser

259 controlled by the presence of either GSH or GSSG.

260 lasting reductions in glutathione oxidation (GSSG/GSH) and remarkably concordant nitrite-induced card

261 emonstrate that HOCl and chloramines oxidize GSSG to two irreversible products in high yield.

262 activity, converting reduced GSH to oxidized GSSG with concomitant scrubbing of ambient dissolved O2

263 electrode toward reduced (GSH) and oxidized (GSSG) forms of glutathione was assessed by CV studies at

264 utathione in its reduced (GSH) and oxidized (GSSG) forms.

265 accurately quantify reduced (GSH), oxidized (GSSG) and total (tGSH) glutathione in biological samples

266 e found that reduced (GSH) but not oxidized (GSSG) glutathione (1-100 microM) inhibited in a dose-dep

267 electrochemical quantification of oxidized (GSSG) and reduced glutathione (GSH), biomarkers of oxida

268 ore, the ratio of reduced (GSH) to oxidized (GSSG) glutathione was also increased suggesting a role f

269 ondria with respiratory substrates prevented GSSG formation and, consequently, ATP synthase glutathio

270 one peroxidase/glutathione reductase (GSH-Px/GSSG-R) functions, protein expression of gamma-glutamylc

271 Glutathione oxidized/reduced ratio (GSSG/GSH) was increased in the blood of exposed animals,

272 es in GSH reductase, an enzyme that recycles GSSG back to GSH, both in vitro and in vivo.

273 ion to its normal functions, it also reduces GSSG for antioxidant protection.

274 Since GSSG cannot be reduced in the ER, maintenance of the ER

275 ropose that in appropriate organic solvents, GSSG self-assembles into an extended network of beta-she

276 ely, 45 or 90 atomic mass units lighter than GSSG.

277 We here report that GSSG, when added to platelets alone, also potentiates pl

278 A biotin switch assay shows that GSSG-ester-induced HIF-1alpha contains reversibly modifi

279 is associated with an oxidising shift in the GSSG/GSH redox potential and is inhibited by the antioxi

280 In addition, dissociation of the GSSG product is inhibited by TriCHQ.

281 Most of the GSSG was converted to GSH by a flavoprotein-dependent pl

282 he release of glutathione after reducing the GSSG disulfide bond and by zeta potential measurements.

283 effects of NOV-002 can be attributed to the GSSG component of the drug, and modulation of cellular r

284 eophilic attack of the Cys53-thiolate to the GSSG-disulfide followed by the deprotonation of Cys56-th

285 Thus, GSSG adsorption and orientation can be tailored by varyi

286 reby facilitating the conversion of GS(.) to GSSG or transfer of GS(.) to form protein-SSG.

287 ts or for a redox potential (ratio of GSH to GSSG), aggregation was further studied with the addition

288 and correction for auto-oxidation of GSH to GSSG.

289 H and GSSG contents, and the ratio of GSH to GSSG.

290 NDH), the flavin subcomplex of complex I, to GSSG resulted in specific S-glutathiolation on the 51 kD

291 and promotes glutathione (GSH) oxidation to GSSG.

292 Up to 3% GSH was auto-oxidized to GSSG during sample workup; the highest oxidations (>1%)

293 se, consisting of diminished GSH relative to GSSG, decreased potential to reduce protein-SSG mixed di

294 ate, consisting of increased GSH relative to GSSG, increases in type 1 and type 2 thiol redox switche

295 The rat alpha2 isoform was more sensitive to GSSG than the alpha1 isoform.

296 to native and -NH2-modified alumina, whereas GSSG is suggested to bind to -SO3H-modified alumina via

297 The mechanism by which GSSG is exported and the consequence of its export from

298 lyceraldehyde-3-phosphate dehydrogenase with GSSG or S-nitrosoglutathione, but these glutathionyl don

299 diamide or incubating cellular extracts with GSSG oxidized PTEN in a manner similar to that of CSNO.

300 cobalamin by a second molecule of GSH yields GSSG.