Acidic peptides of the lens. 8. <i>S</i>-(<i>α β</i>-dicarboxyethyl) glutathione

Calam, D.H.; Waley, S. G.

doi:10.1042/bj0860226

Cited by 45 publications

(23 citation statements)

References 11 publications

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“…The two substances were measured in separate runs by the present HPLC method, to avoid the problem of overlapping peaks in the stimultaneous determination. Calam & Waley reported that the conoentration of S-(l,2-dicarboxyethyl)glutathione was 30 >1/100 g of calf lens and that of S-(l,2-dicarboxyethyl)L-cysteine was lower (1). This value of S-(l,2-dicarboxyethyl)glutathione in calf lens was about 3 times äs much äs that determined by us.…”

Section: Discussionsupporting

confidence: 49%

S-(1,2-Dicarboxyethyl)glutathione and S-(1,2-Dicarboxyethyl)L-cysteine in Lens

Tsuboi¹,

Uda²,

Ikeda³

et al. 1984

Clinical Chemistry and Laboratory Medicine

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Summary: S-(l,2-Dicarboxyethyl)glutathione and S-(l,2-dicarboxyethyl)L-cysteine were determined by high performance liquid chromatography after reaction with 2,4-dinitrofluorobenzene. By this method the former could be determined in the r nge 4.05 μπιοΙ/1-815 μιηοΐ/ΐ, and the latter in the r nge 1.45 μιηοΐ/ΐ-1.45 mmol/1. The recovery from cattle lens homogenate was 90.0 ± 3.2% for S-(l,2-dicarboxyethyl)glutathione and 95.3 ± 3.1% for S-(l,2-dicarboxyethyl)L-cysteine. Using this method S-(l,2-dicarboxyethyl)-glutathione and S-(l,2-dicarboxyethyl)L-cysteine were determined in ienses of several vertebrates and in rat lens during cataract formation by galactose. S*(l,2-Dicarboxyethyl)glutathion und S-(l,2-Dicarboxyethyl)L-cystein in der Linse des AugesZusammenfassung: S-(l,2-Dicarboxyethyl)gIutathion und S-(l,2-Dicarboxyethyl)L-cystein wurden mit Hochleistungsfl ssigkeitschromatographie nach Reaktion mit 2,4-Dinitrofl orobenzol bestimmt. Mit diesem Verfahren konnte das Erste schon ab 4,05 μπιοΐ/ΐ bis zu 815 μπιοΐ/ΐ, und das Letztere ab 1,45 μτηοΐ/ΐ bis zu 1,45 mmol/1 bestimmt werden. Die Wiederfindung aus dem Hoinogenat von Rinderlinsen betrug 90,0 ± 3,2% f r S-(l,2-Dicarboxyethyl)glutathion und 95,3 ± 3,1% f r S-(l,2-Dicarboxyethyl)L-cystein. Unter Verwendung dieses Verfahrens wurden S-(l,2-Dicarboxyethyl)glutathion und S-(l,2-Dicarboxyethyl)L-cystein in den Linsen mehrerer Wirbeltiere und in Rattenlinsen w hrend der Katarakt-Bildung mit Galaktose bestimmt. Introd ction

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Section: Discussionsupporting

confidence: 49%

S-(1,2-Dicarboxyethyl)glutathione and S-(1,2-Dicarboxyethyl)L-cysteine in Lens

Tsuboi¹,

Uda²,

Ikeda³

et al. 1984

Clinical Chemistry and Laboratory Medicine

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“…S-(1,2-dicarboxyethyl)glutathione is typically found in the lens in considerable amounts (Calam and Waley, 1963). In the present study, it was detected in the cortex of normal and control lenses, and its abundance increased following HBO treatment, presumably due to an increase in either L-malate or fumarate, which are substrates for GSH-dependent formation of S-(1,2-dicarboxyethyl)glutathione (Tsuboi et al, 1990).…”

Section: Discussionmentioning

confidence: 99%

Spatial distributions of glutathione and its endogenous conjugates in normal bovine lens and a model of lens aging

Nye-Wood

Spraggins

Caprioli

et al. 2017

Experimental Eye Research

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Glutathione (GSH) is the archetypal antioxidant, and plays a central role in the protection of the ocular lens from cataract formation. High levels of GSH are maintained in the transparent lens, but with advancing age, GSH levels fall in the lens nucleus relative to outer cortical cells, thereby exposing the nucleus of the lens to the damaging effects of oxygen radicals, which ultimately leads to age-related nuclear (ARN) cataract. Under normal conditions, GSH also forms endogenous conjugates to detoxify the lens of reactive cellular metabolites and to maintain cell homeostasis. Due to the intrinsic gradient of lens fibre cell age, the lens contains distinct regions with different metabolic requirements for GSH. To investigate the impact of fibre cell and lens aging on the varied roles that GSH plays in the lens, we have utilised high mass resolution MALDI mass spectrometry profiling and imaging analysis of lens tissue sections. High Dynamic Range (HDR)-MALDI FTICR mass spectrometry was used as an initial screening method to detect regional differences in lens metabolites from normal bovine lenses and in those subjected to hyperbaric oxygen as a model of lens aging. Subsequent MALDI imaging analysis was used to spatially map GSH and its endogenous conjugates throughout all lenses. Accurate mass measurement by MALDI FTICR analysis and LC-MS/MS mass spectrometry of lens region homogenates were subsequently used to identify endogenous GSH conjugates. While the distribution and relative abundance of GSH-related metabolic intermediates involved in detoxification pathways remained relatively unchanged upon HBO treatment, those involved in its antioxidant function were altered under conditions of oxidative stress. For example, reduced glutathione levels were decreased in the lens cortex while oxidised glutathione levels were elevated in the lens outer cortex upon HBO treatment. Interestingly, cysteineglutathione disulfide, was detected in the inner cortex of the normal lens, but was greatly decreased in the HBO-treated lenses. These results contribute to our understanding of the multiple roles that GSH plays in maintenance of lens transparency and in the age-related metabolic changes that lead to lens cataract formation.

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“…The administration of maleic acid into rats has been reported to increase urinary excretion of this compound and the binding of maleic acid to tissue proteins [18]. Moreover, a free thiol group of cysteine is slowly alkylated in a solution containing maleic acid or fumaric acid to form S-(I ,2-dicarboxyethyl)-~-cysteine [14]. Modified mutant human lysozyme was produced in S. cerevisiue when mono[tris(hydroxymethyl)-aminomethane] maleate was added to the culture medium as one of buffer components, but not when it was excluded from the culture medium.…”

Section: Discussionmentioning

confidence: 99%

Occurrence of S‐(1,2‐dicarboxyethyl)‐cysteine at position 77 in mutant human lysozyme secreted by Saccharomyces cerevisiae

Kikuchi

Taniyama

Kanaya

et al. 1990

European Journal of Biochemistry

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A mutant human lysozyme PI1', in which Val110 was replaced with Pro, was secreted by Succharomyces cerevisiae; modification of the cysteine residue at position 77 was found in a purified mutant protein (Pl'O-B) upon primary structure analysis. A peptide fragment containing 15 amino acid residues from Thr70 to Leu84 was obtained by proteolytic digestion of the protein and subsequently isolated by reverse-phase HPLC. This fragment was analyzed by high-resolution fast-atom-bombardment (FAB) mass spectrometry, which showed that 1,2-dicarboxyethyl group was attached to the thiol group of Cys77. This modification was confirmed by comparing it with a sample of chemically synthesized S-(l,2-dicarboxyethyl)-~-cysteine.It was found that the modification caused a disruption of the disulfide bond Cys77-Cys95 in the mutant molecule. These observations, plus structural considerations, suggest that Cys77 and Cys95 either remain uncrosslinked or the disulfide bond Cys77 -Cys95, once formed, is opened during the final step in the folding of human lysozyme in vivo.

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Acidic peptides of the lens. 8. S-(α β-dicarboxyethyl) glutathione

Cited by 45 publications

References 11 publications

S-(1,2-Dicarboxyethyl)glutathione and S-(1,2-Dicarboxyethyl)L-cysteine in Lens

S-(1,2-Dicarboxyethyl)glutathione and S-(1,2-Dicarboxyethyl)L-cysteine in Lens

Spatial distributions of glutathione and its endogenous conjugates in normal bovine lens and a model of lens aging

Occurrence of S‐(1,2‐dicarboxyethyl)‐cysteine at position 77 in mutant human lysozyme secreted by Saccharomyces cerevisiae

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