GSSGPeroxidaseCysteineProteinSynthesisHydrogen peroxideProteinsOxidative StressReductase deficiencyBondsGlutathionylationCompoundsOxidoreductasePeroxidasesPeptidesDeficiencyAlbuminDimethylTripeptideHydroperoxidesAntioxidant defenseMoleculesSupplementationCysteinesImmunocalEnzyme1988Reduction1990MolecularModificationSupplementalCardiovascularSubsequentZincExposureImportanceUrineCompoundLevelsImportantBody
GSSG5
- Glutathione disulfide (GSSG) is a disulfide derived from two glutathione molecules. (wikipedia.org)
- Antioxidant enzymes, such as glutathione peroxidases and peroxiredoxins, generate glutathione disulfide during the reduction of peroxides such as hydrogen peroxide (H2O2) and organic hydroperoxides (ROOH): 2 GSH + ROOH → GSSG + ROH + H2O Other enzymes, such as glutaredoxins, generate glutathione disulfide through thiol-disulfide exchange with protein disulfide bonds or other low molecular mass compounds, such as coenzyme A disulfide or dehydroascorbic acid. (wikipedia.org)
- GSSG, along with glutathione and S-nitrosoglutathione (GSNO), have been found to bind to the glutamate recognition site of the NMDA and AMPA receptors (via their γ-glutamyl moieties), and may be endogenous neuromodulators. (wikipedia.org)
- Glutathione peroxidase oxidizes GSH to glutathione disulfide (GSSG) with concomitant formation of H20 from H2O2. (loinc.org)
- It is a central enzyme of cellular antioxidant defense, and reduces oxidized glutathione disulfide (GSSG) to the sulfhydryl form GSH, which is an important cellular antioxidant. (nih.gov)
Peroxidase4
- The protein encoded by this gene belongs to the glutathione peroxidase family, members of which catalyze the reduction of organic hydroperoxides and hydrogen peroxide (H2O2) by glutathione, and thereby protect cells against oxidative damage. (nih.gov)
- In the resveratrol + As 2 O 3 -treated group, activities of glutathione peroxidase, catalase, and superoxide dismutase, the ratio of reduced glutathione to oxidized glutathione, the total arsenic concentrations, and the percentage of methylated arsenic in urine were significantly increased. (springer.com)
- To be replicated, HIV must compete with its host for glutathione peroxidase and its four constituent nutrients: selenium, cysteine, glutamine and tryptophan. (life-enthusiast.com)
- To illustrate, glutathione peroxidase is one of the body's most significant antioxidants. (life-enthusiast.com)
Cysteine6
- Supplementation with glutathione, a cysteine-containing antioxidative tripeptide, normalized hepatic glutathione redox state modulated by ingestion of 3% CN diet, but it only reversed the oxidized shift of plasma albumin redox state to an extent similar to cystine alone or the constituting amino acid mixture of glutathione (i.e., glutamic acid, cystine, and glycine), indicating that glutathione would primarily serve as a source of cysteine rather than exert its antioxidative activity. (frontiersin.org)
- Immunotec's proprietary manufacturing process preserves the critical disulfide bonds in the glutathione precursor cysteine. (immunotec.com)
- Cysteine, glutathione and albumin thiols reduced TETD with subsequent mixed disulfide formation suggesting a potential route of protein haptenation. (cdc.gov)
- In response to reactive oxygen species (ROS), glutathione plays an important role in redox signaling by forming a disulfide bond with protein cysteine residues, known as glutathionylation. (thieme-connect.com)
- Reducing agents cysteine, glutathione and dithiothreitol in the concentration range of 10 µM-10 mM diminished binding of [ 3 H]3-quinuclidinyl benzilate ([ 3 H]3-QNB) to in situ muscarinic receptor sites of membranes from rat cerebral cortex. (aspetjournals.org)
- Cysteine is then metabolized to sulfite, taurine, and glutathione. (msdmanuals.com)
Protein1
- By delivering this delicate protein to the cell, it enables the body to create glutathione and maximize immune system levels. (immunotec.com)
Synthesis5
- Sulfur is required for the synthesis of glutathione, one of our premier endogenous antioxidants. (marksdailyapple.com)
- Firstly, the oxidized form of cysteamine inhibits glutathione synthesis therefore regulating glutathione levels in tissues. (univ-mrs.fr)
- Although most Americans consume an adequate supply of dietary precursors for GSH {glutathione} synthesis, there is a gap between the amount synthesized and the amount needed (i.e., a decline in GSH is associated with disease risk). (preparedfoods.com)
- Other nutrients can aid in maintaining glutathione status (such as zinc and selenium, which play a role in glutathione synthesis). (preparedfoods.com)
- Supplemental cys from either source supports glutathione synthesis. (mysite.com)
Hydrogen peroxide1
- Oxidation of ZDEC by bleach, iodine or hydrogen peroxide resulted in production of TETD, tetraethylthiocarbamoyl disulfide (TETCD) and tetraethyldicarbamoyl disulfide (TEDCD). (cdc.gov)
Proteins3
- CoDEC does not bind to Cu-proteins or form mixed disulfides with free thiols demonstrating the importance of these properties in ZDEC sensitization. (cdc.gov)
- It is concluded that ZDEC may haptenize proteins through (1) chelation of metals on metalloproteins, (2) TETD mediated formation of mixed disulfides, and (3) possibly through nucleophilic addition onto an TEDCD electrophilic carbamoyl group. (cdc.gov)
- I was wondering if anyone has used a glutathione analog in which the sulfhydral group is blocked to elude bound GST-fusion proteins from a GSH-Sepharose Chromatography Column (Pharmacia). (bio.net)
Oxidative Stress3
- Lead inactivates glutathione by binding to GSH's sulfhydryl group, which causes GSH replenishment to become inefficient, thereby increasing oxidative stress. (medscape.com)
- People that are under oxidative stress, such as smokers, alcoholics and diabetics, have lower levels of glutathione and elevated levels of glutathione disulphide. (preparedfoods.com)
- Therefore, supplementation with amino acids and N-acetylcysteine to increase glutathione in the body will likely only benefit individuals that do not consume enough of these amino acids or who are under oxidative stress. (preparedfoods.com)
Reductase deficiency1
- Rare mutations in this gene result in hereditary glutathione reductase deficiency. (nih.gov)
Bonds3
- Sulfur, in the form of disulfide bonds, provides strength and resiliency to hair, feathers, and feathered hair . (marksdailyapple.com)
- Reduced glutathione (GSH) is currently used, but it binds to our peptides via two disulfide bonds to two cysteines in our target peptide. (bio.net)
- Glycosaminoglycans are the building blocks of joint cartilage, and these molecules are connected with disulfide bonds (the bonding of two sulfur atoms). (springtimeinc.com)
Glutathionylation3
- AtSAL1 phosphatase activity is suppressed by dimerization, intramolecular disulfide formation, and glutathionylation, allowing accumulation of its substrate, PAP, a chloroplast stress retrograde signal that regulates expression of plastid redox associated nuclear genes (PRANGs). (nih.gov)
- Reversible modification of cysteines such as disulfide bond formation, glutathionylation, and nitrosylation may also be a means of protection from further, generally irreversible, modifications to sulfinic (-SO 2 H) or sulfonic (-SO 3 H) acids [ 9 ]. (hindawi.com)
- We briefly review the roles of glutathione, ROS, and glutathionylation in redox regulation. (thieme-connect.com)
Compounds1
- Additionally, items such as milk, blueberries, bottled apple juice and tea contain glutathione-reactive compounds that reduce the amount of glutathione present in food or lining of the small intestine. (preparedfoods.com)
Oxidoreductase1
- This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. (nih.gov)
Peroxidases1
- therefore, by limiting H2O2 accumulation, glutathione peroxidases are also involved in modulating these processes. (nih.gov)
Peptides1
- 2006). The LLNA is based upon characterization of chemicals comprising allergens of different potencies and non- induced proliferative responses in draining lymph nodes allergenic chemicals were evaluated for their ability to react with following topical exposure of mice to chemicals (Gerberick reduced glutathione (GSH) or with two synthetic peptides et al. (cdc.gov)
Deficiency1
- Increased oxidant burden and antioxidant, e.g. glutathione (GSH), deficiency in the lower respiratory tract have been thought to play a role in the progression of IPF. (ersjournals.com)
Albumin1
- Albumin with a free thiol on Cys34 is the reduced form and designated as mercaptalbumin (MA), while the isoforms with oxidized Cys34, such as a mixed disulfide with low molecular weight thiols and sulfinic/sulfonic acid, are the oxidized forms, which are designated as non-mercaptalbumin (NA)-1 and NA-2, respectively. (frontiersin.org)
Dimethyl3
- Rate constants for the reaction of hydroxyl radicals with carbonyl sulfide, carbon disulfide and dimethyl thioether over the temperature range 299-430 K. (cdc.gov)
- The other constituents of note are low molecular weight sulfur-containing constituents, dimethyl sulfide, dimethyl disulfide and methyl mercaptan, The Boundary Composition for the registration substance limits the total amount of sulfur-containing constituents to 6% by weight expressed as sulfur. (europa.eu)
- For worker exposure, the approach used is to consider whole substance (based on pinene data) and sulfides (based on dimethyl disulfide data) (Section 9.0). (europa.eu)
Tripeptide1
- The tripeptide glutathione (l-y-glutamyl-l-cysteinyl-glycine, GSH) plays a pivotal role in metabolic and cell-cycle related functions in virtually all cells. (ersjournals.com)
Hydroperoxides1
- A selenoenzyme that converts GLUTATHIONE plus FATTY ACID HYDROPEROXIDES to GLUTATHIONE DISULFIDE plus hydroxy fatty acids and water. (bvsalud.org)
Antioxidant defense1
- Ninety percent of glutathione in the cell exists in reduced form and 10% in oxidative form, and it typically acts as an antioxidant defense mechanism. (medscape.com)
Molecules2
- In living cells, glutathione disulfide is reduced into two molecules of glutathione with reducing equivalents from the coenzyme NADPH. (wikipedia.org)
- As a thiol-containing metabolite, cysteamine is suspected to engage disulfide bridges with target molecules. (univ-mrs.fr)
Supplementation3
- Animal research with glutathione supplementation has indicated improvements in immune function, 2 protection against oxidant injury in newborn lungs, 3 reduction in the uptake of oxidized lipids 4 and protection against other toxic chemicals. (preparedfoods.com)
- 5 Human research has shown that glutathione from raw fruits and vegetables is associated with a reduced risk of oral cancer 6 and supplementation with glutathione can prevent nephrotoxicity associated with cancer treatment. (preparedfoods.com)
- 7 Clinical trials are needed to confirm glutathione supplementation and the proposed associated health benefits seen in animal studies. (preparedfoods.com)
Cysteines1
- We suspect that the cysteines form a native disulfide bond in the absence of GSH and DTT. (bio.net)
Immunocal1
- Immunocal works by providing important glutathione precursors to the cell. (immunotec.com)
Enzyme1
- This reaction is catalyzed by the enzyme glutathione reductase. (wikipedia.org)
19881
- 1988. Neurological examination, computerized- tomography, cerebral blood-flow and neuropsychological examination in workers with long-term exposure to carbon disulfide. (cdc.gov)
Reduction1
- Dual-targeted glutathione reductase 2 defines a bottleneck for reduction of glutathione disulfide only in plastids. (elsevierpure.com)
19901
- 1990. Carbon disulfide exposure and neurotoxic sequelae among viscose rayon workers. (cdc.gov)
Molecular1
- Glutathione (GSH) is an important low molecular weight thiol compound that is synthesized in cells. (loinc.org)
Modification1
- Modification of thiol-disulfide state of receptor may be involved in the control of binding activity. (aspetjournals.org)
Supplemental1
- Research has indicated that supplemental glutathione results in increased plasma glutathione levels in humans, despite an expected degradation that may occur in the intestine. (preparedfoods.com)
Cardiovascular2
- 1985. Effect of carbon disulphide on the cardiovascular system. (cdc.gov)
- Elevated levels of glutathione disulfide are associated with increased carotid intima media thickness, a measurement of the thickness of artery walls and an indication of cardiovascular disease risk. (preparedfoods.com)
Subsequent1
- Glutathione donates electrons to oxidants to sequester, or squelch, their free radical activity, helping to prevent DNA damage and subsequent chronic disease. (preparedfoods.com)
Zinc1
- Zinc diethyldithiocarbamate (ZDEC) and its disulfide, tetraethylthiuram disulfide (TETD) are rubber accelerant contact allergens that cross-react in some individuals. (cdc.gov)
Exposure1
- 1992. Regional cerebral blood flow after long-term exposure to carbon disulfide. (cdc.gov)
Importance1
- 1980. Measurements of emission rates of carbon disulfide from biogenic sources and its possible importance to the stratospheric aerosol layer. (cdc.gov)
Urine1
- Homocysteine accumulates and dimerizes to form the disulfide homocystine, which is excreted in the urine. (msdmanuals.com)
Compound1
- March 2011 -Glutathione is an endogenously produced compound that protects the body against the bombardment of free radicals. (preparedfoods.com)
Levels4
- Research has observed lower levels of glutathione in adults over 45 years old, in comparison to younger people. (preparedfoods.com)
- Elevated levels of glutathione disulphide are an indication of a large utilization of glutathione and are often observed in individuals over the age of 45. (preparedfoods.com)
- Processing, such as canning, curing and drying significantly reduce glutathione levels present in food. (preparedfoods.com)
- Maintains high levels of reduced glutathione in the cytosol. (nih.gov)
Important1
- The results suggested that a disulfide bond, which could be reduced and reoxidized, may play an important role in ligand binding. (aspetjournals.org)
Body2
- ROS are stabilized by glutathione in the body. (medscape.com)
- Glutathione disulphide, the oxidized form of glutathione that has already reacted with a free radical, is also present in the body. (preparedfoods.com)