Everything below concerns redox balance. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Updated 2025-11-18. Numbers and descriptions here follow the published literature rather than marketing material.
In cells, glutathione exists mainly in a reduced form called GSH. When two GSH molecules react, they form oxidized glutathione, or GSSG, which contains a disulfide bond. The ratio of GSH to GSSG is often used as an indicator of oxidative stress. Enzymes such as glutathione peroxidase and glutathione reductase help cycle the molecule between these two states. This cycling supports antioxidant defense, detoxification of reactive molecules, and regulation of certain signaling pathways.
Glutathione is present in most tissues, with especially high concentrations in the liver. It also serves as a cofactor for some enzymes and helps transport amino acids across cell membranes. In plants and microorganisms, glutathione contributes to stress responses and metal handling. The molecule is synthesized in two ATP-dependent steps, first producing gamma-glutamylcysteine and then adding glycine. Because cysteine availability often limits synthesis, dietary and metabolic factors can influence glutathione levels. Research continues to examine how these levels relate to health and disease.
Within cells, glutathione serves as a cofactor for glutathione peroxidases and glutathione S-transferases. These enzymes reduce hydrogen peroxide and organic peroxides or conjugate electrophilic compounds to the thiol group. The resulting conjugates can be exported and processed through mercapturic acid pathways. Glutathione also contributes to protein thiol homeostasis and to recycling of other antioxidants such as ascorbate. Its precise roles vary by tissue, and many regulatory effects observed in laboratory systems remain difficult to quantify in whole organisms.
Glutathione is a tripeptide composed of glutamate, cysteine, and glycine. It occurs in nearly all living cells, with highest concentrations in liver, kidney, and red blood cells, and exists in reduced (GSH) and oxidized disulfide (GSSG) forms. The cysteine thiol group enables reversible oxidation and reduction reactions. This property makes glutathione a central participant in cellular redox balance. The balance between these forms is often used as an indicator of oxidative stress.
| Property | Value | Notes |
|---|---|---|
| Common name | Glutathione | Tripeptide of glutamate, cysteine, and glycine |
| Reduced form | GSH | Dominant intracellular thiol |
| Oxidized form | GSSG | Disulfide-linked dimer |
| Molar mass | 307.32 g/mol | For reduced glutathione |
| Functional motif | Gamma-glutamyl-cysteinyl-glycine | Gamma linkage resists many peptidases |
Biosynthesis proceeds in two ATP-dependent steps. First, glutamate-cysteine ligase joins glutamate and cysteine. Second, glutathione synthetase adds glycine to the intermediate. The pathway is regulated by cysteine availability, enzyme expression, and feedback inhibition by glutathione itself. Liver tissue has a particularly high capacity for synthesis and export. Because the molecule is made inside cells, circulating glutathione reflects a balance of release, uptake, and breakdown rather than simple dietary supply.
Functionally, glutathione supports redox balance by donating electrons and becoming oxidized. It also serves as a cofactor for enzymes such as glutathione peroxidases and glutathione S-transferases. These enzymes participate in peroxide reduction and in conjugation reactions that help process reactive molecules. Separate from antioxidant roles, glutathione can modify protein cysteines through S-glutathionylation, influencing enzyme activity and signaling. Research continues to examine how these chemical roles translate into whole-organism effects.
Glutathione supports several cellular processes beyond direct antioxidant action. It serves as a cofactor for glutathione peroxidase and glutathione S-transferase enzymes, which reduce peroxides and conjugate electrophiles, respectively. The molecule also acts as a reservoir of cysteine, an amino acid that can limit protein synthesis and redox signaling. In human nutrition, oral glutathione is sold as a supplement, but how much intact glutathione reaches tissues after ingestion remains an active research question. Clinical claims about supplementation are not uniformly supported by controlled trials.
Glutathione is a small tripeptide built from glutamic acid, cysteine, and glycine. Its peptide bond between glutamate and cysteine involves the gamma-carboxyl group rather than the usual alpha-carboxyl group. This structure gives the molecule a reactive thiol on the cysteine residue. The reduced form, often abbreviated GSH, is the predominant intracellular species in many cell types. Because the thiol can donate electrons, glutathione participates in redox chemistry and in the conjugation of reactive molecules.
Interpreting glutathione measurements requires attention to pre-analytical variables. The GSSG concentration in a sample can rise artificially during storage or processing, making the GSH/GSSG ratio unreliable if not controlled. Reference ranges vary by specimen type, assay, and population, so comparisons across studies are difficult. Plasma glutathione is low and sensitive to hemolysis, while whole blood reflects primarily erythrocyte content. Many studies measure total glutathione rather than the reduced and oxidized forms separately, which limits conclusions about redox status.
Accurate measurement of glutathione begins with careful sample handling. Because GSH oxidizes rapidly to GSSG, samples must be processed quickly or frozen immediately. Acid precipitation with metaphosphoric acid or perchloric acid is common; it lowers pH, precipitates proteins, and helps preserve the reduced form. Chelating agents such as EDTA can limit metal-catalyzed oxidation. For whole blood, hemolysis releases glutathione from erythrocytes, so plasma and serum values differ substantially from whole blood values.
== Diagnosis == Research on prenatal diagnosis has shown that a diagnosis can be made prenatally in approximately 50% of fetuses presenting arthrogryposis. It could be found during routine ultrasound scanning showing a lack of mobility and abnormal position of the foetus. There are other options for visualization of details and structures using techniques such as 4D ultrasound. In clinic a child can be diagnosed with arthrogryposis with physical examination, confirmed by ultrasound, MRI, or muscle biopsy.
==== Chromium ==== Clinical and experimental studies have reported antidepressant activity of chromium particularly in atypical depression, characterized by increased appetite and carbohydrate craving.
Strychnine poisoning in animals usually occurs from ingestion of baits designed for use against gophers, rats, squirrels, moles, chipmunks and coyotes. Strychnine is also used as a rodenticide, but is not specific to such unwanted pests and may kill other small animals. In the United States, most baits containing strychnine have been replaced with zinc phosphide baits since 1990. In the European Union, rodenticides with strychnine have been forbidden since 2006. Some animals are immune to strychnine; usually these have evolved resistance to poisonous strychnos alkaloids in the fruit they eat, such as fruit bats. The drugstore beetle has a symbiotic gut yeast that allows it to digest pure strychnine. Strychnine toxicity in rats is dependent on sex. It is more toxic to females than to males when administered via subcutaneous injection or intraperitoneal injection. Differences are due to higher rates of metabolism by male rat liver microsomes. Dogs and cats are more susceptible among domestic animals, pigs are believed to be as susceptible as dogs, and horses are able to tolerate relatively large amounts of strychnine. Birds affected by strychnine poisoning exhibit wing droop, salivation, tremors, muscle tenseness, and convulsions. Death occurs as a result of respiratory arrest. The clinical signs of strychnine poisoning relate to its effects on the central nervous system. The first clinical signs of poisoning include nervousness, restlessness, twitching of the muscles, and stiffness of the neck.
For high-risk patients (white blood cell count >10,000/μL), treatment usually entails ATRA plus ATO along with the addition of chemotherapy (such as idarubicin) during induction to rapidly control leukocytosis and reduce early death and relapse risk. Effectiveness appears similar to Realgar/Indigo naturalis, which can be taken by mouth and is less expensive but is less available. It works by encouraging the proteosome breakdown of retinoic acid receptor alpha, by moving the protein on to the nuclear matrix and increasing ubiquitination. This use was approved for leukemia treatment in the United States in 2000. A liquid form of arsenic trioxide that can be given by mouth, (Oral-ATO; ARSENOL®) for the treatment of acute promyelocytic leukaemia.
== History == Buserelin was first described in 1976 and was introduced for medical use in 1984. Intranasal buserelin was the first GnRH agonist demonstrated to achieve medical castration in humans. This was initially observed via a marked decrease in circulating testosterone levels in a single patient in 1980.
Sources: en.wikipedia.org
The Mark V initially used a single power source for the flashlight, sprinting, and oxygen supply; in Half-Life 2: Episode Two the flashlight was given a separate power source to improve gameplay. The symbol on Gordon's HEV suit is the lowercase Greek letter Lambda, λ. This symbol is used by scientists to denote the decay constant of radioactive elements (related to the half-life of an element). As well as appearing on Gordon's suit, the symbol replaces the letter "a" in the game title (Hλlf-Life) and is the name of the complex in the Black Mesa Research Facility where teleportation experiments are conducted in the first game. The Lambda symbol is also seen in Half-Life 2 as a marking of the human resistance, seen close to hidden supplies and on the armbands of better equipped resistance fighters.
== History == Effective pharmaceutical female sex-hormonal medications, including androgens, estrogens, and progestogens, first became available in the 1920s and 1930s, and might have been prescribed for transitions as early as the late 30s or 40s. The earliest report of hormone therapy in transgender women was published by Danish endocrinologist Christian Hamburger in 1953. One of his patients was Christine Jorgensen, who he had treated starting in 1950. Additional reports of hormone therapy in transgender women were published by Hamburger, the German-American endocrinologist Harry Benjamin, and other researchers in the mid-to-late 1960s. However, Benjamin had several hundred transgender patients under his care by the late 1950s, and had treated transgender women with hormone therapy as early as the late 1940s or early 1950s. In any case, Hamburger is said to be the first to treat transgender women with hormone therapy. One of the first transgender health clinics was opened in the mid-1960s at the Johns Hopkins School of Medicine. By 1981, there were almost 40 such centers. A review of the hormonal regimens of 20 of the centers was published that year. The first International Symposium on Gender Identity, chaired by Christopher John Dewhurst, was held in London in 1969, and the first medical textbook on transness, titled Transsexualism and Sex Reassignment and edited by Richard Green and John Money, was published by Johns Hopkins University Press in 1969. This textbook included a chapter on hormone therapy written by Christian Hamburger and Harry Benjamin.
Bully: Tyler Height: 6'1" Weight: 250 lbs Victim(s): Joe and Dylan Fighter: Daniel Cormier Height: 5'11" Weight: 247 lbs Money earned by Bully: $0 Money earned by victim(s): $10,000 Original airing: This episode aired on MTV2 on September 29, 2012. In MTV Latin America, this is run as the first episode of season 3, followed by the "Michael" episode, thus omitting the episode where Mayhem fights Andy.
A subarachnoid hemorrhage is acute bleeding under the arachnoid; it may occur spontaneously or as a result of trauma. A subdural hematoma (SDH) is an extracerebral collection of blood located in the potential space that can separate arachnoid from the dura mater. The origin is usually venous, caused by injury to the bridging veins that connect the dura mater and the arachnoid. Once these are torn, blood leaks into this area. SDHs occur in about 30% cases of severe head trauma. An epidural hematoma (EDH) is a collection of blood between the skull and the dura mater, underlying a bare bone surface. It is often associated with skull fracture. EDH may be arterial (caused by injury of a meningeal artery) or venous (related to damage to of a dural venous sinus or bleeding from diploic veins).
Sources: en.wikipedia.org
== Musicians, composers, and lyricists == Burnet Tuthill (1909), musicologist, conductor, founder and secretary of the National Association of Schools of Music Roy Webb (1910), composer for Notorious and Abe Lincoln in Illinois Richard Hale (1914), opera and concert singer; narrator, Peter and the Wolf Oscar Hammerstein II (1916), lyricist for Show Boat, Oklahoma! and The King and I, among other Broadway musical hits Howard Dietz (1917), director of publicity for MGM and lyricist for "Dancing in the Dark" Lorenz Hart (1918), lyricist for Pal Joey and other Broadway musical hits Richard Rodgers* (1923), composer and collaborator with Lorenz Hart and Oscar Hammerstein II; wrote music for Carousel, The Sound of Music, and Victory at Sea, among many others; one of the only two people to have won an Emmy, a Grammy, an Oscar, a Tony Award, and a Pulitzer Prize Elie Siegmeister (1927), composer, music teacher, writer on music Richard Franko Goldman (1930), composer, music professor, president of the Peabody Institute 1969–1977 Milton Katims (1930), conductor, music director of the Seattle Symphony 1954–1976 Mordecai Bauman (1935), baritone Emerson Buckley (1936), conductor, The Crucible, The Ballad of Baby Doe; director of the Florida Grand Opera 1950–1973 Eddie Sauter (1936), jazz musician Elliott Schwartz (1936), composer and professor emeritus of Bowdoin College John La Touche* (1937), lyricist for Cabin in the Sky and The Golden Apple Howard Shanet (1939), conductor and composer, former head of Columbia University's music department Leonard B.
Vasculogenesis is the process of blood vessel formation, occurring by a de novo production of endothelial cells. It is the first stage of the formation of the vascular network, closely followed by angiogenesis. This is the creation of blood vessels during early development particularly in embryos. Blood vessels start to form from special cells known as endothelial progenitor cells. While this process mostly happens during embryonic development, it can also occur in adults when the body needs to repair damaged blood vessels or grow new ones after an injury occurs. Vasculogenesis is the formation of new blood vessels, in blood islands, which first arise in the mesoderm of the yolk sac at 3 weeks of development, when there are no pre-existing ones. For example, if a monolayer of endothelial cells begins sprouting to form capillaries, angiogenesis is occurring. Vasculogenesis, in contrast, is when endothelial precursor cells (angioblasts) migrate and differentiate in response to local cues (such as growth factors and extracellular matrices) to form new blood vessels. These vascular trees are then pruned and extended through angiogenesis. Vasculogenesis can also arise in the adult organism from circulating endothelial progenitor cells (derivatives of stem cells). These cells are able to contribute, albeit to varying degrees, to neovascularization. Examples of where vasculogenesis can occur in adults are:
Choriogonadotropin subunit beta (CG-beta) also known as chorionic gonadotrophin chain beta is a protein that in humans is encoded by the CGB gene. This gene is a member of the glycoprotein hormone beta chain family and encodes the beta 3 subunit of chorionic gonadotropin (CG). Glycoprotein hormones are heterodimers consisting of a common alpha subunit and a unique beta subunit which confers biological specificity. CG is produced by the trophoblastic cells of the placenta and stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy. The beta subunit of CG is encoded by 6 genes which are arranged in tandem and inverted pairs on chromosome 19q13.3 and contiguous with the luteinizing hormone beta subunit gene.
In a move seen as marking her return to political life, former prime minister Liz Truss writes an article for The Sunday Telegraph in which she says her economic agenda was never given a "realistic chance". 6 February 2022–2023 National Health Service strikes: Ambulance staff and nurses walk out, with further disruption to follow in the week, in what is expected to be the biggest-ever round of NHS strikes. Foreign Secretary James Cleverly offers his condolences to victims of the 7.8 magnitude Turkey–Syria earthquake and says the UK is deploying emergency response teams, including 76 search and rescue specialists, equipment and rescue dogs. The government issues an urgent warning to British travellers and holidaymakers who may be in or planning to visit the region. 7 February Former Met Police officer David Carrick, one of the UK's most prolific sex offenders, is sentenced at Southwark Crown Court to 36 life sentences with a minimum term of 30 years in prison. Sunak performs a cabinet reshuffle. Greg Hands is named as the new Conservative Party chairman; Grant Shapps becomes the secretary of state for energy, security and net zero in a newly-formed department; Kemi Badenoch is appointed as the first secretary of state at the newly created Department for Business and Trade, with continued responsibility as equalities minister. 8 February Ukraine's President Volodymyr Zelensky addresses a joint session of Parliament during his first visit to the UK since Russia invaded his country. He later visits Buckingham Palace for a meeting with the King.
==== Detection methods ==== One of the earliest methods for protein analysis has been Edman degradation (introduced in 1967) where a single peptide is subjected to multiple steps of chemical degradation to resolve its sequence. These early methods have mostly been supplanted by technologies that offer higher throughput. More recently implemented methods use mass spectrometry-based techniques, a development that was made possible by the discovery of "soft ionization" methods developed in the 1980s, such as matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI). These methods gave rise to the top-down and the bottom-up proteomics workflows where often additional separation is performed before analysis (see below).
Sources: en.wikipedia.org
Glutathione is a tripeptide made from glutamate, cysteine, and glycine. Its cysteine residue provides a thiol group that is central to its redox activity. The glutamate-cysteine bond forms through the gamma-carboxyl group of glutamate.
Reduced glutathione, GSH, can donate electrons and become oxidized to GSSG. The balance between these forms reflects the cell's redox environment. A shift toward GSSG is commonly interpreted as evidence of oxidative stress, though the ratio can vary by tissue and method.
Glutathione occurs in nearly all cell types, with notable amounts in the liver. It is also present in the lungs, kidneys, and red blood cells. Concentrations differ among tissues and change with age, diet, and disease states.
GSH is the reduced thiol form, while GSSG is the disulfide-linked oxidized dimer. The GSH:GSSG ratio is used as a redox indicator, though the ratio can vary with sample handling and cell type.