#Taurine amino acid free
However, taurine is not a scavenger of free radicals, and the precise mechanism of antioxidant action is unclear. Taurine also acts as an antioxidant: concentration is particularly high in cells exposed to oxidative stress, and deficiency is linked with cell death ( Jong et al., 2013). Deficiency is associated with cardiomyopathy, renal and pancreatic dysfunction, retinal damage, and diabetes.
In the central nervous system, taurine functions as an intracellular osmolyte, regulating cell volume and stabilizing cell membranes, and its presence is important for optimal cell development in the brain, retina, skeletal muscle, and other organs ( Stapleton et al., 1998). Taurine’s role varies according to cell type ( Stapleton et al., 1998). Taurine as a regulator of cellular function Taurine is a common ingredient in energy drinks, though since many of these also include high levels of caffeine, it’s not clear whether any perceived energy boost is attributable to taurine.
Formula milk is often supplemented with taurine, though evidence is mixed as to whether this is beneficial or not ( Chawla et al., 2018). Human breast milk contains high levels of taurine which is sufficient for newborns. Premature infants are vulnerable to taurine deficiency because they lack the enzymes needed to synthesize cysteine. Because of taurine’s role in retinal and brain development, children who consume diets low in animal protein may need to supplement their taurine intake ( Wójcik et al., 2010). People following vegetarian or vegan diets have been shown to have lower levels of taurine in plasma ( Laidlaw et al., 1988). Meat and fish are good sources of taurine, and a diet containing animal products usually contains sufficient taurine for physiological needs. Excess taurine is excreted through urine or conjugated to bile acids. It is transported to the liver and released into the blood stream, then enters cells throughout the body via the taurine transporter (TauT). Most taurine is obtained through diet and absorbed in the small intestine. This is converted into hypotaurine with assistance from several enzymes, and then oxidized to form taurine.
It is then decarboxylated by cysteine sulfinic acid decarboxylase (CSAD) to form hypotaurine. in the cysteine sulfinic pathway, cysteine is oxidized to cysteine sulfinic acid by the enzyme cysteine dioxygenase.Taurine is synthesized in humans in the liver via two pathways: Unlike other amino acids, taurine contains a sulfide group instead of a carboxyl group, which makes it an amino sulfonic acid. Taurine is derived from the conditionally essential amino acid, cysteine, which is a product of methionine catabolism. However, given its significant role in many biological processes including bile salt formation, osmoregulation, antioxidation, retinal development, and the central nervous and cardiovascular systems, its presence in the body appears very much essential ( Ripps et al., 2012 Stapleton et al., 1998). Taurine is considered a “conditionally” essential amino acid, due to its lack of involvement in protein synthesis. Taurine does not appear to be present to the same degree in plants ( Jacobsen et al., 1968 Hou et al., 2019). Over the following decades, studies revealed the presence of taurine in animal bile and muscle tissue, including human bile in 1846 ( Ronalds et al., 2019). Referencing this, taurine gets its name from the Latin taurus, meaning bull or ox. It was first isolated from ox bile in 1827 by two German scientists, Friedrich Tiedemann and Leopold Gmelin ( Tiedemann et al., 1827). Taurine is an aminosulfonic acid with high intracellular concentrations in the brain, retina, heart, skeletal muscles, and leukocytes in humans ( Bayarmaa et al., 2013 Lourenço et al., 2002).
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