Abstract
Human thioredoxin (TRX) is a 12-kDa protein with redox-active dithiol in the active site -Cys-Gly-Pro-Cys-, which is induced by biological stress due to oxidative damage, metabolic dysfunction, chemicals, infection/inflammation, irradiation, or hypoxia/ischemia-reperfusion. Our research has demonstrated that exogenous TRX is effective in a wide variety of inflammatory diseases, including viral pneumonia, acute lung injury, gastric injury, and dermatitis, as well as in the prevention and amelioration of food allergies. Preclinical and clinical studies using recombinant TRX (rhTRX) are now underway. We have also identified substances that induce the expression of TRX in the body, in vegetables and other plant ingredients. Skincare products are being developed that take advantage of the anti-inflammatory and anti-allergic action of TRX. Furthermore, we are currently engaged in the highly efficient production of pure rhTRX in several plants, such as lettuce, grain and rice.
Highlights
Thioredoxin (TRX) is a small protein with a catalytically active dithiol site (Cys-Gly-Pro-Cys) found in a variety of life forms on earth, including bacteria, plants, and animals [1,2,3]
Denver Colorado, USA as the “regain” antibody [6], which was confirmed to be identical to the was first identified as a secretory autocrine and IL-2 receptor inducing protein, adult T cell leukemia unknown myeloma protein studied by Bennich and Johansson’s group in Sweden [7]
ATL characterized by abnormal leukemia cells having multiwere frequent in the southern regions of Japan, and soon proved to be associated with retrovirus convoluted nuclei and T cell properties was reported in Japan in the early 1970s
Summary
Thioredoxin (TRX) is a small protein with a catalytically active dithiol site (Cys-Gly-Pro-Cys) found in a variety of life forms on earth, including bacteria, plants, and animals [1,2,3]. TRX in the reduced state catalyzes the cleavage of disulfide bonds in the target proteins, and it becomes oxidized after completion of the reaction. Oxidized TRX is restored to the reduced form by the nicotinamide adenine dinucleotide phosphate (NADPH)-dependent thioredoxin reductase. TRX is associated with membrane lipid rafts, where it can control the redox inflammation. Extracellular TRX is associated with membrane lipid rafts, where it can control the state ofstate cell surface and influence theinfluence downstream pathway. The extracellular TRX is mediated lipid rafts. Txnip form a redox-sensitive signaling complex termed ‘redoxisome’, which may reducing activity of TRX. TRX and Txnip form a redox-sensitive signaling complex termed play a centralwhich role in theplay regulation diverse from metabolic and ‘redoxisome’, may a centralofrole in thebiological regulationprocesses of diverseranging biological processes ranging immunological pathways to inflammatory response and tumorigenesis. In the earlyof1960s, TRX was reported as awith ribonucleotide-reducing co-enzyme by the Karolinska
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