PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34638176-5 2021 TPO and TG are the two key proteins necessary for the biosynthesis of thyroid hormones in the presence of iodide and H2O2. Hydrogen Peroxide 117-121 thyroid peroxidase Homo sapiens 0-3 23883148-4 2013 The prohormone thyroxine (T4) is synthesized on thyroglobulin by thyroid peroxidase (TPO), a heme enzyme that uses iodide and hydrogen peroxide to perform iodination and phenolic coupling reactions. Hydrogen Peroxide 126-143 thyroid peroxidase Homo sapiens 85-88 6847661-1 1983 Thyroid peroxidase (TPO) and lactoperoxidase (LPO) display significant catalatic activity at pH 7.0 in the presence of low concentrations of iodide, based both on measurements of H2O2 disappearance and O2 evolution. Hydrogen Peroxide 179-183 thyroid peroxidase Homo sapiens 0-18 6847661-1 1983 Thyroid peroxidase (TPO) and lactoperoxidase (LPO) display significant catalatic activity at pH 7.0 in the presence of low concentrations of iodide, based both on measurements of H2O2 disappearance and O2 evolution. Hydrogen Peroxide 179-183 thyroid peroxidase Homo sapiens 20-23 2996435-0 1985 Spectral characteristics and catalytic properties of thyroid peroxidase-H2O2 compounds in the iodination and coupling reactions. Hydrogen Peroxide 72-76 thyroid peroxidase Homo sapiens 53-71 2996435-1 1985 Hog thyroid peroxidase (TPO) was highly purified in order to study the spectral properties and catalytic specificities of its H2O2 compounds in iodothyronine biosynthesis. Hydrogen Peroxide 126-130 thyroid peroxidase Homo sapiens 4-22 2996435-1 1985 Hog thyroid peroxidase (TPO) was highly purified in order to study the spectral properties and catalytic specificities of its H2O2 compounds in iodothyronine biosynthesis. Hydrogen Peroxide 126-130 thyroid peroxidase Homo sapiens 24-27 2996435-4 1985 On addition of an equimolar amount of H2O2, TPO formed a stable compound with an absorption maximum at 417 nm. Hydrogen Peroxide 38-42 thyroid peroxidase Homo sapiens 44-47 2996435-8 1985 In the presence of an excess of H2O2, it formed TPO-compound III with an absorption maximum at 420 nm. Hydrogen Peroxide 32-36 thyroid peroxidase Homo sapiens 48-51 31172499-1 2019 Extracellular hydrogen peroxide is required for thyroperoxidase-mediated thyroid hormone synthesis in the follicular lumen of the thyroid gland. Hydrogen Peroxide 14-31 thyroid peroxidase Homo sapiens 48-63 27331089-5 2016 This article presents data describing the molecular changes that occur to a TPx mimic upon exposure to H2O2, and then the thiol mercaptoethanol, as characterised by UV-vis spectroscopy and HPLC retention time. Hydrogen Peroxide 103-107 thyroid peroxidase Homo sapiens 76-79 25905405-8 2000 TPO sits at the apical plasma membrane, where it reduces H2O2, elevating the oxidation state of iodide to an iodinating species, and attaches the iodine to tyrosyls in Tg. Hydrogen Peroxide 57-61 thyroid peroxidase Homo sapiens 0-3 25595679-5 2015 This inhibition may occur because GSH acts as a competitive substrate for hydrogen peroxide, or possibly reduce the oxidized form of iodide, requirements for TPO action. Hydrogen Peroxide 74-91 thyroid peroxidase Homo sapiens 158-161 21511237-6 2011 They are the principal elements generating the hydrogen peroxide needed for TPO function. Hydrogen Peroxide 47-64 thyroid peroxidase Homo sapiens 76-79 19952225-1 2010 CONTEXT: Thyroid hormone synthesis requires H(2)O(2) produced by dual oxidases (Duoxes) and thyroperoxidase (TPO). Hydrogen Peroxide 44-52 thyroid peroxidase Homo sapiens 109-112 20826581-1 2010 CONTEXT: Thyroperoxidase (TPO) and dual oxidase (DUOX) are present at the apical membrane of thyrocytes, where TPO catalyzes thyroid hormone biosynthesis in the presence of H2O2 produced by DUOX. Hydrogen Peroxide 173-177 thyroid peroxidase Homo sapiens 9-24 20826581-1 2010 CONTEXT: Thyroperoxidase (TPO) and dual oxidase (DUOX) are present at the apical membrane of thyrocytes, where TPO catalyzes thyroid hormone biosynthesis in the presence of H2O2 produced by DUOX. Hydrogen Peroxide 173-177 thyroid peroxidase Homo sapiens 26-29 20826581-1 2010 CONTEXT: Thyroperoxidase (TPO) and dual oxidase (DUOX) are present at the apical membrane of thyrocytes, where TPO catalyzes thyroid hormone biosynthesis in the presence of H2O2 produced by DUOX. Hydrogen Peroxide 173-177 thyroid peroxidase Homo sapiens 111-114 20826581-4 2010 DESIGN: The functional consequences of DUOX-TPO interaction were studied by measuring extracellular H2O2 concentration and TPO activity in a heterologous system. Hydrogen Peroxide 100-104 thyroid peroxidase Homo sapiens 44-47 20826581-7 2010 RESULTS: We observed that production of H2O2 decreases both TPO and DUOX activities. Hydrogen Peroxide 40-44 thyroid peroxidase Homo sapiens 60-63 20826581-8 2010 We show that TPO presents a catalase-like effect that protects DUOX from inhibition by H2O2. Hydrogen Peroxide 87-91 thyroid peroxidase Homo sapiens 13-16 20826581-11 2010 Normally, TPO consumes H2O2 produced by DUOX, decreasing the availability of this substance at the apical membrane of thyrocytes and, in turn, probably decreasing the oxidative damage of macromolecules. Hydrogen Peroxide 23-27 thyroid peroxidase Homo sapiens 10-13 17379648-7 2007 BP2 at 300 nmol/liter combined with the TPO substrate H(2)O(2) (10 mumol/liter) inactivated hrTPO; this was, however, prevented by micromolar amounts of iodide. Hydrogen Peroxide 54-62 thyroid peroxidase Homo sapiens 40-43 17666482-4 2007 EVIDENCE SYNTHESIS: In humans, H2O2 production by dual-oxidases and consequently thyroid hormone synthesis by thyroperoxidase are controlled by the phospholipase C-Ca2+-diacylglycerol arm of TSH receptor action. Hydrogen Peroxide 31-35 thyroid peroxidase Homo sapiens 110-125 16843823-5 2006 Our work reveals that TPO generates radical adducts in the presence of H2O2, but that the generation of these adducts can be suppressed by the addition of substrates and inhibitors. Hydrogen Peroxide 71-75 thyroid peroxidase Homo sapiens 22-25 16843823-7 2006 Iodide strongly suppresses the H2O2-generated production of TPO radical adducts and protects the enzyme from loss of enzyme activity. Hydrogen Peroxide 31-35 thyroid peroxidase Homo sapiens 60-63 16843823-8 2006 Because the normal catalytic mechanism of TPO involves the production of radical species, TPO is potentially more susceptible to oxidative damage than most enzymes which do not require H2O2 as a substrate. Hydrogen Peroxide 185-189 thyroid peroxidase Homo sapiens 42-45 16843823-8 2006 Because the normal catalytic mechanism of TPO involves the production of radical species, TPO is potentially more susceptible to oxidative damage than most enzymes which do not require H2O2 as a substrate. Hydrogen Peroxide 185-189 thyroid peroxidase Homo sapiens 90-93 12755690-3 2003 Decreased H2O2 availability may be another mechanism of inhibition of thyroperoxidase activity produced by thioureylene compounds, as propylthiouracil (PTU) and methimazole (MMI) are antioxidant agents. Hydrogen Peroxide 10-14 thyroid peroxidase Homo sapiens 70-85 15972824-1 2005 Duox2 (and probably Duox1) is a glycoflavoprotein involved in thyroid hormone biosynthesis, as the thyroid H2O2 generator functionally associated with Tpo (thyroperoxidase). Hydrogen Peroxide 107-111 thyroid peroxidase Homo sapiens 151-154 15972824-1 2005 Duox2 (and probably Duox1) is a glycoflavoprotein involved in thyroid hormone biosynthesis, as the thyroid H2O2 generator functionally associated with Tpo (thyroperoxidase). Hydrogen Peroxide 107-111 thyroid peroxidase Homo sapiens 156-171 15591162-1 2005 The dual oxidase (Duox)2 flavoprotein is strongly expressed in the thyroid gland, where it plays a critical role in the synthesis of thyroid hormones by providing thyroperoxidase with H2O2. Hydrogen Peroxide 184-188 thyroid peroxidase Homo sapiens 163-178 15116324-2 2004 We analyzed the ultracytochemical localization of thyroperoxidase (TPO), TPO-associated hydrogen peroxide-generating sites (H(2)O(2) sites), and monoamine oxidase (MAO) in terms of morphology and biochemical TPO activity in abnormal thyroids. Hydrogen Peroxide 88-105 thyroid peroxidase Homo sapiens 73-76 15116324-2 2004 We analyzed the ultracytochemical localization of thyroperoxidase (TPO), TPO-associated hydrogen peroxide-generating sites (H(2)O(2) sites), and monoamine oxidase (MAO) in terms of morphology and biochemical TPO activity in abnormal thyroids. Hydrogen Peroxide 88-105 thyroid peroxidase Homo sapiens 73-76 15611814-4 2004 Iodide oxidation and organification occur mainly in the thyrocyte apical surface and these reactions are catalyzed by thyroperoxidase (TPO) in the presence of hydrogen peroxide. Hydrogen Peroxide 159-176 thyroid peroxidase Homo sapiens 118-133 15611814-4 2004 Iodide oxidation and organification occur mainly in the thyrocyte apical surface and these reactions are catalyzed by thyroperoxidase (TPO) in the presence of hydrogen peroxide. Hydrogen Peroxide 159-176 thyroid peroxidase Homo sapiens 135-138 15611814-5 2004 Thus, thyroid iodide organification depends on TPO activity, which is modulated by the concentration of substrates (thyroglobulin and iodide) and cofactor (hydrogen peroxide). Hydrogen Peroxide 156-173 thyroid peroxidase Homo sapiens 47-50 9760285-10 1998 Incubation of LMG with TPO, iodide, and tyrosine in the presence of a H2O2-generating system yielded oxidation products that were identified by using on-line LC/APCI-MS as desmethyl LMG, 2desmethyl LMG, 3desmethyl LMG, MG, and MG N-oxide. Hydrogen Peroxide 70-74 thyroid peroxidase Homo sapiens 23-26 11762710-1 2001 Duox2, and probably Duox1 are glycoflavoproteins involved in the thyroid H2O2 generator functionally associated to thyroperoxidase (TPO). Hydrogen Peroxide 73-77 thyroid peroxidase Homo sapiens 115-130 11762710-1 2001 Duox2, and probably Duox1 are glycoflavoproteins involved in the thyroid H2O2 generator functionally associated to thyroperoxidase (TPO). Hydrogen Peroxide 73-77 thyroid peroxidase Homo sapiens 132-135 11295360-11 2001 The variants of TPx I and TPx II appeared within 2 min of the addition of H2O2 to the culture medium. Hydrogen Peroxide 74-78 thyroid peroxidase Homo sapiens 16-19 11295360-11 2001 The variants of TPx I and TPx II appeared within 2 min of the addition of H2O2 to the culture medium. Hydrogen Peroxide 74-78 thyroid peroxidase Homo sapiens 26-29 10601291-2 1999 Hydrogen peroxide is the final electron acceptor for the biosynthesis of thyroid hormone catalyzed by thyroperoxidase at the apical surface of thyrocytes. Hydrogen Peroxide 0-17 thyroid peroxidase Homo sapiens 102-117 8837329-4 1996 Treatment of MN with TPO in the presence of the H2O2 generating system, glucose-glucose oxidase, resulted in the formation of a black product (or products). Hydrogen Peroxide 48-52 thyroid peroxidase Homo sapiens 21-24 9497358-1 1998 A new type of peroxidase enzyme, named thioredoxin peroxidase (TPx), that reduces H2O2 with the use of electrons from thioredoxin and contains two essential cysteines was recently identified. Hydrogen Peroxide 82-86 thyroid peroxidase Homo sapiens 39-61 9497358-1 1998 A new type of peroxidase enzyme, named thioredoxin peroxidase (TPx), that reduces H2O2 with the use of electrons from thioredoxin and contains two essential cysteines was recently identified. Hydrogen Peroxide 82-86 thyroid peroxidase Homo sapiens 63-66 9464451-8 1997 Incubation of either isoflavone with TPO in the presence of H2O2 caused irreversible inactivation of the enzyme; however, the presence of iodide ion in the incubations completely abolished the inactivation. Hydrogen Peroxide 60-64 thyroid peroxidase Homo sapiens 37-40 9388194-6 1997 TPx II, unlike Bcl-2, could prevent hydrogen peroxide accumulation in cells, suggesting that it functions upstream of Bcl-2 in the protection from apoptosis and may be implicated as an endogenous regulator of apoptosis. Hydrogen Peroxide 36-53 thyroid peroxidase Homo sapiens 0-3 8924586-5 1996 Other flavonoids inhibited TPO by different mechanisms, such as myricetin and naringin, showed noncompetitive inhibition of tyrosine iodination with respect to iodine ion and linear mixed-type inhibition with respect to hydrogen peroxide. Hydrogen Peroxide 220-237 thyroid peroxidase Homo sapiens 27-30 8068644-9 1994 The oxidation of thyroid peroxidase and lactoperoxidase by hydrogen peroxide produces catalytic intermediates containing unpaired electron density on amino acid residues similar to that seen with cytochrome c peroxidase. Hydrogen Peroxide 59-76 thyroid peroxidase Homo sapiens 17-35 7483672-4 1995 The two-electron oxidation of TPO by H2O2 produces an oxoferryl porphyrin pi-cation radical compound I that isomerizes spontaneously to a form of compound I that contains an oxoferryl haem and the second oxidizing equivalent as an amino acid radical. Hydrogen Peroxide 37-41 thyroid peroxidase Homo sapiens 30-33