| Name | thioredoxins |
|---|---|
| Synonyms | ADF; TRX 1; TRX1; ATL derived factor; SASP; Surface associated sulphydryl protein; TRDX; TRX… |
| Name | acrolein |
|---|---|
| CAS | 2-propenal |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 18023956 | Szadkowski A, Myers CR: Acrolein oxidizes the cytosolic and mitochondrial thioredoxins in human endothelial cells. Toxicology. 2008 Jan 14;243(1-2):164-76. Epub 2007 Oct 10. |
164(2,2,2,4) | Details |
| 17982132 | Go YM, Halvey PJ, Hansen JM, Reed M, Pohl J, Jones DP: Reactive modification of thioredoxin-1 activates early steps of inflammation and cell adhesion. Am J Pathol. 2007 Nov;171(5):1670-81. Acrolein and (HNE) are reactive aldehydes generated during active inflammation as a consequence of lipid peroxidation; both react with protein thiols, including thioredoxin-1 (Trx1), a protein recently found to regulate antioxidant function in endothelial cells. |
82(1,1,1,2) | Details |
| 19135121 | Myers CR, Myers JM: The effects of acrolein on peroxiredoxins, thioredoxins, and thioredoxin reductase in human bronchial epithelial cells. Toxicology. 2009 Mar 4;257(1-2):95-104. Epub 2008 Dec 24. |
14(0,0,2,4) | Details |
| 15388247 | Yang X, Wu X, Choi YE, Kern JC, Kehrer JP: Effect of acrolein and depleting agents on thioredoxin. . Toxicology. 2004 Nov 15;204(2-3):209-18. |
8(0,0,1,3) | Details |
| 17360766 | Hamada Y, Miyata S, Nii-Kono T, Kitazawa R, Kitazawa S, Higo S, Fukunaga M, Ueyama S, Nakamura H, Yodoi J, Fukagawa M, Kasuga M: Overexpression of thioredoxin1 in transgenic mice suppresses development of diabetic nephropathy. Nephrol Dial Transplant. 2007 Jun;22(6):1547-57. Epub 2007 Mar 14. In the present study, the effects of thioredoxin1 (TRX1) overexpression, a small protein with antioxidant property, on the development of diabetic nephropathy in streptozotocin-induced diabetic animals were investigated using TRX1 transgenic mice (TRX1-Tg). In parallel, urinary excretion of and acrolein adduct and the immunostaining intensities of these markers in the kidney were significantly higher in diabetic WT compared with non-diabetic mice. |
6(0,0,0,6) | Details |
| 15318812 | Liu XW, Sok DE: Inactivation of protein disulfide isomerase by alkylators including alpha,beta-unsaturated aldehydes at low physiological pHs. Biol Chem. 2004 Jul;385(7):633-7. In addition, PDIred was found to be inactivated by acrolein (IC50=10 microM) at pH 6.3, and this inactivation was also greater at pH 6.3 than at pH 7. Protein disulfide isomerase (PDI) is known to contain the thioredoxin box motif with a low pKa residue. |
1(0,0,0,1) | Details |
| 15652504 | Park YS, Misonou Y, Fujiwara N, Takahashi M, Miyamoto Y, Koh YH, Suzuki K, Taniguchi N: Induction of thioredoxin reductase as an adaptive response to acrolein in human umbilical vein endothelial cells. Biochem Biophys Res Commun. 2005 Feb 25;327(4):1058-65. Mammalian thioredoxin reductase (TR), a central antioxidant enzyme, is a selenoprotein that catalyzes the reduction of oxidized thioredoxin. |
1(0,0,0,1) | Details |
| 20149621 | Zhu L, Liu Z, Feng Z, Hao J, Shen W, Li X, Sun L, Sharman E, Wang Y, Wertz K, Weber P, Shi X, Liu J: protects against oxidative damage by simultaneous activation of mitochondrial biogenesis and phase II detoxifying enzyme systems in retinal pigment epithelial cells. J Nutr Biochem. 2010 Feb 9. Studies in this laboratory have previously shown that the major antioxidant polyphenol in olives, protects ARPE-19 human retinal pigment epithelial cells from oxidative damage induced by acrolein, an environmental toxin and endogenous end product of lipid oxidation, that occurs at increased levels in age-related macular degeneration lesions. The activation of Nrf2 led to activation of phase II detoxifying enzymes, including gamma-glutamyl-cysteinyl-ligase, -quinone-oxidoreductase 1, heme-oxygenase-1, superoxide dismutase, peroxiredoxin and thioredoxin as well as other antioxidant enzymes, while the activation of PPARGC1alpha led to increased protein expression of mitochondrial transcription factor A, uncoupling protein 2 and mitochondrial complexes. |
1(0,0,0,1) | Details |