نتایج جستجو برای: thioredoxin

تعداد نتایج: 6000  

The extensive use of heavy metals and nanoparticles (NPs) has led to their release into the environment that might have negative impacts on both organisms and the environment. In this study, the molecular responses of wheat seedlings to silver nitrate and silver nanoparticles (AgNPs) were assessed by transcript accumulation analysis of genes coding for products potentially involved in heavy met...

2010
Kornelia Edes Pamela Cassidy Paul J. Shami Philip J. Moos

BACKGROUND The selenoenzyme thioredoxin reductase 1 has a complex role relating to cell growth. It is induced as a component of the cellular response to potentially mutagenic oxidants, but also appears to provide growth advantages to transformed cells by inhibiting apoptosis. In addition, selenocysteine-deficient or alkylated forms of thioredoxin reductase 1 have also demonstrated oxidative, pr...

Journal: :Circulation 2004
Jun Yoshioka P Christian Schulze Mihaela Cupesi Jeremy D Sylvan Catherine MacGillivray Joseph Gannon Hayden Huang Richard T Lee

BACKGROUND Although cellular redox balance plays an important role in mechanically induced cardiac hypertrophy, the mechanisms of regulation are incompletely defined. Because thioredoxin is a major intracellular antioxidant and can also regulate redox-dependent transcription, we explored the role of thioredoxin activity in mechanically overloaded cardiomyocytes in vitro and in vivo. METHODS A...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2005
Damon Huber Myoung-Il Cha Laurent Debarbieux Anne-Gaëlle Planson Nelly Cruz Gary López María Luisa Tasayco Alain Chaffotte Jon Beckwith

Escherichia coli thioredoxin is normally a cytoplasmic protein involved in the reduction of disulfide bonds. However, thioredoxin can be translocated to the periplasm when it is attached to a cotranslational signal sequence. When exported to the periplasm, it can partially replace the activity of DsbA in promoting the formation of disulfide bonds. In contrast, when thioredoxin is fused to a pos...

Journal: :Cancer research 2001
L Shao M B Diccianni T Tanaka R Gribi A L Yu J D Pullen B M Camitta J Yu

Increased expression of intracellular thioredoxin has been implicated in the inhibition of apoptosis and in a decrease in the sensitivity of the malignancies to drug-induced apoptosis. In the present studies, we analyzed expression of thioredoxin in samples from 28 children with T-cell acute lymphoblastic leukemia and analyzed their sensitivity toward inhibition of thioredoxin expression. Thior...

2006
Guang-Hui Liu Jing Qu Xun Shen William Tansey

PPAR , a member of the nuclear receptor superfamily, and thioredoxin, a critical redox-regulator in cells, were found to form a negative feedback loop, which autoregulates transcriptional activity of PPAR . Thioredoxin was identified as a target gene of PPAR . Activation of PPAR leads to increase of thioredoxin expression as well as its translocation from cytoplasm to nucleus, whereas ectopic o...

Journal: :European journal of biochemistry 2000
C H Williams

Recent publications make it evident that the thioredoxin± thioredoxin reductase system has come of age. The four minireviews presented here attempt to put this field in perspective. The system was first recognized in the early 1960s as the reductant of methionine sulfoxide and PAPS (3 0-phosphoadenosine-5 0-phosphosulfate) in yeast and of ribonucleotides in Escherichia coli [1±3]. It became cle...

2018
Zhihong Zheng Shengjun Fan Jing Zheng Wei Huang Cristina Gasparetto Nelson J Chao Jianda Hu Yubin Kang

BACKGROUND Although current chemotherapy using bortezomib (Velcade) against multiple myeloma in adults has achieved significant responses and even remission, a majority of patients will develop acquired resistance to bortezomib. Increased thioredoxin level has been reported to be associated with carcinogenesis; however, the role of thioredoxin in bortezomib drug resistance of myeloma remains un...

Journal: :Molecular cell 2012
Alison M Day Jonathon D Brown Sarah R Taylor Jonathan D Rand Brian A Morgan Elizabeth A Veal

Eukaryotic 2-Cys peroxiredoxins (Prx) are abundant antioxidant enzymes whose thioredoxin peroxidase activity plays an important role in protecting against oxidative stress, aging, and cancer. Paradoxically, this thioredoxin peroxidase activity is highly sensitive to inactivation by peroxide-induced Prx hyperoxidation. However, any possible advantage in preventing Prx from removing peroxides und...

Journal: :Zeitschrift fur Naturforschung. C, Journal of biosciences 1991
J Bodenstein H Follmann

Heart tissue contains two different thioredoxins. One is a specific mitochondrial protein and is best prepared from pre-isolated, intact heart mitochondria (mt-thioredoxin) whereas mitochondria-depleted tissue homogenates contain the major cellular thioredoxin of cytoplasmic origin (c-thioredoxin). Both heat-stable proteins are clearly differentiated chromatographically. They exhibit slightly d...

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