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'Electronic switch' opens doors in rheumatoid joints
January 03, 2008A breakthrough in understanding the way atoms move across cell membranes in the human body could pave the way for the development of new treatments for inflammatory diseases such as rheumatoid arthritis.
Scientists at the University of Leeds have identified a previously unknown natural mechanism that opens ion channels - proteins at the cell surface that act as doorways into and out of cells - through the naturally occurring protein thioredoxin.
Ion channels allow movement of ions - electrically charged atoms - across the cell membrane to carry out various functions such as pain transmission, timing of the heart beat, and regulation of blood glucose. Often, they need to be stimulated to open and, until now, two main groups of activating mechanisms have been acknowledged: changes in cell voltage and binding of chemical factors.
In a paper published today (03 January) in Nature, Professor Beech and colleagues from the University's Faculty of Biological Sciences reveal that thioredoxin works in a different manner: it activates an ion channel by donating electrons to it, in a process Professor Beech likens to "an electronic on-switch".
"Thioredoxin is naturally present in cells and is secreted to help the body counter stressful chemical reactions that occur in inflammation, which can damage cells," he explains. "We already knew that inflammatory diseases cause the production of high levels of thioredoxin - in fact with rheumatoid arthritis, it's striking how much is present in affected joints. But we didn't know until now that thioredoxin can also activate ion channels, conferring additional protective potential and offering opportunities for mimicking the effect with drugs."
"It would seem that the body's own natural defences have provided us with new understanding that could be significant in the development of future treatments for arthritis and related diseases," he says.
University of Leeds
In a paper published today (03 January) in Nature, Professor Beech and colleagues from the University's Faculty of Biological Sciences reveal that thioredoxin works in a different manner: it activates an ion channel by donating electrons to it, in a process Professor Beech likens to "an electronic on-switch".
"Thioredoxin is naturally present in cells and is secreted to help the body counter stressful chemical reactions that occur in inflammation, which can damage cells," he explains. "We already knew that inflammatory diseases cause the production of high levels of thioredoxin - in fact with rheumatoid arthritis, it's striking how much is present in affected joints. But we didn't know until now that thioredoxin can also activate ion channels, conferring additional protective potential and offering opportunities for mimicking the effect with drugs."
"It would seem that the body's own natural defences have provided us with new understanding that could be significant in the development of future treatments for arthritis and related diseases," he says.
University of Leeds
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Biothiols, Part B: Glutathione and Thioredoxin: Thiols in Signal Transduction and Gene Regulation, Volume 252 (Methods in Enzymology) by John N. Abelson (Editor), Melvin I. Simon (Editor), Helmut Sies (Editor) The critically acclaimed laboratory standard for forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerlyawaited, frequently consulted, and praised by researchers and reviewers alike. More than 250 volumes have been published (all of them still in print) and much of the material is relevant even today--truly an essential publication for researchers in all fields of life sciences. Key Features * Distribution, biosynthesis, metabolism, and transport of glutathione * Signal transduction and gene regulation * Thioredoxin and glutaredoxin * Mimics of biological thiols and thiol inhibitors |
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Thioredoxines: Structure et fonctions : colloque international CNRS-NASA, Berkeley, Californie, 21-24 juin 1981 = Thioredoxins : structure and functions (French Edition) by Editions du Centre national de la recherche scientifique (Publisher) | |
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Protein Sensors of Reactive Oxygen Species, Part A: Selenoproteins and Thioredoxin, Volume 347 (Methods in Enzymology) by Lester Packer (Editor), Helmut Sies (Editor) This volume of Methods in Enzymology is concerned with the rapidly developing field of selenoprotein synthesis and its related molecular genetics. Progressive information on the topics of proteins as redox sensors, selenoproteins, and the thioredoxin system is studied using methods such as bioinformatics, DNA chip technology, cell biology, molecular genetics, and enzymology. The information on novel selenoproteins identified from genomic sequence data, as well as current knowledge on glutathione peroxidases, selenoprotein P, iodothyronine deiodinases, and thioredoxin reductases, is presented in a method-based approach. |
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The Glyoxalase System, Inhibition of Thioredoxin Reductase and Use of Methylene Blue as Drug Development Strategies Against the Malarial Parasite Plasmodium Falciparum by Monique Bate Akoachere (Author) | |
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Thioredoxin and Glutaredoxin Systems: Structure and Function by Arne Holmgren (Editor) | |
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Thioredoxin in the cyanobacteria: Structural and functional homology to thioredoxins from other organisms by Florence K Gleason (Author) | |
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Aspects of the x-ray data collection of proteins and the low resolution structure of oxidized thioredoxin from Escherichia coli B (N.S. diss. / Lantbrukshögskolan) by Bengt-Olof Söderberg (Author) |
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