The thiol pool in human plasma: the central contribution of albumin to redox processes.
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TLDR
A critical review of the plasma thiol pool is provided with a focus on human serum albumin, an important target for oxidants and electrophiles due to its reactivity with a wide variety of species and its relatively high concentration.About:
This article is published in Free Radical Biology and Medicine.The article was published on 2013-12-01 and is currently open access. It has received 519 citations till now. The article focuses on the topics: Human serum albumin & Thiol.read more
Citations
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A novel and automated assay for thiol/disulphide homeostasis.
Ozcan Erel,Salim Neselioglu +1 more
TL;DR: In this paper, the authors developed a novel and automated assay determining plasma thiol/disulphide homeostasis, which consists of thiol-disoulphide exchanges.
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Existing and potential therapeutic uses for N-acetylcysteine: the need for conversion to intracellular glutathione for antioxidant benefits.
TL;DR: A key conclusion is a reinforcement of the concept that NAC should not be considered to be a powerful antioxidant in its own right: its strength is the targeted replenishment of GSH in deficient cells and it is likely to be ineffective in cells replete in GSH.
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N-Acetylcysteine as an antioxidant and disulphide breaking agent: the reasons why
Giancarlo Aldini,Alessandra Altomare,Giovanna Baron,Giulio Vistoli,Marina Carini,Luisa Borsani,Francesco Sergio +6 more
TL;DR: The disulphide breaking activity of NAC also explains its mucolytic activity which is due to its effect in reducing heavily cross-linked mucus glycoproteins and free thiols as well as reduced proteins which have important direct antioxidant activity.
Journal ArticleDOI
Peptide and protein nanoparticle conjugates: versatile platforms for biomedical applications
TL;DR: A comprehensive overview of the key sequences and structures utilised to provide biological and physical stability to nano-constructs, direct particles to their target and influence their cellular and tissue distribution, induce and control biological responses, and form polypeptide self-assembled nanoparticles are provided.
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The Reactive Species Interactome: Evolutionary Emergence, Biological Significance, and Opportunities for Redox Metabolomics and Personalized Medicine.
Miriam M. Cortese-Krott,Anne M. Koning,Gunter G. C. Kuhnle,Péter Nagy,Christopher L. Bianco,Christopher L. Bianco,Andreas Pasch,David A. Wink,Jon M. Fukuto,Jon M. Fukuto,Jon M. Fukuto,Alan Jackson,Harry van Goor,Kenneth R. Olson,Martin Feelisch +14 more
TL;DR: This work introduces a novel integrative concept defined as the reactive species interactome (RSI), a primeval multilevel redox regulatory system whose architecture allows efficient sensing and rapid adaptation to environmental changes and various other stressors to enhance fitness and resilience at the local and whole-organism level.
References
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The peroxidase and peroxynitrite reductase activity of human erythrocyte peroxiredoxin 2.
TL;DR: In this paper, the peroxiredoxin 2 (Prx2) was studied in a steady-state approach yielding an apparent K(M) of 2.4 microM for human thioredoxin and a very low K (M) for H2O2 (0.7 microM).
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Investigation of an albumin-enriched fraction of human serum and its albuminome.
TL;DR: 35 proteins, of which 24 are intact, were found to be associated with albumin, and they include both known high and low abundance proteins.
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Peroxynitrite reaction with the reduced and the oxidized forms of lipoic acid: new insights into the reaction of peroxynitrite with thiols
Madia Trujillo,Rafael Radi +1 more
TL;DR: Testing various low-molecular-weight thiols, it is found that an increase in the thiol pK (pK(SH)) value correlated with a decrease of k(2app) for the reaction with peroxynitrite at pH 7.4.
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Carbon Dioxide Stimulates the Production of Thiyl, Sulfinyl, and Disulfide Radical Anion from Thiol Oxidation by Peroxynitrite
Marcelo G. Bonini,Ohara Augusto +1 more
TL;DR: It is demonstrated that HCO 3 − /CO2 diverts thiol oxidation by peroxynitrite from two- to one-electron mechanisms particularly at neutral pH, which indicates that thiyl, RSO and RSSR⋅ − are reactive radicals that may contribute to the biodamaging and bioregulatory actions of peroxlynitrite.
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Albumin thiolate anion is an intermediate in the formation of albumin-S-S-homocysteine
Shantanu Sengupta,Hong Chen,Tadayasu Togawa,Patricia M. DiBello,Alana K. Majors,Beatrix Büdy,Beatrix Büdy,Michael E. Ketterer,Donald W. Jacobsen +8 more
TL;DR: Studies are presented to show that the formation of albumin-bound homocysteine proceeds through the generation of an albumin thiolate anion, and using an in vitro model system to study the mechanisms of this disulfide bond formation, it is shown that homocystine binds to albumin in two steps.