By Vladimir Uversky, Tilman Grune, Betul Catalgol, Tobias Jung
Reviews our present figuring out of the position of protein oxidation in getting older and age-related diseases
Protein oxidation is on the middle of the getting older technique. environment forth a number of new equipment and ways, this e-book is helping researchers very easily by way of exploring the getting older strategy and constructing more advantageous remedies to avoid or deal with age-related ailments. there were many reports devoted to the connection among protein oxidation and age-related pathology; now it truly is attainable for researchers and readers to profit new suggestions as using protein oxidation items as biomarkers for aging.
Protein Oxidation and Aging starts with an outline of the large number of protein oxidation items. in addition, it covers:• significant features of the protein oxidation process
• mobile mechanisms for handling oxidized proteins
• function of protein oxidation in aging
• impact of genetic and environmental components on protein oxidation
• Measuring protein oxidation within the getting older process
• Protein oxidation in age-related diseases
References on the finish of every bankruptcy function a gateway to the starting to be physique of unique examine reviews and stories within the box.
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Additional resources for Protein Oxidation and Aging (Wiley Series in Protein and Peptide Science)
The damage in the enzyme is limited and thus is reversible (203). Reversal may be provided by the loss of O2 from ROO• and the resulting stable carbon-centered species. Many oxidative enzymes, such as LOXs and the CYP450 family, can generate radical species during their interaction with substrates and, in some cases, inactivate themselves via this way. Thus, lipid peroxyl radicals are released during lipoxygenase action, and the product hydroperoxides of linoleic acid can inactivate the enzyme if iron is available (from the enzyme or elsewhere).
Although O2•− is relatively unreactive in comparison with many other radicals, biological systems can convert it into other more reactive species, such as peroxyl (ROO•), alkoxyl (RO•), and hydroxyl (•OH) radicals. The last of these can originate from the Fenton reaction, in which the metal ion redox cycles, with reduction effected by O2•− and oxidation effected by its dismutation product, hydrogen peroxide (H2O2). Iron and copper are biologically important transition metal ions, with their reduced forms capable of rapidly cleaving organic (including lipid) hydroperoxides, forming radicals that can initiate chain reactions, ultimately giving stable products such as lipid hydroxides (44).
Enzymes readily oxidizable by MFO are also found to be oxidized in the physiological aging process. This led Oliver et al. (31) and Stadtman (255) to the suggestion of a leading role of MFO in age-related protein oxidation. Zhou and Gafni (260) tested whether reduction after MFO may result in a protein identical to the native enzyme. PGK was exposed to an ascorbate : FeCl3 system, which leads to an inactivation of the enzyme. This can be partially reversed by addition of 2-mercaptoethanol. It was proposed that the selective oxidation of the reactive Cys residues in PGK was having a role in PGK inactivation.