Post-translational protein modifications significantly expand the portfolio of proteins with specific properties encoded by the genetic code. They allow for the production of multiple variants of a single gene product through specific, potentially reversible, covalent alterations of amino acid side chains. To date, about 200 distinct post-translational protein modifications are known (Khidekel and Hsieh-Wilson, 2004). However, we are just at the beginning of a thorough qualitative and quantitative characterization of only a few of these post-translational modifications in the ''aging proteome.'' Importantly, proteins will not necessarily only incorporate a single modification, but often multiple modifications accumulate specifically on long-lived proteins in tissues with low protein turnover (e.g., the crystallins in the lens). Considering the progressive age-dependent functional changes of most cell types and tissues, an accurate profile of age-dependent post-translational protein modifications is mandatory. The following paragraphs will focus on the proteomic characterization of selected post-translational protein modifications such as phosphorylation and oxidation.
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