Glycation is a non-enzymatic post-translational modification (PTM) that is correlated with many diseases, including diabetes, cancer and age-related disorders. Although recent work points to the importance of glycation as a functional PTM, it remains an open question whether glycation has a causal role in cellular signaling and/or disease development. In this Review, we contextualize glycation as a specific mechanism of carbon stress and consolidate what is known about advanced glycation end-product (AGE) structures and mechanisms. We highlight the current understanding of glycation as a PTM, focusing on mechanisms for installing, removing or recognizing AGEs. Finally, we discuss challenges that have hampered a more complete understanding of the biological consequences of glycation. The development of tools for predicting, modulating, mimicking or capturing glycation will be essential for interpreting a post-translational glycation network. Therefore, continued insights into the chemistry of glycation will be necessary to advance understanding of glycation biology.
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Protein glycation compromises the bioavailability of milk protein-derived lysine in vivo in healthy adult males: a double-blind randomized cross-over trial.
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Department of Human Biology, NUTRIM Institute of Nutrition and Translational Research in Metabolism, Maastricht University Medical Centre+, Maastricht, the Netherlands. Electronic address:
Background: Industrial processing and storage of milk products can strongly increase protein glycation level. Previously, we have reported that ingestion of highly glycated milk protein attenuates the post-prandial rise in plasma lysine concentrations when compared to the ingestion of an equivalent amount of milk protein with a low glycation level. Whether the attenuated increase in plasma lysine availability is attributed to compromised protein digestion and subsequent lysine absorption remains to be established.
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