From Ouroboros: "Advanced glycation endproducts (AGEs) have been implicated in age-related disease and aging itself, convincingly enough that significant effort has gone into finding compounds that can 'break' or reverse them. Among many unresolved questions: Are specific proteins AGEylated, and if so, which proteins are being modified within cells? Unterluggauer et al. report that in [senescent cells], the chaperone Hsc70 is modified by AGE ... If a major chaperone is modified by AGEs, and the modification is deleterious to its function, this could dramatically decrease the efficiency of protein folding, which (given that chaperones are proteins too) could dramatically decrease the number of chaperones, which [leads to a] garbage catastrophe ... (Then again: senescent cells persist in culture for a long time, implying that they have some way to deal with the admittedly hypothetical protein-folding death spiral implied in the previous paragraph.)"