Nuclear proteasome activation and degradation of carboxymethylated histones in human keratinocytes following glyoxal treatment.

@article{CervantesLaurean2005NuclearPA,
  title={Nuclear proteasome activation and degradation of carboxymethylated histones in human keratinocytes following glyoxal treatment.},
  author={Daniel Cervantes-Laurean and Michael J. Roberts and Elaine L. Jacobson},
  journal={Free radical biology & medicine},
  year={2005},
  volume={38 6},
  pages={
          786-95
        }
}
Nuclear DNA damage has been studied in detail, but much less is known concerning the occurrence and fate of nuclear protein damage. Glycoxidation, protein damage that results from a combination of protein glycation and oxidation, leads to the formation of protein-advanced glycation end products (AGE) of which N(epsilon)-carboxymethyllysine (CML) is a major AGE. We have used glyoxal, a product of environmental exposures that readily leads to the formation of CML, to study nuclear protein… CONTINUE READING
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