Protein glycation: a firm link to endothelial cell dysfunction.

@article{Wautier2004ProteinGA,
  title={Protein glycation: a firm link to endothelial cell dysfunction.},
  author={J L Wautier and Ann Marie Schmidt},
  journal={Circulation research},
  year={2004},
  volume={95 3},
  pages={233-8}
}
The advanced glycation end products (AGEs) are a heterogeneous class of molecules, including the following main subgroups: bis(lysyl)imidazolium cross-links, hydroimidazolones, 3-deoxyglucosone derivatives, and monolysyl adducts. AGEs are increased in diabetes, renal failure, and aging. Microvascular lesions correlate with the accumulation of AGEs, as demonstrated in diabetic retinopathy or renal glomerulosclerosis. On endothelial cells, ligation of receptor for AGE (RAGE) by AGEs induces the… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 163 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 55 references

Similar Papers

Loading similar papers…