Effect of advanced glycation end products on lens epithelial cells in vitro

Sung Baek Hong, Kwang Won Lee, James T. Handa, Choun Ki Joo

Research output: Contribution to journalArticlepeer-review

33 Scopus citations


The extended exposure of proteins to reducing sugars leads to nonenzymatic glycation with the accumulation of advanced glycation end products (AGEs). Long-lived proteins, such as collagen and crystallins, are subjected to this modification, and are implicated as causal factors in several diseases including diabetic complications, cataracts, and arteriosclerosis. One means through which AGEs modulate cellular interactions is via binding to specific receptors. In the current study, the existence of AGEs in human anterior polar lens capsules of cataracts was confirmed using a combination of dot-immunoblot and fluorescent detection. Human lens epithelial cells (LECs) attached to anterior lens capsules expressed mRNA for the receptor for AGEs (RAGE). The interaction of LECs with AGEs using bovine lens epithelial explants demonstrated that AGEs induced mRNAs and proteins of fibronectin, collagen type I, aberrant extracellular matrix proteins, and α-SMA, a specific marker for myofibroblastic cells. These findings suggest that AGEs may alter cellular functions which induce mRNAs and proteins associated with fibrosis in LECs. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)53-59
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Aug 18 2000
Externally publishedYes


  • AGEs
  • Bovine lens explants
  • Cataracts
  • Extracellular matrix
  • Fibrosis
  • Glycation
  • RAGE
  • Transdifferentiation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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