Graded sensitiveness of the various retinal neuron populations on the glyoxal-mediated formation of advanced glycation end products and ways of protection

Graefes Arch Clin Exp Ophthalmol. 2003 Mar;241(3):213-25. doi: 10.1007/s00417-002-0528-1. Epub 2003 Feb 7.

Abstract

Background: The accumulation of advanced glycation end products (AGEs) in retinal cells is known to be associated with the risk of diabetic retinopathy. To develop a model of AGE-related metabolic stress in retinal organ cultures, we investigated the accumulation of a typical glycoxidation product (N(epsilon)-[carboxymethyl] lysine [CML]) and its possible pro-apoptotic effects on different retinal cell populations.

Methods: Retinal organ cultures (rat) were kept for 9 h in the Ames medium containing 0 (control), 5, 25, 50, 150, 300 and 800 micro M glyoxal. The expression of bax, active caspase-3, and the accumulation of CML were studied by using immunohistochemistry after the paraffin embedding of retinal explants. Apoptosis was studied using the terminal deoxynucleotidyl transferase-mediated dUTP digoxigenin nick end labeling (TUNEL) test and electron microscopy. Alpha lipoic acid (alpha-LA), sodium metavanadate (NaVO(3)), N-acetylcysteine (NAC), aminoguanidine (AG), and nicotinamide (NA) were used to influence glyoxal effects in organ cultures.

Results: In cultured normal non-diabetic retinae, small amounts of CML and the apoptosis-promoting factors bax and active caspase-3 were present. CML, bax and active caspase-3 increased after incubation with glyoxal. Incubation with glyoxal (<300 micro M, 9 h) increased apoptotic events in all layers. At low glyoxal concentrations, we found a graded sensitiveness of the different layers: at 25 micro M 39.4% in GCL, 28.2% in INL, 11.9% in ONL. After 800 micro M glyoxal, approximately 50% of the cells in all layers of the retina were apoptotic. In the ONL, this ratio was reduced by NaVO(3) (17%), by AG (27%), by NA (24.8%), by NAC (25.2%), and by alpha-LA (33.5%). In the INL, AG (25.9%) produced the best result. In the GCL, NAC, NaVO(3) and AG reduced apoptosis. A-LA had no significant protective effect.

Conclusion: The glyoxal-induced rapid formation of CML shows the ability of our retina model to simulate AGE-related effects in vitro. The dose-dependent expression of apoptosis-promotor molecules indicates that the apoptosis-inducing machinery starts in most retinal cells within 9 h. The neurotoxicity of glyoxal-induced AGE formation was shown by the significantly increased rate of cell death in the retina. The significant decrease of apoptotic events (P<0.01) indicates that antioxidants and AGE formation blocker can exert a differentiated cytoprotection for each of the retinal cell layers.

MeSH terms

  • Acetylcysteine / pharmacology
  • Animals
  • Apoptosis / drug effects
  • Caspase 3
  • Caspases / metabolism
  • Dose-Response Relationship, Drug
  • Female
  • Glycation End Products, Advanced / metabolism*
  • Glyoxal / toxicity*
  • Guanidines / pharmacology
  • Immunoenzyme Techniques
  • In Situ Nick-End Labeling
  • Lysine / analogs & derivatives*
  • Lysine / metabolism
  • Male
  • Neurons / drug effects*
  • Neurons / metabolism
  • Neurons / pathology
  • Niacinamide / pharmacology
  • Organ Culture Techniques
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2*
  • Rats
  • Rats, Sprague-Dawley
  • Retina / drug effects*
  • Retina / metabolism
  • Retina / pathology
  • Thioctic Acid / pharmacology
  • Vanadates / pharmacology
  • bcl-2-Associated X Protein

Substances

  • Bax protein, rat
  • Glycation End Products, Advanced
  • Guanidines
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • bcl-2-Associated X Protein
  • Niacinamide
  • Vanadates
  • Glyoxal
  • N(6)-carboxymethyllysine
  • Thioctic Acid
  • Casp3 protein, rat
  • Caspase 3
  • Caspases
  • Lysine
  • pimagedine
  • Acetylcysteine