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The effectiveness of putative anti-cataract agents in the prevention of protein glycation
1National Vision Research Institute of Australia, Carlton, Australia.
Background:
Recent data have favored non-enzymatic glycation as a likely mechanism in diabetic cataract formation. The advanced glycation end products (AGEs) that are formed lead to opacification of the lens by disrupting the short-range order between the proteins. Attempts to decrease AGE formation has led to the use of various anti-glycating agents. Their efficacy, however, has been questionable.
Methods:
The extent of AGE formation was monitored in fetal bovine eyes using non-tryptophan fluorescence. The amount of carbohydrate bound to the proteins was measured after reduction with radio-labelled sodium borohydride.
Results:
While the addition of glucose, glucose-6-phosphate or fructose increased the levels of glycation by only 25 percent and the levels of AGEs by 40 percent, glyceraldehyde resulted in a 70 percent increase in glycation and showed extensive AGE formation (an increase of over 6600 percent when compared to the unglycated protein). The anti-glycating agents aspirin and ibuprofen were unable to significantly decrease the extent of bound metabolite or reduce the amount of AGE formed. In contrast, penicillamine and aminoguanidine were more effective in reducing the levels of AGEs, even though the levels of bound metabolite appeared unchanged.
Conclusions:
Triose phosphates are likely to be the major metabolic intermediates that result in AGE formation. The anti-glycating agents, whereas penicillamine and aminoguanidine-which react with the Amadori-derived fragmentation products-significantly decreased levels of AGEs.
Insights
Triose phosphates, not simple sugars, significantly increase advanced glycation end products (AGEs) linked to diabetic cataracts. Certain anti-glycating agents like penicillamine effectively reduce AGEs, offering potential therapeutic avenues.
Area of Science:
- Biochemistry
- Ophthalmology
- Diabetic Complications
Background:
- Non-enzymatic glycation and advanced glycation end products (AGEs) are implicated in diabetic cataract formation.
- AGEs disrupt lens protein structure, leading to opacification.
- The efficacy of current anti-glycating agents in preventing AGE formation is uncertain.
Purpose of the Study:
- To investigate the role of different carbohydrates in AGE formation.
- To evaluate the effectiveness of various anti-glycating agents in reducing AGEs.
Main Methods:
- AGE formation was assessed in fetal bovine eyes using non-tryptophan fluorescence.
- Carbohydrate-protein binding was quantified after reduction with radio-labelled sodium borohydride.
Main Results:
- Glyceraldehyde dramatically increased glycation (70%) and AGEs (over 6600%), unlike glucose or fructose.
- Aspirin and ibuprofen showed minimal impact on glycation and AGE levels.
- Penicillamine and aminoguanidine effectively reduced AGEs, despite unchanged carbohydrate-protein binding.
Conclusions:
- Triose phosphates are likely key intermediates in AGE formation.
- Penicillamine and aminoguanidine, by reacting with Amadori-derived products, significantly reduce AGE levels.
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