A systematic approach to evaluate the modification of lens proteins by glycation-induced crosslinking.

@article{Lee1999ASA,
  title={A systematic approach to evaluate the modification of lens proteins by glycation-induced crosslinking.},
  author={K W Lee and G Simpson and Beryl J. Ortwerth},
  journal={Biochimica et biophysica acta},
  year={1999},
  volume={1453 1},
  pages={
          141-51
        }
}
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Sugar-mediated crosslinking of alpha-biotinylated-Lys to cysteamine-agarose support: a method to isolate Maillard Lys-Lys-like crosslinks.
TLDR
This work reports here a simple approach that allows the preparation and isolation of milligram quantities of sugar-mediated AGE Lys-Lys-like crosslinks from glycation mixtures, and fractionation of these preparations over a monomeric avidin column afforded a complete separation of cane sugar modifications and the crosslinks.
Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins.
Inhibitors of advanced glycation end product-associated protein cross-linking.
Effect of advanced glycation end products on lens epithelial cells in vitro.
TLDR
The existence of AGEs in human anterior polar lens capsules of cataracts was confirmed using a combination of dot-immunoblot and fluorescent detection and the interaction of LECs with AGE s induced mRNAs and proteins of fibronectin, collagen type I, aberrant extracellular matrix proteins, and alpha-SMA, a specific marker for myofibroblastic cells.
New insights into protein crosslinking via the Maillard reaction: structural requirements, the effect on enzyme function, and predicted efficacy of crosslinking inhibitors as anti-ageing therapeutics.
Glycation induced conformational transitions in cystatin proceed to form biotoxic aggregates: A multidimensional analysis.
Glycation promotes the formation of genotoxic aggregates in glucose oxidase
TLDR
The study suggests that glycated GOD results in the formation of aggregates and the advanced glycated end products, which are genotoxic in nature.
Identification of C1q as a Binding Protein for Advanced Glycation End Products.
TLDR
The presence of serum proteins that are capable of binding glycated bovine serum albumin (AGEs-BSA), prepared upon incubation of BSA with dehydroascorbate, is examined and complement component C1q subcomponent subunit A is identified as a novel AGE-binding protein in human serum, providing the first evidence of AGEs as a new ligand recognized by C 1q, stimulating the C1Q-dependent classical complement pathway.
2-Ammonio-6-(3-oxidopyridinium-1-yl)hexanoate (OP-lysine) Is a Newly Identified Advanced Glycation End Product in Cataractous and Aged Human Lenses*
TLDR
The results argue that OP-lysine is a newly identified glycation product of lysine in the lens that is a marker of aging and pathology of the lens, and its formation could be considered as a potential cataract risk-factor based on its concentration and its photochemical properties.
UVA Light-excited Kynurenines Oxidize Ascorbate and Modify Lens Proteins through the Formation of Advanced Glycation End Products
TLDR
The data suggest that kynurenine-mediated ASC oxidation followed by AGE formation may be an important mechanism for lens aging and the development of senile cataracts in humans.
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References

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Several amine-containing compounds were tested as inhibitors of crosslinking; however, 2-aminoguanidine was the most effective and the rate of synthesis of Lys-Lys, Lys-Arg, and Lys-His crosslinks was determined by measuring the incorporation of [14C]lysine into specific amino acid homopolymers.
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ASCORBIC ACID GLYCATION OF LENS PROTEINS PRODUCES UVA SENSITIZERS SIMILAR TO THOSE IN HUMAN LENS
TLDR
The possibility that the sensitizer activity was due to an ascorbate‐induced oxidation of tryptophan was eliminated by the presence of a heavy metal ion chelator during the incubation and by showing equivalent effects with ascorBate‐incubated ribonuclease A, which is devoid of tryPTophan.
Glutathione inhibits the glycation and crosslinking of lens proteins by ascorbic acid.
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