Propagation of protein glycation damage involves modification of tryptophan residues via reactive oxygen species: inhibition by pyridoxamine.

@article{Chetyrkin2008PropagationOP,
  title={Propagation of protein glycation damage involves modification of tryptophan residues via reactive oxygen species: inhibition by pyridoxamine.},
  author={Sergei V. Chetyrkin and Missy Mathis and A. L. Ham and David L. Hachey and Billy G. Hudson and Paul A. Voziyan},
  journal={Free radical biology \& medicine},
  year={2008},
  volume={44 7},
  pages={
          1276-85
        }
}
Glucose autoxidation induces functional damage to proteins via modification of critical arginine residues.
TLDR
It is demonstrated that glucose autoxidation induced inhibition of lysozyme activity as well as NC1 domain binding to α(V)β(3) integrin receptor via modification of critical arginine residues by reactive carbonyl species (RCS) glyoxal and methylglyoxal while nonoxidative glucose adduction to the protein did not affect protein function.
How Does Pyridoxamine Inhibit the Formation of Advanced Glycation End Products? The Role of Its Primary Antioxidant Activity
TLDR
The results show that, at physiological pH, pyridoxamine can trap the •OCH3 radical, in both aqueous and lipidic media, with rate constants in the diffusion limit (>1.0 × 108 M−1 s−1).
Oxidative modifications in glycated insulin
TLDR
This work investigated the site-specific oxidation of native and glycated insulin through metal-catalyzed oxidation, with a combination of liquid chromatography and mass spectrometry, and identified the residues that were mainly oxidized, and peptide sequences resulting from oxidative cleavage of insulin.
Glycoxidation of biological macromolecules: a critical approach to halt the menace of glycation.
TLDR
The prevention of glycation reaction using therapeutic drugs such as metformin, pyridoxamine and aminoguanidine are discussed with special emphasis on the novel concept of the bioconjugation of these drugs like, AG with gold nanoparticles (GNPs).
Ribosylation of bovine serum albumin induces ROS accumulation and cell death in cancer line (MCF-7)
TLDR
Investigation of glycation-induced structural modifications in BSA and their functional consequences in breast cancer cell line (MCF-7) revealed cytotoxicity of ribosylated BSA on MCF- 7 cells, which suggests that glycation with d-ribose induced aggregation of BSA into amyloid-like deposits.
...
...

References

SHOWING 1-10 OF 66 REFERENCES
Pyridoxamine, an Inhibitor of Advanced Glycation Reactions, Also Inhibits Advanced Lipoxidation Reactions
TLDR
PM, as a potent inhibitor of both AGE and ALE formation, may prove useful for limiting the increased chemical modification of tissue proteins and associated pathology in aging and chronic diseases, including both diabetes and atherosclerosis.
Modification of Proteins In Vitro by Physiological Levels of Glucose
TLDR
Investigation of the conversion of protein-Amadori intermediate to protein-AGE and the mechanism of its inhibition by pyridoxamine, a potent AGE inhibitor that has been shown to prevent diabetic complications in animal models demonstrated that PM does not react with the Amadori.
Chelating Activity of Advanced Glycation End-product Inhibitors*
TLDR
Inhibition of AGE formation results primarily from the chelating or antioxidant activity of the AGE inhibitors, rather than their carbonyl trapping activity.
Degradation products of proteins damaged by glycation, oxidation and nitration in clinical type 1 diabetes
TLDR
There are profound increases in proteolytic products of glycated and oxidised proteins in diabetic patients, concurrent with much lower increases in protein glycation and oxidation adduct residues.
Superoxide free radical generation by Amadori compounds: the role of acyclic forms and metal ions.
TLDR
In addition to the metal ion-catalyzed oxygen free radical formation, metal-free enol oxidation of fructosyl groups on glycated amino acid residues may contribute to the generation of oxygen free radicals and their subsequent oxidative damage to proteins.
Protein aging by carboxymethylation of lysines generates sites for divalent metal and redox active copper binding: relevance to diseases of glycoxidative stress.
TLDR
CML-rich proteins immunoprecipitated from serum of uremic patients oxidized four times more ascorbate than control and generated spin adducts of DMPO in the presence of H(2)O(2).
3-Hydroxykynurenine-mediated Modification of Human Lens Proteins
TLDR
3OHKYN modifies lens proteins independent of glycation to form products that may contribute to protein aggregation and browning during cataract formation, and the effect of Glycation on tryptophan oxidation and kynurenine-mediated modification of lens proteins is investigated.
Immunological Evidence for Methylglyoxal-derived Modifications in Vivo
TLDR
It is shown that rabbit antibodies to MG-modified ribonuclease A identify proteins modified by the Maillard reaction of glucose, fructose, ribose, glyceraldehyde, glyoxal, ascorbate, and asCorbate oxidation products in addition to those modified by MG.
In Vitro Kinetic Studies of Formation of Antigenic Advanced Glycation End Products (AGEs)
TLDR
The mechanism-based approach to the study of AGE inhibition appears promising for the design and discovery of novel post-Amadori AGE inhibitors of therapeutic potential that may complement others, such as aminoguanidine, known to either prevent initial sugar attachment or to scavenge highly reactive dicarbonyl intermediates.
...
...