ArticleBiochemistry2011
Glucose autoxidation induces functional damage to proteins via modification of critical arginine residues.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 72 citations in OpenAlex.
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- Understanding the Role of Protein Glycation in the Amyloid Aggregation Process.International journal of molecular sciences · 2021Review
- Complexities of the glomerular basement membrane.Nature reviews. Nephrology · 2021Review
- In vitro antioxidant and antidiabetic activity of essential oils encapsulated in gelatin-pectin particles against sugar, lipid and protein oxidation and amylase and glucosidase activity.Food science & nutrition · 2020Article
- In vitro and ex vivo anti-diabetic and anti-hyperglycemic properties of Zataria multiflora essential oil.Molecular biology reports · 2020Article
- Isolevuglandins as mediators of disease and the development of dicarbonyl scavengers as pharmaceutical interventions.Pharmacology & therapeutics · 2020Review
- Understanding Diabetic Neuropathy: Focus on Oxidative Stress.Oxidative medicine and cellular longevity · 2020Review
- Glycation of Plant Proteins: Regulatory Roles and Interplay with Sugar Signalling?International journal of molecular sciences · 2019Review
- Bifunctional Chloroplastic DJ-1B fromAntioxidants (Basel, Switzerland) · 2019Article
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
Nonenzymatic modification of proteins in hyperglycemia is a major mechanism causing diabetic complications. These modifications can have pathogenic consequences when they target active site residues, thus affecting protein function. In the present study, we examined the role of glucose autoxidation in functional protein damage using lysozyme and RGD-α3NC1 domain of collagen IV as model proteins in vitro. We 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 (GO) and methylglyoxal while nonoxidative glucose adduction to the protein did not affect protein function. The role of RCS in protein damage was confirmed using pyridoxamine which blocked glucose autoxidation and RCS production, thus protecting protein function, even in the presence of high concentrations of glucose. Glucose autoxidation may cause protein damage in vivo since increased levels of GO-derived modifications of arginine residues were detected within the assembly interface of collagen IV NC1 domains isolated from renal ECM of diabetic rats. Since arginine residues are frequently present within protein active sites, glucose autoxidation may be a common mechanism contributing to ECM protein functional damage in hyperglycemia and oxidative environment. Our data also point out the pitfalls in functional studies, particularly in cell culture experiments, that involve glucose treatment but do not take into account toxic effects of RCS derived from glucose autoxidation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.