Accumulation of free adduct glycation, oxidation, and nitration products follows acute loss of renal function
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Glycation, oxidation, and nitration of endogenous proteins occur spontaneously and these modifications are also present in foods. Increased levels of these chemical changes are associated with chronic renal failure; however, little is known about acute kidney failure. We measured these modifications of plasma protein and related free adducts in plasma following bilateral nephrectomy and bilateral ureteral obstruction. Advanced glycation end-product (AGE) residues of plasma protein were increased 3 h post-surgery, and thereafter slowly decreased in all groups, reflecting changes in plasma protein synthesis and transcapillary flow post-surgery. Ureteral ligation increased oxidation and nitration adduct residues. There were, however, marked increases in AGE, dityrosine, or 3-nitrotyrosine free adducts in both nephrectomized and ureter-ligated rats compared to rats that had undergone sham operations. There were lower modified adduct concentrations in the ureter-ligated compared to the nephrectomized rats, reflecting residual glomerular filtration and tubular removal. There was no increase in glycated, oxidized, and nitrated proteins. Glyoxal and methylglyoxal were also increased in both renal failure models. Our study shows that the acute loss of renal function and urinary excretion leads to the accumulation of AGE, oxidation, and nitration free adducts in the plasma.
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Acute/chronic kidney disease and end-stage renal failure can reduce AGE clearance, leading to accelerated progression and/or exacerbation of kidney malfunction and nephropathy.
“On the other hand, acute/chronic kidney disease and end-stage renal failure can reduce AGE clearance. Consequently, glomerular and tubular cells are exposed to potentially harmful AGEs for extended periods of time owing to the lower rates of glomerular filtration. These changes lead to accelerated progression and/or exacerbation of kidney malfunction and nephropathy along with greater amounts of”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [69]
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- Authors
- Rabbani, N., Sebekova, K., Sebekova, K., Heidland, A., & Thornalley, P. J.
- Affiliations
- University of Warwick (GB)
- University of Würzburg (DE)
- Corresponding author
- Thornalley, P.J.
- Venue
- Kidney International
- Publisher
- Elsevier BV
- Published
- 2007-11
- Volume
- 72
- Issue
- 9
- Pages
- 1113-1121
- ISSN
- 0085-2538 (ISSN-L)
- OpenAlex
- W2002874967
- Cited by
- 90
- References
- 39
- Citations by year
- 2025: 5 · 2024: 2 · 2023: 2 · 2022: 5 · 2021: 4 · 2020: 4 · 2019: 7 · 2018: 3 · 2017: 2 · 2016: 4 · 2015: 5 · 2014: 6 · 2013: 4 · 2012: 5
- FWCI
- 5.92
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Kidney International (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Health Sciences › Medicine › Nephrology › Acute Kidney Injury Research
- Health Sciences › Medicine › Nephrology › Chronic Kidney Disease and Diabetes
- Keywords
- acute kidney injury, advanced glycation end products, protein glycation, protein oxidation, nitration, nitrotyrosine, dityrosine, glyoxal, methylglyoxal, bilateral nephrectomy, ureteral obstruction, renal failure, urinary excretion
- MeSH terms
- Animals, Body Weight, Disease Models, Animal, Glyoxal, Kidney Failure, Chronic, Ligation, Male, Nephrectomy, Pyruvaldehyde, Tyrosine, Glycation End Products, Advanced, Rats, Wistar, Oxidative Stress, Rats
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