Dietary glycotoxins: inhibition of reactive products by aminoguanidine facilitates renal clearance and reduces tissue sequestration
Abstract
Evidence indicates that the metabolic turnover of food-derived reactive orally absorbed advanced glycation end products (AGEs) or glycotoxins (GTs) is delayed, possibly contributing to the tissue damage induced by endogenous AGEs, especially in patients with diabetes and kidney disease. The aim of this study was to explore whether pharmacologic inhibition of dietary AGE bioreactivity by aminoguanidine (AG) can improve turnover and renal excretion of these substances. Normal Sprague-Dawley rats were fed single-labeled [14C]AGE-ovalbumin, double-labeled [14C-125I]AGE-ovalbumin, or control 125I-labeled ovalbumin diet plus free [14C]glucose, with or without AG (0.2% in water). [14C]AGE- and 125I-labeled peptide-associated radioactivity (RA) were compared with AGE immunoreactivity (by enzyme-linked immunosorbent assay) in tissues, serum, and 72-h urine samples. The effect of AG on dietary AGE bioreactivity was assessed by monitoring the inhibition of covalent complex formation between fibronectin (FN) peptide fragments and serum components, after a meal of labeled dietary AGE with or without AG. The radiolabeled AGE diet produced serum absorption and urinary excretion peaks kinetically distinct from those of free [14C]glucose or [125I]ovalbumin. Some 26% of the orally absorbed AGE-ovalbumin was excreted in the urine, whereas after AG treatment, urinary excre-tion of dietary AGEs increased markedly (to >50% of absorbed). More than 60% of tissue-bound RA was found covalently deposited in kidneys and liver, whereas after treatment with AG, tissue AGE deposits were reduced to <15% of the amount found in untreated AGE-fed controls. Sera enriched for dietary GTs formed covalently linked complexes with FN, a process completely inhibitable by AG cotreatment. Amelioration of dietary GT bioreactivity by AG improves renal elimination and prevents tissue deposition of food GTs. This may afford a novel and potentially protective use of AG against excessive tissue AGE toxicity in diabetic patients with renal disease.
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These indirect effects include up- or down-regulation of resistin, leptin, adiponectin, lipocalin 2, osteopontin and insulin itself.
“These effects include the up-or down-regulation of the synthesis of resistin (138) , leptin, adiponectin (139) , lipocalin 2 (140) , osteopontin (141) , and of insulin itself.”
From Dietary factors and low-grade inflammation in relation to overweight and obesity (2011) · cites this paper as [140]
At present, RAGE seems to be the only advanced glycation end product receptor involved in cell activation.
“At present, RAGE seems to be the only receptor involved in cell activation (140) .”
From Dietary factors and low-grade inflammation in relation to overweight and obesity (2011) · cites this paper as [140]
Advanced glycation end product receptors have a dual function, being involved in both advanced glycation end product removal and advanced glycation end product-induced cell activation.
“AGE receptors have a dual function and are involved in both AGE removal and AGE-induced cell activation (140) .”
From Dietary factors and low-grade inflammation in relation to overweight and obesity (2011) · cites this paper as [140]
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Šebeková, K., Faist, V., Hofmann, T. F., Schinzel, R., & Heidland, A. (2003) · American Journal of Kidney Diseases · doi:10.1053/ajkd.2003.50084 · Cited by 51 · see citing works
Mazumder, M. A. R., Hongsprabhas, P., & Vasudevan, R. T. (2019) · Journal of Food Biochemistry · doi:10.1111/jfbc.13089 · Cited by 48 · see citing works
Enomoto, M., Adachi, H., Yamagishi, S., Takeuchi, M., Furuki, K., Hino, A., Hiratsuka, A., Takajo, Y., & Imaizumi, T. (2006) · Metabolism · doi:10.1016/j.metabol.2006.02.019 · Cited by 44 · see citing works
Advanced Glycation End Products: Link between Diet and Ovulatory Dysfunction in PCOS?
Garg, D., & Merhi, Z. O. (2015) · Nutrients · doi:10.3390/nu7125524 · Cited by 43 · see citing works
- Authors
- He, C., Sabol, J., Mitsuhashi, T., & Vlassara, H.
- Affiliations
- Icahn School of Medicine at Mount Sinai (US)
- ORCID
- He, C
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 1999-06-01
- Volume
- 48
- Issue
- 6
- Pages
- 1308-1315
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W2124616258
- Cited by
- 191
- References
- 0
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 4 · 2023: 5 · 2022: 12 · 2021: 11 · 2020: 6 · 2019: 12 · 2018: 9 · 2017: 11 · 2016: 11 · 2015: 15 · 2014: 2 · 2013: 10 · 2012: 9
- FWCI
- 4.76
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Diabetes (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (AG09453, R01AG009453)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Agricultural and Biological Sciences › Food Science › Potato Plant Research
- Health Sciences › Medicine › Nephrology › Dialysis and Renal Disease Management
- Keywords
- advanced glycation end products, aminoguanidine, renal clearance, urinary excretion, tissue deposition, fibronectin, covalent cross-linking, diabetic nephropathy
- MeSH terms
- Animals, Diet, Enzyme Inhibitors, Female, Guanidines, Kidney, Metabolic Clearance Rate, Peptide Fragments, Glycation End Products, Advanced, Rats, Sprague-Dawley, Rats
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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