Cited by 27Advanced Glycation End Products researchPotato Plant ResearchDiet, Metabolism, and Disease

The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.

Are Food Advanced Glycation End Products Toxic in Biological Systems?

CHUYEN, N.V, ARAI, H, NAKANISHI, T, UTSUNOMIYA, N.·2005·Annals of the New York Academy of Sciences

Abstract

Model food advanced glycation end products (AGEs) were prepared as glycated casein (GC) and glycated soy protein (GS) by the reaction of casein or soy protein with glucose at 50 degrees C, relative humidity 75% for seven days in a powder state. These browned proteins were used as materials for animal experiments. A mixture of 20% glycated proteins (GC:GS = 1:1) diet was fed to streptozotocin (STZ)-diabetic rats for 11 weeks. The results showed that: (1) fructoselysine was observed in the hepatic portal veins, arteries, and femoral veins of rats fed with glycated proteins after 2 h of feeding; (2) blood sugar of glycated protein-fed rats was lower than that of diabetic rats fed with intact protein, while HbA1C in blood and glucose in urine of both groups were similar; (3) lipid peroxidation status in serum, liver, and kidney of both groups was similar; (4) superoxide dismutase (SOD) and glutathione-S-transferase (GST) enzymatic activity in serum and liver of both groups were also similar; (5) there were no differences in degree of cataract formation and concentration of glucose, fructose, sorbitol, and lipid peroxide in the lenses of both groups. From the above results, it can be estimated that food AGEs are not toxic in biological systems, and reactive oxygen species increase in diabetic rats is not caused by glycated proteins but by other pathways.

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Crossref · 10.1196/annals.1333.053

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9 of 9 references verified0 citation errors · 0 not checkable

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Research works printed but not linked: 2

  1. Habig W.H., 1974, Glutathione‐S‐transferase: the first enzymatic step in mercapturic acid formation, J. Biol. Chem., 249, 7130
  2. Imajo T., 1977, Improved measurement method of superoxide dismutase, Igaku no Ayumi, 101, 496

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Metadata

Authors
CHUYEN, N. V., ARAI, H., NAKANISHI, T., & UTSUNOMIYA, N.
Affiliations
  • Japan Women's University (JP)
  • Kyoritsu Women's University (JP)
Corresponding author
UTSUNOMIYA, N.
Venue
Annals of the New York Academy of Sciences
Publisher
Wiley
Published
2005-06
Volume
1043
Issue
1
Pages
467-473
ISSN
  • 0077-8923 (ISSN-L)
  • 1749-6632
OpenAlex
W1998753026
Cited by
27
References
9
Citations by year
2025: 1 · 2022: 1 · 2021: 1 · 2019: 2 · 2018: 3 · 2016: 1 · 2015: 4 · 2014: 3 · 2013: 1 · 2012: 2
FWCI
0.89
Type
journal article
Language
en
Open access
closed
Locations
  • Annals of the New York Academy of Sciences (publishedVersion)
  • PubMed (publishedVersion)
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 › Endocrinology, Diabetes and Metabolism › Diet, Metabolism, and Disease
Keywords
advanced glycation end products, glycated proteins, casein, soy protein, fructoselysine, streptozotocin-induced diabetes, lipid peroxidation, superoxide dismutase, glutathione S-transferase, cataract, reactive oxygen species, blood glucose, HbA1c, dietary toxicity
MeSH terms
Animals, Animal Feed, Diabetes Mellitus, Experimental, Glycosylation, Lysine, Male, Portal System, Maillard Reaction, Glycation End Products, Advanced, Rats, Wistar, Soybean Proteins, Rats

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