Short-chain aldehyde-derived ligands for RAGE and their actions on endothelial cells
Abstract
The formation and accumulation of advanced glycation endproducts (AGE) have been implicated in the development of diabetic vascular complications. Their biological responses are known to be mediated by the receptor for AGE (RAGE). Recently, AGE have been proposed to be derived not only from the classical Maillard reaction but also from other pathways of sugar autoxidation and metabolism. Here, we report the identification of glyceraldehydes (Gcer)- and glycolaldehyde (Gcol)-derived AGE as RAGE ligands and their presence in vivo. The apparent dissociation constants assessed by surface-plasmon resonance (SPR) analysis with purified human RAGE proteins were 360 nM for Gcer-AGE and 1.35 microM for Gcol-AGE. The radiolabeled-ligand binding assay with RAGE-expressing COS-7 cells revealed similar association kinetics. Competitive SPR assay with antibodies specific to the respective AGE fractions demonstrated abundant existence of both Gcer- and Gcol-AGE in RAGE affinity-purified proteins from human sera. The serum contents of Gcer- and Gcol-AGE in a diabetic patient were about twice as high as those in a healthy control. Functionally, Gcer- and Gcol-AGE upregulated the endothelial cell levels of mRNA for vascular endothelial growth factor (VEGF) and the secretion of its protein product into the culture media and DNA synthesis in a dose-dependent manner. Further, these endothelial responses were augmented by RAGE overexpression. The results suggest that RAGE engagement of Gcer- and Gcol-AGE may elicit angiogenesis through the induction of autocrine VEGF, thereby contributing to the development and progression of diabetic angiopathies.
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The three RAGE forms bind various ligands with similar affinities, including AGEs and amyloid β peptide.
“The three RAGE forms bind various ligands with similar affinities, including multiple advanced glycation end-products (AGEs) and amyloid β peptide31–37.”
From Vascular RAGE transports oxytocin into the brain to elicit its maternal bonding behaviour in mice (2019) · cites this paper as [32]
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- Authors
- Yamamoto, Y., Yonekura, H., Watanabe, T., Sakurai, S., Li, H., Harashima, A., Myint, K. M., Osawa, M., Takeuchi, A., Takeuchi, M., & Yamamoto, H.
- Affiliations
- Kanazawa University (JP)
- Hokuriku University (JP)
- Corresponding author
- Yamamoto, Hiroshi
- ORCID
- Venue
- Diabetes Research and Clinical Practice
- Publisher
- Elsevier BV
- Published
- 2007-09
- Volume
- 77
- Issue
- 3
- Pages
- S30-S40
- ISSN
- 0168-8227 (ISSN-L)
- OpenAlex
- W1994269968
- Cited by
- 44
- References
- 38
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 2 · 2023: 2 · 2022: 4 · 2021: 2 · 2020: 2 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 4 · 2015: 3 · 2014: 2 · 2012: 3
- FWCI
- 2.86
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Diabetes Research and Clinical Practice (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (16790183, 16570113, 17590241, 97L00805)
- Japan Diabetes Foundation
- Ministry of Education, Culture, Sports, Science and Technology (13670113)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Health Sciences › Medicine › Ophthalmology › Retinal Diseases and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
- Keywords
- advanced glycation end products, receptor for advanced glycation end products, RAGE ligands, endothelial cells, vascular endothelial growth factor, angiogenesis, diabetic vascular complications, diabetic vascular disease
- MeSH terms
- Receptor for Advanced Glycation End Products, Aldehydes, Animals, Haplorhini, Cell Line, Cells, Cultured, Chlorocebus aethiops, DNA Replication, Endothelium, Vascular, Humans, Ligands, Receptors, Immunologic, RNA, Messenger, Umbilical Veins, COS Cells, Reverse Transcriptase Polymerase Chain Reaction, Surface Plasmon Resonance
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