The Receptor for Advanced Glycation End Products (RAGE) Specifically Recognizes Methylglyoxal-Derived AGEs
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Diabetes-induced hyperglycemia increases the extracellular concentration of methylglyoxal. Methylglyoxal-derived hydroimidazolones (MG-H) form advanced glycation end products (AGEs) that accumulate in the serum of diabetic patients. The binding of hydroimidozolones to the receptor for AGEs (RAGE) results in long-term complications of diabetes typified by vascular and neuronal injury. Here we show that binding of methylglyoxal-modified albumin to RAGE results in signal transduction. Chemically synthesized peptides containing hydroimidozolones bind specifically to the V domain of RAGE with nanomolar affinity. The solution structure of an MG-H1–V domain complex revealed that the hydroimidazolone moiety forms multiple contacts with a positively charged surface on the V domain. The high affinity and specificity of hydroimidozolones binding to the V domain of RAGE suggest that they are the primary AGE structures that give rise to AGEs–RAGE pathologies.
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The interaction of AGE-RAGE triggers intracellular and extracellular signaling pathways through activation of ERK1/2, MAPK, PI3K, AKT, NADPH oxidase, and NF-κB.
“The interaction of AGE-RAGE triggers intracellular and extracellular signaling pathways through the activation of extracellular signal-regulated kinases 1 and 2 (ERK1/2), mitogen-activated protein kinases (MAPK), phosphoinositide 3-kinase (PI3K), protein kinase B (AKT), NADPH oxidase, and nuclear factor-κB (NF-κB).”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [40]
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- Authors
- Xue, J., Ray, R., Singer, D., Böhme, D., Burz, D. S., Rai, V., Hoffmann, R., & Shekhtman, A.
- Affiliations
- State University of New York (US)
- Institute of Life Sciences (IN)
- Leipzig University (DE)
- Universität Leipzig , , ,
- Corresponding author
- Shekhtman, Alexander
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2014-05-05
- Volume
- 53
- Issue
- 20
- Pages
- 3327-3335
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- PMC
- PMC4038343
- OpenAlex
- W2075351997
- Cited by
- 186
- References
- 47
- Citations by year
- 2026: 8 · 2025: 13 · 2024: 14 · 2023: 18 · 2022: 22 · 2021: 22 · 2020: 16 · 2019: 19 · 2018: 7 · 2017: 14 · 2016: 14 · 2015: 15 · 2014: 4
- FWCI
- 10.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Biochemistry (publishedVersion, other-oa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM085006)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Immunology and Microbiology › Immunology › Galectins and Cancer Biology
- Keywords
- receptor for advanced glycation end products, RAGE, methylglyoxal, hydroimidazolone, advanced glycation end products, V domain, signal transduction, peptide binding, protein-protein complex structure, diabetes complications, hyperglycemia
- MeSH terms
- Receptor for Advanced Glycation End Products, Cell Line, Humans, Pyruvaldehyde, Receptors, Immunologic, Signal Transduction, Glycation End Products, Advanced, Protein Structure, Secondary, Protein Structure, Tertiary
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