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Unlocking the biology of RAGE in diabetic microvascular complications
Open accessAbstract
The discovery of the receptor for advanced glycation end-products (RAGE) set the stage for the elucidation of important mechanisms underpinning diabetic complications. RAGE transduces the signals of advanced glycation end-products (AGEs), proinflammatory S100/calgranulins, and high mobility group box 1 (HMGB1), and is a one of a family of receptors for lysophosphatidic acid (LPA). These ligand tales weave a theme of vascular perturbation and inflammation linked to the pathogenesis of the chronic complications of diabetes. Once deemed implausible, this concept of inflammatory cues participating in diabetic complications is now supported by a plethora of experimental evidence in the macro- and microvasculature. We review the biology of ligand-RAGE signal transduction and its roles in diabetic microvascular complications, from animal models to human subjects.
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“RAGE, a member of the immunoglobulin superfamily of pattern recognition receptors, is not known to be related to oxytocin or oxytocin signalling22–33.”
From Vascular RAGE transports oxytocin into the brain to elicit its maternal bonding behaviour in mice (2019) · cites this paper as [24]
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Receptor for Advanced Glycation End Products (RAGEs) and Experimental Diabetic Neuropathy
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Mirza, O. A., Iftekhar, M. F., Hussain, R., Din, H.-U., Kumar, A., & Ibrahim, M. T. (2022) · Pakistan Journal of Medical and Health Sciences · doi:10.53350/pjmhs22164833
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Bone health in diabetes mellitus
Hoffmanová, P., Galuška, D., Kaňková, K., & Goldbergová, M. P. (2026) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-026-10091-0
Metadata
- Authors
- Manigrasso, M. B., Juranek, J., Ramasamy, R., & Schmidt, A. M.
- Affiliations
- NYU Langone Health (US)
- Venue
- Trends in Endocrinology & Metabolism
- Publisher
- Elsevier BV
- Published
- 2014-01
- Volume
- 25
- Issue
- 1
- Pages
- 15-22
- ISSN
- 1043-2760 (ISSN-L)
- PMC
- PMC3877224
- OpenAlex
- W2042130085
- Cited by
- 209
- References
- 92
- Citations by year
- 2026: 9 · 2025: 13 · 2024: 13 · 2023: 14 · 2022: 15 · 2021: 19 · 2020: 16 · 2019: 17 · 2018: 11 · 2017: 16 · 2016: 21 · 2015: 22 · 2014: 19
- FWCI
- 2.17
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Trends in Endocrinology and Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (P01HL060901)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
- Health Sciences › Medicine › Nephrology › Chronic Kidney Disease and Diabetes
- Keywords
- receptor for advanced glycation end products, RAGE, advanced glycation end products, diabetic microvascular complications, S100/calgranulins, high mobility group box 1, lysophosphatidic acid receptor, inflammation, vascular dysfunction, signal transduction, diabetes complications
- MeSH terms
- Receptor for Advanced Glycation End Products, Formins, Animals, Carrier Proteins, Diabetic Angiopathies, Diabetic Nephropathies, Diabetic Retinopathy, Humans, Hyperglycemia, Inflammation, Kidney, Ligands, Receptors, Immunologic, Signal Transduction, Glycation End Products, Advanced, HMGB1 Protein, Leukocyte L1 Antigen Complex, Diabetes Complications
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