Familial Amyloid Polyneuropathy: Receptor for Advanced Glycation End Products-Dependent Triggering of Neuronal Inflammatory and Apoptotic Pathways
Open accessAbstract
Familial amyloid polyneuropathy (FAP) is a neurodegenerative disorder associated with extracellular deposition of mutant transthyretin (TTR) amyloid fibrils, particularly in the peripheral nervous system. We have hypothesized that binding of TTR fibrils to the receptor for advanced glycation end products (RAGE) on critical cellular targets is associated with a destructive stress response underlying peripheral nerve dysfunction. Analysis of nerve biopsy samples from patients with FAP (n = 16) at different stages of disease (0-3), compared with age-matched controls (n = 4), by semiquantitative immunohistology and in situ hybridization showed increased levels of RAGE, beginning at the earliest stages of the disease (FAP 0; p < 0.02) and especially localized in axons. Upregulation of proinflammatory cytokines (tumor necrosis factor-alpha and interleukin-1beta) (approximately threefold; p < 0.02) and the inducible form of nitric oxide synthase (iNOS) ( approximately 2.5-fold; p < 0.04) was also observed in a distribution overlapping RAGE expression. Tyrosine nitration and increased activated caspase-3 in axons from FAP patients (p < 0.03) were apparent. Although these data suggest the presence of ongoing neuronal stress, there was no upregulation of neurotrophins (nerve growth factor and neurotrophin-3) in FAP nerves. Studies on cultured neuronal-like, Schwann, and endothelial cells incubated with TTR fibrils displayed RAGE-dependent expression of cytokines and iNOS at early times (6 and 12 hr, respectively), followed by later (24 hr) activation of caspase-3 and DNA fragmentation. We propose that the interaction of TTR fibrils with RAGE may contribute to cellular stress and toxicity in FAP. Furthermore, there is an apparent lack of responsiveness of Schwann cells in FAP nerve to provide neurotrophic factors.
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RAGE is a well-known mediator of inflammation and is recognized for interacting with soluble oligomers of various amyloid proteins, including TTR and SAA.
“The receptor for advanced glycation end products (RAGE) is a well-known mediator of inflammation and is recognized for interacting with soluble oligomers of various amyloid proteins, including TTR and SAA73,74.”
From Oligomeric cystatin C supports the immunosuppressive activity of myeloid cells through interaction with inhibitory receptors (2025) · cites this paper as [73]
The section on TTR fibrils inducing cell stress reports RAGE-dependent inflammatory cytokine expression, and the introductory passage says RAGE binds fibrillar TTR and amyloid A (page numbers unavailable). The paper does not establish binding to soluble oligomers of TTR or SAA; its cell experiments distinguish fibrillar TTR from soluble TTR, which did not induce the reported responses. (LLM, conf=0.88)
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- Authors
- Sousa, M. M., Du Yan, S., Fernandes, R., Guimarães, A., Stern, D., & Saraiva, M. J.
- Affiliations
- Hospital de Santo António (PT)
- Columbia University (US)
- Instituto de Ciências Biomédicas Albel Salazar (PT)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2001-10-01
- Volume
- 21
- Issue
- 19
- Pages
- 7576-7586
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6762914
- OpenAlex
- W2129227455
- Cited by
- 212
- References
- 45
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 9 · 2023: 8 · 2022: 4 · 2021: 5 · 2020: 8 · 2019: 7 · 2018: 4 · 2017: 8 · 2016: 9 · 2015: 12 · 2014: 16 · 2013: 9 · 2012: 14
- FWCI
- 2.92
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neuroscience (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- KU ScholarWorks (The University of Kansas) (submittedVersion, other-oa)
- Funders
- National Institutes of Health (5p01ag016223-04)
- U.S. Public Health Service
- National Institute on Aging (AG-17490, P01AG017490, AG16223)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Amyloidosis: Diagnosis, Treatment, Outcomes
- Health Sciences › Medicine › Neurology › Peripheral Neuropathies and Disorders
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- hereditary transthyretin amyloidosis, receptor for advanced glycation end products, RAGE, neuroinflammation, neuronal apoptosis, caspase-3, nitric oxide synthase, TNF-α, IL-1β, tyrosine nitration, Schwann cells, nerve growth factor, neurotrophin-3, peripheral nerve dysfunction, neurodegeneration
- MeSH terms
- Receptor for Advanced Glycation End Products, Adolescent, Adult, Biopsy, Cells, Cultured, Humans, Inflammation, Middle Aged, Nerve Growth Factors, Neurons, Prealbumin, Protein Binding, Receptors, Immunologic, RNA, Messenger, Schwann Cells, Sural Nerve, Signal Transduction, Cytokines, Apoptosis, Amyloid Neuropathies, Oxidative Stress, Nitric Oxide Synthase, Macromolecular Substances, Nitric Oxide Synthase Type II
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