Cited by 212Amyloidosis: Diagnosis, Treatment, OutcomesPeripheral Neuropathies and DisordersAlzheimer's disease research and treatments

The DOI matches its Crossref record; 44 of the 45 references it cites were found in a registry or an index.

Familial Amyloid Polyneuropathy: Receptor for Advanced Glycation End Products-Dependent Triggering of Neuronal Inflammatory and Apoptotic Pathways

Open access

Sousa, Mónica Mendes, Du Yan, Shi, Fernandes, Rui, Guimarães, António, Stern, David, Saraiva, Maria João·2001·The Journal of Neuroscience

DOI 10.1523/jneurosci.21-19-07576.2001PMC PMC6762914

Open this paper in CoChat — free account Open PDF

Abstract

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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1523/jneurosci.21-19-07576.2001

Cites

44 of 44 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The biochemistry of apoptosis
Hengartner, M. O. (2000) · Nature · doi:10.1038/35037710 · Cited by 5,779
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160
RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
Yan, S. D., Chen, X., Fu, J., Chen, M., Zhu, H., Roher, A., Slattery, T., Zhao, L., Nagashima, M., Morser, J., et al. (1996) · Nature · doi:10.1038/382685a0 · Cited by 2,012
Self-citation
RAGE Mediates a Novel Proinflammatory Axis
Hofmann, M. A., Drury, S., Fu, C., Qu, W., Taguchi, A., Lu, Y., Avila, C., Kambham, N., Bierhaus, A., Nawroth, P., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80801-6 · Cited by 1,864
Self-citation
Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
Morgan, D., Diamond, D. M., Gottschall, P. E., Ugen, K. E., Dickey, C. A., Hardy, J., Duff, K., Jantzen, P. T., DiCarlo, G., Wilcock, D. M., et al. (2000) · Nature · doi:10.1038/35050116 · Cited by 1,506
Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
Janus, C., Pearson, J., McLaurin, J., Mathews, P. M., Jiang, Y., Schmidt, S. D., Chishti, M. A., Horne, P., Heslin, D., French, J., et al. (2000) · Nature · doi:10.1038/35050110 · Cited by 1,431
Widespread Peroxynitrite-Mediated Damage in Alzheimer’s Disease
Smith, M. A., Richey Harris, P. L., Sayre, L. M., Beckman, J. S., & Perry, G. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-08-02653.1997 · Cited by 1,239
The Receptor for Advanced Glycation End Products (RAGE) Is a Cellular Binding Site for Amphoterin
Hori, O., Brett, J., Slattery, T., Cao, R., Zhang, J., Chen, J. X., Nagashima, M., Lundh, E. R., Vijay, S., Nitecki, D., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.43.25752 · Cited by 1,151
Self-citation
Plaque-independent disruption of neural circuits in Alzheimer’s disease mouse models
Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123
A model for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease.
Hensley, K., Carney, J. M., Mattson, M. P., Aksenova, M., Harris, M., Wu, J. F., Floyd, R. A., & Butterfield, D. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.8.3270 · Cited by 1,086

Show all 45 references

Sorted by citations

Molecular Mechanisms of Amyloidosis
Merlini, G., & Bellotti, V. (2003) · New England Journal of Medicine · doi:10.1056/nejmra023144 · Cited by 1,955
The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses
Schmidt, A. M., Yan, S. D., Yan, S. F., & Stern, D. M. (2001) · Journal of Clinical Investigation · doi:10.1172/jci14002 · Cited by 1,256
Self-citation
Transthyretin (TTR) Cardiac Amyloidosis
Ruberg, F. L., & Berk, J. L. (2012) · Circulation · doi:10.1161/circulationaha.111.078915 · Cited by 710
Glycation, Inflammation, and RAGE: A Scaffold for the Macrovascular Complications of Diabetes and Beyond
Yan, S. F., Ramasamy, R., Naka, Y., & Schmidt, A. M. (2003) · Circulation Research · doi:10.1161/01.res.0000103862.26506.3d · Cited by 513
Hereditary transthyretin amyloidosis: a model of medical progress for a fatal disease
Adams, D., Koike, H., Slama, M., & Coelho, T. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0210-4 · Cited by 469
Amyloidosis-Associated Kidney Disease
Dember, L. M. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006050460 · Cited by 408
Transthyretin (ATTR) amyloidosis: clinical spectrum, molecular pathogenesis and disease-modifying treatments
Sekijima, Y. (2015) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2014-308724 · Cited by 337
Soluble protein oligomers as emerging toxins in Alzheimer’s and other amyloid diseases
Ferreira, S. T., Vieira, M. N. N., & De Felice, F. G. (2007) · IUBMB Life · doi:10.1080/15216540701283882 · Cited by 335
Glycation Induces Formation of Amyloid Cross-β Structure in Albumin
Bouma, B., Kroon-Batenburg, L. M. J., Wu, Y., Brünjes, B., Posthuma, G., Kranenburg, O., de Groot, P. G., Voest, E. E., & Gebbink, M. F. B. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303925200 · Cited by 292
Receptor for advanced glycation endproducts: a multiligand receptor magnifying cell stress in diverse pathologic settings
Stern, D. M., Yan, S. D., Yan, S. F., & Schmidt, A. M. (2002) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00160-6 · Cited by 281
Self-citation
Lysozyme Amyloid Oligomers and Fibrils Induce Cellular Death via Different Apoptotic/Necrotic Pathways
Gharibyan, A. L., Zamotin, V., Yanamandra, K., Moskaleva, O. S., Margulis, B. A., Kostanyan, I. A., & Morozova‐Roche, L. A. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.101 · Cited by 209
Suppression of experimental autoimmune encephalomyelitis by selective blockade of encephalitogenic T-cell infiltration of the central nervous system
Yan, S. S., Wu, Z., Zhang, H. P., Furtado, G. D. C., Chen, X., Yan, S. F., Schmidt, A. M., Brown, C., Stern, A., Lafaille, J. J., et al. (2003) · Nature Medicine · doi:10.1038/nm831 · Cited by 182
Self-citation
A brief overview of amyloids and Alzheimer's disease
Ow, S., & Dunstan, D. E. (2014) · Protein Science · doi:10.1002/pro.2524 · Cited by 188
The sour side of neurodegenerative disorders: the effects of protein glycation
Miranda, H. V., & Outeiro, T. F. (2009) · The Journal of Pathology · doi:10.1002/path.2682 · Cited by 172
The role of advanced glycation end products in various types of neurodegenerative disease: a therapeutic approach
Salahuddin, P., Rabbani, G., & Khan, R. H. (2014) · Cellular & Molecular Biology Letters · doi:10.2478/s11658-014-0205-5 · Cited by 175
Blockade of receptor for advanced glycation endproducts: a new target for therapeutic intervention in diabetic complications and inflammatory disorders
Hudson, B. I., Bucciarelli, L. G., Wendt, T., Sakaguchi, T., Lalla, E., Qu, W., Lu, Y., Lee, L., Stern, D. M., Naka, Y., et al. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.08.030 · Cited by 167
Self-citation
Doxycycline disrupts transthyretin amyloid: evidence from studies in a FAP transgenic mice model
Cardoso, I., & Saraiva, M. (2006) · The FASEB Journal · doi:10.1096/fj.05-4509com · Cited by 161
Self-citation
Pathologies Involving the S100 Proteins and Rage
Heizmann, C. W., Ackermann, G. E., & Galichet, A. (2007) · Springer eBooks · doi:10.1007/978-1-4020-6191-2_5 · Cited by 161
A review on mechanism of inhibition of advanced glycation end products formation by plant derived polyphenolic compounds
Anwar, S., Khan, A. A., Almatroudi, A., Khan, A. A., Alsahli, M. A., Almatroodi, S. A., & Rahmani, A. H. (2021) · Molecular Biology Reports · doi:10.1007/s11033-020-06084-0 · Cited by 158
RAGE: A Multi-Ligand Receptor Unveiling Novel Insights in Health and Disease
Alexiou, P., Chatzopoulou, M., Pegklidou, K., & Demopoulos, V. J. (2010) · Current Medicinal Chemistry · doi:10.2174/092986710791331086 · Cited by 140
Tempering the wrath of RAGE: An emerging therapeutic strategy against diabetic complications, neurodegeneration, and inflammation
Yan, S. F., Yan, S. D., Ramasamy, R., & Schmidt, A. M. (2009) · Annals of Medicine · doi:10.1080/07853890902806576 · Cited by 135
The systemic amyloidoses
Buxbaum, J. N. (2003) · Current Opinion in Rheumatology · doi:10.1097/00002281-200401000-00013 · Cited by 131
4 ′‐iodo‐4′‐Deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: screening for TTR fibril disrupters
Cardoso, I., Merlini, G., & Saraiva, M. J. (2003) · The FASEB Journal · doi:10.1096/fj.02-0764com · Cited by 130
Self-citation
The Clinical Relevance of Advanced Glycation Endproducts (AGE) and Recent Developments in Pharmaceutics to Reduce AGE Accumulation
Smit, A. J., & Lutgers, H. L. (2004) · Current Medicinal Chemistry · doi:10.2174/0929867043364342 · Cited by 133
Neurodegeneration in familial amyloid polyneuropathy: from pathology to molecular signaling
Sousa, M. M., & Saraiva, M. J. (2003) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2003.11.002 · Cited by 132
Self-citation
The neuroinflammatory role of Schwann cells in disease
Ydens, E., Lornet, G., Smits, V., Goethals, S., Timmerman, V., & Janssens, S. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.03.005 · Cited by 122
Impaired neuronal migration and endochondral ossification in Pex7 knockout mice: a model for rhizomelic chondrodysplasia punctata
Brites, P. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg236 · Cited by 116
Schwann cell and endothelial cell damage in transthyretin familial amyloid polyneuropathy
Koike, H., Ikeda, S., Takahashi, M., Kawagashira, Y., Iijima, M., Misumi, Y., Ando, Y., Ikeda, S.-I., Katsuno, M., & Sobue, G. (2016) · Neurology · doi:10.1212/wnl.0000000000003362 · Cited by 109
Evidence for Early Cytotoxic Aggregates in Transgenic Mice for Human Transthyretin Leu55Pro
Sousa, M. M., Fernandes, R., Palha, J. A., Taboada, A., Vieira, P., & Saraiva, M. J. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64469-0 · Cited by 108
Self-citation
Risk of transmission of systemic transthyretin amyloidosis after domino liver transplantation
Lladó, L., Baliellas, C., Casasnovas, C., Ferrer, I., Fabregat, J., Ramos, E., Castellote, J., Torras, J., Xiol, X., & Rafecas, A. (2010) · Liver Transplantation · doi:10.1002/lt.22174 · Cited by 103
Purple Sweet Potato Color Ameliorates Cognition Deficits and Attenuates Oxidative Damage and Inflammation in Aging Mouse Brain Induced by D‐Galactose
Shan, Q., Lu, J. L., Zheng, Y., Li, J., Zhou, Z., Hu, B., Zhang, Z.-F., Fan, S., Mao, Z., Wang, Y., et al. (2009) · BioMed Research International · doi:10.1155/2009/564737 · Cited by 101
Argpyrimidine, a methylglyoxal-derived advanced glycation end-product in familial amyloidotic polyneuropathy
Gomes, R. A., Silva, M. S., Quintas, A., CORDEIRO, C. A., Freire, A., Paulino, J., MARTINS, A., Monteiro, E., Barroso, E., & Freire, A. P. (2005) · Biochemical Journal · doi:10.1042/bj20040833 · Cited by 102
PPARα-activation results in enhanced carnitine biosynthesis and OCTN2-mediated hepatic carnitine accumulation
van Vlies, N., Ferdinandusse, S., Turkenburg, M., Wanders, R. J. A., & Vaz, F. M. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.07.001 · Cited by 98
RAGE–TXNIP axis is required for S100B-promoted Schwann cell migration, fibronectin expression and cytokine secretion
Sbai, O., Devi, T. S., Melone, M. A. B., Feron, F. P., Khrestchatisky, M., Singh, L. P., & Perrone, L. (2010) · Journal of Cell Science · doi:10.1242/jcs.074674 · Cited by 96
Electrophysiological Manifestations of Cardiac Amyloidosis
Hartnett, J., Jaber, W. A., Maurer, M. S., Sperry, B. W., Hanna, M. A., Collier, P. H., Patel, D. R., Wazni, O. M., & Donnellan, E. (2021) · JACC CardioOncology · doi:10.1016/j.jaccao.2021.07.010 · Cited by 99
AGE-RAGE axis culminates into multiple pathogenic processes: a central road to neurodegeneration
Bhattacharya, R., Alam, R., Kamal, M. A., Seo, K. J., & Singh, L. R. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1155175 · Cited by 96
The S100B/RAGE Axis in Alzheimer's Disease
Leclerc, E., Sturchler, E., & Vetter, S. W. (2010) · Cardiovascular Psychiatry and Neurology · doi:10.1155/2010/539581 · Cited by 97
A New Face for Old Antibiotics: Tetracyclines in Treatment of Amyloidoses
Stoilova, T., Colombo, L., Forloni, G., Tagliavini, F., & Salmona, M. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400161p · Cited by 97
Neuroinflammation in the peripheral nerve: Cause, modulator, or bystander in peripheral neuropathies?
Martini, R., & Willison, H. J. (2015) · Glia · doi:10.1002/glia.22899 · Cited by 92
UNRESOLVED ISSUES IN DIALYSIS: Dialysis‐Related Amyloidosis: Late Finding or Hidden Epidemic?
Dember, L. M., & Jaber, B. L. (2006) · Seminars in Dialysis · doi:10.1111/j.1525-139x.2006.00134.x · Cited by 88
Diagnostic hallmarks and pitfalls in late-onset progressive transthyretin-related amyloid-neuropathy
Dohrn, M. F., Röcken, C., Bleecker, J. D., Martin, J., Vorgerd, M., den Bergh, P. Y. K. V., Ferbert, A., Hinderhofer, K., Schröder, J. M., Weis, J., et al. (2013) · Journal of Neurology · doi:10.1007/s00415-013-7124-7 · Cited by 87
Endoplasmic Reticulum Stress Associated with Extracellular Aggregates
Teixeira, P. F., Cerca, F., Santos, S. D., & Saraiva, M. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602302200 · Cited by 80
Self-citation
Up‐regulation of the extracellular matrix remodeling genes, biglycan, neutrophil gelatinase‐associated lipocalin and matrix metalloproteinase‐9 in familial amyloid polyneuropathy
Sousa, M. M., do Amaral, B., Guimarães, A., & Saraiva, M. J. (2004) · The FASEB Journal · doi:10.1096/fj.04-2022fje · Cited by 80
Self-citation
A phytol-enriched diet induces changes in fatty acid metabolism in mice both via PPARα-dependent and -independent pathways
Gloerich, J., van Vlies, N., Jansen, G. A., Denis, S. W., Ruiter, J. P. N., van Werkhoven, M. A., Durán, M., Vaz, F. M., Wanders, R. J. A., & Ferdinandusse, S. (2005) · Journal of Lipid Research · doi:10.1194/jlr.m400337-jlr200 · Cited by 80
Biology of diabetic neuropathy
Vincent, A. M., Calabek, B., Roberts, L., & Feldman, E. L. (2013) · Handbook of clinical neurology · doi:10.1016/b978-0-444-52902-2.00034-5 · Cited by 80
Transthyretin oligomers induce calcium influx via voltage‐gated calcium channels
Hou, X., Parkington, H. C., Coleman, H. A., Mechler, Á., Martin, L. L., Aguilar, M., & Small, D. H. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04210.x · Cited by 76
Quantitative sensation and autonomic test abnormalities in transthyretin amyloidosis polyneuropathy
Kim, D. H., Zeldenrust, S. R., Low, P. A., & Dyck, P. J. B. (2009) · Muscle & Nerve · doi:10.1002/mus.21332 · Cited by 72
Food advanced glycation end products as potential endocrine disruptors: An emerging threat to contemporary and future generation
Ravichandran, G., Lakshmanan, D. K., Raju, K., Elangovan, A., Nambirajan, G., Devanesan, A. A., & Thilagar, S. (2019) · Environment International · doi:10.1016/j.envint.2018.12.032 · Cited by 70
The role of transthyretin in cell biology: impact on human pathophysiology
Magalhães, J., Eira, J., & Liz, M. A. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03899-3 · Cited by 69
Inflammatory profiling of patients with familial amyloid polyneuropathy
Azevedo, E. P., Guimaraes-Costa, A. B., Bandeira-Melo, C., Chimelli, L., Waddington-Cruz, M., Saraiva, E. M., Palhano, F. L., & Foguel, D. (2019) · BMC Neurology · doi:10.1186/s12883-019-1369-4 · Cited by 66
The heat shock response modulates transthyretin deposition in the peripheral and autonomic nervous systems
Santos, S. D., Fernandes, R., & Saraiva, M. J. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.04.001 · Cited by 69
Self-citation
Hereditary transthyretin-related amyloidosis
Finsterer, J., Iglseder, S., Wanschitz, J., Topakian, R., Löscher, W. N., & Grisold, W. (2018) · Acta Neurologica Scandinavica · doi:10.1111/ane.13035 · Cited by 64
Deposition and passage of transthyretin through the blood-nerve barrier in recipients of familial amyloid polyneuropathy livers
Sousa, M. M., Ferrão, J., Fernandes, R., Guimarães, A., Geraldes, J., Perdigoto, R., Tomé, L., Mota, O., Negrão, L., Furtado, A. L., et al. (2004) · Laboratory Investigation · doi:10.1038/labinvest.3700107 · Cited by 63
Self-citation
Pathology of human diabetic neuropathy
Malik, R. A. (2014) · Handbook of clinical neurology · doi:10.1016/b978-0-444-53480-4.00016-3 · Cited by 61
RAGE: A journey from the complications of diabetes to disorders of the nervous system – striking a fine balance between injury and repair
Rong, L., Gooch, C. L., Szabolcs, M., Herold, K. C., Lalla, E., Hays, A. P., Yan, S. F., Yan, S. S. D., & Schmidt, A. M. (2005) · Restorative Neurology and Neuroscience · doi:10.3233/rnn-2005-00322 · Cited by 58
Hereditary transthyretin amyloidosis: molecular basis and therapeutical strategies
Saraiva, M. J. (2002) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399402004647 · Cited by 57
Self-citation
Activation of ERK1/2 MAP kinases in Familial Amyloidotic Polyneuropathy
Monteiro, F. A., Sousa, M. M., Cardoso, I., do Amaral, B., Guimarães, A., & Saraiva, M. J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03716.x · Cited by 57
Self-citation
Transthyretin Deposition in Articular Cartilage: A Novel Mechanism in the Pathogenesis of Osteoarthritis
Akasaki, Y., Reixach, N., Matsuzaki, T., Álvarez-García, Ó., Olmer, M., Iwamoto, Y., Buxbaum, J. N., & Lotz, M. (2015) · Arthritis & Rheumatology · doi:10.1002/art.39178 · Cited by 56
Induced Pluripotent Stem Cell Modeling of Multisystemic, Hereditary Transthyretin Amyloidosis
Leung, A., Nah, S., Reid, W., Ebata, A., Koch, C. M., Monti, S., Genereux, J. C., Wiseman, R. L., Wolozin, B. L., Connors, L. H., et al. (2013) · Stem Cell Reports · doi:10.1016/j.stemcr.2013.10.003 · Cited by 54
Isorhynchophylline improves learning and memory impairments induced by D-galactose in mice
Xian, Y., Su, Z., Chen, J., Lai, X., Mao, Q., Cheng, C. H. K., Ip, S., & Lin, Z. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.06.011 · Cited by 53
Role of aggregated medin in the pathogenesis of thoracic aortic aneurysm and dissection
Peng, S., Larsson, A., Wassberg, E., Gerwins, P., Thelin, S., Fu, X., & Westermark, P. (2007) · Laboratory Investigation · doi:10.1038/labinvest.3700679 · Cited by 54
Metabolism of phytol to phytanic acid in the mouse, and the role of PPARα in its regulation
Gloerich, J., van den Brink, D. M., Ruiter, J. P. N., van Vlies, N., Vaz, F. M., Wanders, R. J. A., & Ferdinandusse, S. (2006) · Journal of Lipid Research · doi:10.1194/jlr.m600050-jlr200 · Cited by 53
Curcumin: A multi-target disease-modifying agent for late-stage transthyretin amyloidosis
Ferreira, N., Gonçalves, N. P., Saraiva, M. J., & Almeida, M. R. (2016) · Scientific Reports · doi:10.1038/srep26623 · Cited by 55
Self-citation
Interleukin-1 signaling pathway as a therapeutic target in transthyretin amyloidosis
Gonçalves, N. P., Vieira, P., & Saraiva, M. J. (2014) · Amyloid · doi:10.3109/13506129.2014.927759 · Cited by 50
Self-citation
Role of RAGE in the Pathogenesis of Neurological Disorders
Juranek, J., Mukherjee, K., Kordas, B., Załęcki, M., Korytko, A., Zglejc-Waszak, K., Szuszkiewicz, J., & Banach, M. (2022) · Neuroscience Bulletin · doi:10.1007/s12264-022-00878-x · Cited by 45
RAGE expression is up-regulated in human cerebral ischemia and pMCAO rats
Zhai, D., Kong, Q., Xu, W., Bai, S., Peng, H., Zhao, K., Li, G., Wang, D., Sun, B., Wang, J., et al. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.08.077 · Cited by 46
Pivotal role of AGE-RAGE axis in brain aging with current interventions
Vitorakis, N., & Piperi, C. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102429 · Cited by 48
Pattern recognition receptors in chronic pain: Mechanisms and therapeutic implications
Kato, J., Agalave, N. M., & Svensson, C. I. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.06.039 · Cited by 44
Emerging treatment approaches for the systemic amyloidoses.
Dember, L. (2005) · Kidney International · doi:10.1111/j.1523-1755.2005.00535.x · Cited by 45
Carvedilol treatment reduces transthyretin deposition in a familial amyloidotic polyneuropathy mouse model
Macedo, B., Magalhães, J., Batista, A. R., & Saraiva, M. J. (2010) · Pharmacological Research · doi:10.1016/j.phrs.2010.08.001 · Cited by 39
Self-citation
Targeting transthyretin ‐ Mechanism‐based treatment approaches and future perspectives in hereditary amyloidosis
Dohrn, M. F., Ihne-Schubert, S. M., Hegenbart, U., Medina, J., Zuchner, S. L., Coelho, T., & Hahn, K. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15233 · Cited by 39
Amyloidogenic and non-amyloidogenic transthyretin variants interact differently with human cardiomyocytes: insights into early events of non-fibrillar tissue damage
Manral, P., & Reixach, N. (2014) · Bioscience Reports · doi:10.1042/bsr20140155 · Cited by 39
Neuroprotective effects of folic acid on experimental diabetic peripheral neuropathy
Yilmaz, M., Aktuğ, H., Oltulu, F., & Erbaş, O. (2013) · Toxicology and Industrial Health · doi:10.1177/0748233713511513 · Cited by 38
Advances in protein misfolding, amyloidosis and its correlation with human diseases
Kundu, D., Prerna, K., Chaurasia, R., Bharty, M. K., & Dubey, V. K. (2020) · 3 Biotech · doi:10.1007/s13205-020-2166-x · Cited by 40
Amyloid Proteins and Peripheral Neuropathy
Albariqi, M. M. H., Engelsman, S., Eijkelkamp, N., & Höppener, J. W. M. (2020) · Cells · doi:10.3390/cells9061553 · Cited by 41
Presence of variant transthyretin in aqueous humor of a patient with familial amyloidotic polyneuropathy after liver transplantation
Haraoka, K., Ando, Y., Ando, E., Sun, X., 中村政明, Terazaki, H., Misumi, S., Tanoue, Y., Tajiri, T., Shoji, S., et al. (2002) · Amyloid · doi:10.3109/13506120209114101 · Cited by 35
Unveiling the Role of Schwann Cell Plasticity in the Pathogenesis of Diabetic Peripheral Neuropathy
Razak, N. H. A., Idris, J., Hassan, N. H., Zaini, F., Muhamad, N., & Daud, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910785 · Cited by 37
Misfolding of Amyloidogenic Proteins and Their Interactions with Membranes
Relini, A., Marano, N., & Gliozzi, A. (2013) · Biomolecules · doi:10.3390/biom4010020 · Cited by 34
Corneal sub‐basal whorl‐like nerve plexus: a landmark for early and follow‐up evaluation in transthyretin familial amyloid polyneuropathy
Zhang, Y., Liu, Z., Zhang, Y., Wang, H., Liu, X., Zhang, S., Liu, X., & Fan, D. (2020) · European Journal of Neurology · doi:10.1111/ene.14563 · Cited by 34
In vitro inhibition of transthyretin aggregate‐induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE)
Monteiro, F. A., Cardoso, I., Sousa, M. M., & Saraiva, M. J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.05.020 · Cited by 34
Self-citation
Cholesterol and anionic phospholipids increase the binding of amyloidogenic transthyretin to lipid membranes
Hou, X., Mechler, Á., Martin, L. L., Aguilar, M., & Small, D. H. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.09.018 · Cited by 34
Differential expression of Cathepsin E in transthyretin amyloidosis: from neuropathology to the immune system
Gonçalves, N. P., Moreira, J., Martins, D. F., Vieira, P., Obici, L. P., Merlini, G., Saraiva, M., & Saraiva, M. J. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-017-0891-9 · Cited by 35
Self-citation
Glycated proteome: From reaction to intervention
Kulkarni, M. J., Korwar, A. M., Mary, S., Bhonsle, H. S., & Giri, A. P. (2012) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201200101 · Cited by 32
Clearance of extracellular misfolded proteins in systemic amyloidosis: Experience with transthyretin
Almeida, M. R., & Saraiva, M. J. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.07.029 · Cited by 32
Self-citation
Drug-induced Glomerulonephritis: The Spectre of Biotherapeutic and Antisense Oligonucleotide Immune Activation in the Kidney
Frazier, K. S., & Obert, L. (2018) · Toxicologic Pathology · doi:10.1177/0192623318789399 · Cited by 32
Crosstalk Between Calcium, Amyloid β and the Receptor for Advanced Glycation Endproducts in Alzheimer's Disease
Leclerc, E., Sturchler, E., Vetter, S. W., & Heizmann, C. W. (2009) · Reviews in the Neurosciences · doi:10.1515/revneuro.2009.20.2.95 · Cited by 31
Polymer-doxycycline conjugates as fibril disrupters: An approach towards the treatment of a rare amyloidotic disease
Conejos‐Sánchez, I., Cardoso, I., Oteo, M., Romero, E., Paul, A., Ruiz‐Saurí, A., Morcillo, M. Á., Saraiva, M. J., & Vicent, M. J. (2014) · Journal of Controlled Release · doi:10.1016/j.jconrel.2014.12.003 · Cited by 30
Self-citation
Proteostasis Perturbations and Their Roles in Causing Sterile Inflammation and Autoinflammatory Diseases
Papendorf, J. J., Krüger, E., & Ebstein, F. (2022) · Cells · doi:10.3390/cells11091422 · Cited by 34
Underlying Immune Disorder May Predispose Some Transthyretin Amyloidosis Subjects to Inotersen-Mediated Thrombocytopenia
Narayanan, P., Curtis, B. R., Shen, L., Schneider, E., Tami, J. A., Paz, S., Burel, S. A., Tai, L.-J., Machemer, T., Kwoh, T. J., et al. (2020) · Nucleic Acid Therapeutics · doi:10.1089/nat.2019.0829 · Cited by 29
TRPM8 and Nav1.8 sodium channels are required for transthyretin-induced calcium influx in growth cones of small-diameter TrkA-positive sensory neurons
Gasperini, R., Hou, X., Parkington, H. C., Coleman, H., Klaver, D. W., Vincent, A. J., Foa, L. C., & Small, D. H. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-19 · Cited by 31
Sweet and Sour - Oxidative and Carbonyl Stress in Neurological Disorders
Harris, R. A., & Amor, S. (2011) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152711794488656 · Cited by 27
The inflammatory response to sciatic nerve injury in a familial amyloidotic polyneuropathy mouse model
Gonçalves, N. P., Teixeira-Coelho, M., & Saraiva, M. J. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.04.030 · Cited by 27
Self-citation
Clusterin Overexpression and Its Possible Protective Role in Transthyretin Deposition in Familial Amyloidotic Polyneuropathy
Magalhães, J., & Saraiva, M. J. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31823a44f4 · Cited by 27
Self-citation
Modern Treatment of Amyloidosis
Dember, L. M. (2008) · Journal of the American Society of Nephrology · doi:10.1681/asn.2008070793 · Cited by 26
Bacteroides fragilis Enterotoxin Upregulates Intercellular Adhesion Molecule-1 in Endothelial Cells via an Aldose Reductase-, MAPK-, and NF-κB–Dependent Pathway, Leading to Monocyte Adhesion to Endothelial Cells
Roh, H. C., Yoo, D. Y., Ko, S. H., Kim, Y.-J., & Kim, J. M. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1101226 · Cited by 26
Biomarkers in the Assessment of Therapies for Familial Amyloidotic Polyneuropathy
Macedo, B., Batista, A. R., do Amaral, B., & Saraiva, M. J. (2007) · Molecular Medicine · doi:10.2119/2007-00068.macedo · Cited by 26
Self-citation
Contributions of Animal Models to the Mechanisms and Therapies of Transthyretin Amyloidosis
Ibrahim, R. B., Liu, Y., Yeh, S.-Y., & Tsai, J. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00338 · Cited by 25
RAGE signaling mediates post-injury arterial neointima formation by suppression of liver kinase B1 and AMPK activity
Yu, W., Liu‐Bryan, R., Stevens, S., Damanahalli, J. K., & Terkeltaub, R. A. (2012) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2012.04.001 · Cited by 25
The receptor for advanced glycation endproducts is a mediator of toxicity by IAPP and other proteotoxic aggregates: Establishing and exploiting common ground for novel amyloidosis therapies
Abedini, A., Derk, J., & Schmidt, A. M. (2018) · Protein Science · doi:10.1002/pro.3425 · Cited by 25
Anaemia of chronic disease in AA amyloidosis is associated with allele 2 of the interleukin‐1β‐511 promoter gene and raised levels of interleukin‐1β and interleukin‐18
Maury, C. P. J., Liljeström, M., Laiho, K., Tiitinen, S., Kaarela, K., & Hurme, M. (2004) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2004.01353.x · Cited by 26

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)
ORCID: Sousa, Mónica Mendes
Fernandes, Rui
Saraiva, Maria João
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
DOI: 10.1523/jneurosci.21-19-07576.2001
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: Health Sciences › Medicine › Internal Medicine › Amyloidosis: Diagnosis, Treatment, Outcomes
Health Sciences › Medicine › Clinical Neurology › Peripheral Neuropathies and Disorders
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Familial Amyloid Polyneuropathy: Receptor for Advanced Glycation End Products-Dependent Triggering of Neuronal Inflammatory and Apoptotic Pathways

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks