Table of Contents
Cardiovascular Psychiatry and Neurology
Volume 2010, Article ID 539581, 11 pages
http://dx.doi.org/10.1155/2010/539581
Review Article

The S100B/RAGE Axis in Alzheimer's Disease

1Department of Pharmaceutical Sciences, North Dakota State University, Dept. 2665, P.O. Box 6050, Fargo, ND 58108-6050, USA
2Department of Drug Discovery, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA

Received 4 March 2010; Accepted 6 May 2010

Academic Editor: Rosario Donato

Copyright © 2010 Estelle Leclerc et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. L. E. Hebert, P. A. Scherr, J. L. Bienias, D. A. Bennett, and D. A. Evans, “Alzheimer disease in the US population: prevalence estimates using the 2000 census,” Archives of Neurology, vol. 60, no. 8, pp. 1119–1122, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  2. B. Muller-Hill and K. Beyreuther, “Molecular biology of Alzheimer's disease,” Annual Review of Biochemistry, vol. 58, pp. 287–307, 1989. View at Google Scholar · View at Scopus
  3. G. G. Glenner and C. W. Wong, “Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein,” Biochemical and Biophysical Research Communications, vol. 120, no. 3, pp. 885–890, 1984. View at Google Scholar · View at Scopus
  4. M. A. Lovell, J. D. Robertson, W. J. Teesdale, J. L. Campbell, and W. R. Markesbery, “Copper, iron and zinc in Alzheimer's disease senile plaques,” Journal of the Neurological Sciences, vol. 158, no. 1, pp. 47–52, 1998. View at Publisher · View at Google Scholar · View at Scopus
  5. K. S. Kosik, C. L. Joachim, and D. J. Selkoe, “Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease,” Proceedings of the National Academy of Sciences of the United States of America, vol. 83, no. 11, pp. 4044–4048, 1986. View at Google Scholar · View at Scopus
  6. E. Thies and E.-M. Mandelkow, “Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1,” Journal of Neuroscience, vol. 27, no. 11, pp. 2896–2907, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  7. I. E. Vega, E. E. Traverso, and E. E. Traverso, “A novel calcium-binding protein is associated with tau proteins in tauopathy,” Journal of Neurochemistry, vol. 106, no. 1, pp. 96–106, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  8. C. Supnet and I. Bezprozvanny, “The dysregulation of intracellular calcium in Alzheimer disease,” Cell Calcium, vol. 47, no. 2, pp. 183–189, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  9. R. E. Mrak and W. S. T. Griffin, “The role of activated astrocytes and of the neurotrophic cytokine S100B in the pathogenesis of Alzheimer's disease,” Neurobiology of Aging, vol. 22, no. 6, pp. 915–922, 2001. View at Publisher · View at Google Scholar · View at Scopus
  10. A. Boom, R. Pochet, and R. Pochet, “Astrocytic calcium/zinc binding protein S100A6 over expression in Alzheimer's disease and in PS1/APP transgenic mice models,” Biochimica et Biophysica Acta, vol. 1742, no. 1–3, pp. 161–168, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  11. H. Akiyama, K. Ikeda, M. Katoh, E. G. McGeer, and P. L. McGeer, “Expression of MRP14, 27E10, interferon-α and leukocyte common antigen by reactive microglia in postmortem human brain tissue,” Journal of Neuroimmunology, vol. 50, no. 2, pp. 195–201, 1994. View at Publisher · View at Google Scholar · View at Scopus
  12. C. E. Shepherd, J. Goyette, V. Utter, F. Rahimi, Z. Yang, C. L. Geczy, and G. M. Halliday, “Inflammatory S100A9 and S100A12 proteins in Alzheimer's disease,” Neurobiology of Aging, vol. 27, no. 11, pp. 1554–1563, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  13. S. D. Yan, X. Chen, and X. Chen, “RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease,” Nature, vol. 382, no. 6593, pp. 685–691, 1996. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  14. M. C. Miller, R. Tavares, and R. Tavares, “Hippocampal RAGE immunoreactivity in early and advanced Alzheimer's disease,” Brain Research, vol. 1230, pp. 273–280, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  15. A. M. Schmidt, M. Vianna, and M. Vianna, “Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung which are present on the endothelial cell surface,” The Journal of Biological Chemistry, vol. 267, no. 21, pp. 14987–14997, 1992. View at Google Scholar · View at Scopus
  16. M. Neeper, A. M. Schmidt, and A. M. Schmidt, “Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins,” The Journal of Biological Chemistry, vol. 267, no. 21, pp. 14998–15004, 1992. View at Google Scholar · View at Scopus
  17. N. Ahmed, U. Ahmed, P. J. Thornalley, K. Hager, G. Fleischer, and G. Münch, “Protein glycation, oxidation and nitration adduct residues and free adducts of cerebrospinal fluid in Alzheimer's disease and link to cognitive impairment,” Journal of Neurochemistry, vol. 92, no. 2, pp. 255–263, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  18. J. Li and A. M. Schmidt, “Characterization and functional analysis of the promoter of RAGE, the receptor for advanced glycation end products,” The Journal of Biological Chemistry, vol. 272, no. 26, pp. 16498–16506, 1997. View at Publisher · View at Google Scholar · View at Scopus
  19. A. Bierhaus, S. Schiekofer, and S. Schiekofer, “Diabetes-associated sustained activation of the transcription factor nuclear factor-κB,” Diabetes, vol. 50, no. 12, pp. 2792–2808, 2001. View at Google Scholar · View at Scopus
  20. A.-M. Schmidt, M. Hofmann, A. Taguchi, S. D. Yan, and D. M. Stern, “RAGE: a multiligand receptor contributing to the cellular response in diabetic vasculopathy and inflammation,” Seminars in Thrombosis and Hemostasis, vol. 26, no. 5, pp. 485–493, 2000. View at Google Scholar · View at Scopus
  21. D. W. Dickson, S. Sinicropi, S.-H. Yen, L.-W. Ko, L. A. Mattiace, R. Bucala, and H. Vlassara, “Glycation and microglial reaction in lesions of Alzheimer's disease,” Neurobiology of Aging, vol. 17, no. 5, pp. 733–743, 1996. View at Publisher · View at Google Scholar · View at Scopus
  22. N. Sasaki, R. Fukatsu, and R. Fukatsu, “Advanced glycation end products in Alzheimer's disease and other neurodegenerative diseases,” American Journal of Pathology, vol. 153, no. 4, pp. 1149–1155, 1998. View at Google Scholar · View at Scopus
  23. M. A. Smith, S. Taneda, and S. Taneda, “Advanced Maillard reaction end products are associated with Alzheimer disease pathology,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 12, pp. 5710–5714, 1994. View at Publisher · View at Google Scholar · View at Scopus
  24. M. M. Sousa, S. D. Yan, D. Stern, and M. J. Saraiva, “Interaction of the receptor for advanced glycation end products (RAGE) with transthyretin triggers nuclear transcription factor kB (NF-kB) activation,” Laboratory Investigation, vol. 80, no. 7, pp. 1101–1110, 2000. View at Google Scholar · View at Scopus
  25. E. Stürchler, A. Galichet, M. Weibel, E. Leclerc, and C. W. Heizmann, “Site-specific blockade of RAGE-Vd prevents amyloid-β oligomer neurotoxicity,” Journal of Neuroscience, vol. 28, no. 20, pp. 5149–5158, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  26. K. Takuma, F. Fang, and F. Fang, “RAGE-mediated signaling contributes to intraneuronal transport of amyloid-β and neuronal dysfunction,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 47, pp. 20021–20026, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  27. R. Deane, S. D. Yan, and S. D. Yan, “RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain,” Nature Medicine, vol. 9, no. 7, pp. 907–913, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  28. J. N. Buxbaum, Z. Ye, and Z. Ye, “Transthyretin protects Alzheimer's mice from the behavioral and biochemical effects of Aβ toxicity,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 7, pp. 2681–2686, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  29. O. Hori, J. Brett, T. Slattery et al., “The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of RAGE and amphoterin in the developing nervous system,” The Journal of Biological Chemistry, vol. 270, no. 43, pp. 25752–25761, 1995. View at Publisher · View at Google Scholar · View at Scopus
  30. G. P. Sims, D. C. Rowe, S. T. Rietdijk, R. Herbst, and A. J. Coyle, “HMGB1 and RAGE in inflammation and cancer,” Annual Review of Immunology, vol. 28, pp. 367–388, 2010. View at Google Scholar
  31. C. W. Heizmann, G. E. Ackermann, and A. Galichet, “Pathologies involving the S100 proteins and RAGE,” in Calcium Signalling and Disease, vol. 45 of Subcellular Biochemistry, pp. 93–138, 2007. View at Google Scholar
  32. R. Donato, “Intracellular and extracellular roles of S100 proteins,” Microscopy Research and Technique, vol. 60, no. 6, pp. 540–551, 2003. View at Google Scholar · View at Scopus
  33. D. B. Zimmer, P. Wright Sadosky, and D. J. Weber, “Molecular mechanisms of S100-target protein interactions,” Microscopy Research and Technique, vol. 60, no. 6, pp. 552–559, 2003. View at Google Scholar · View at Scopus
  34. I. Marenholz, R. C. Lovering, and C. W. Heizmann, “An update of the S100 nomenclature,” Biochimica et Biophysica Acta, vol. 1763, no. 11, pp. 1282–1283, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  35. K. Sugaya, T. Fukagawa, and T. Fukagawa, “Three genes in the human MHC class III region near the junction with the class II: gene for receptor of advanced glycosylation end products, PBX2 homeobox gene and a notch homolog, human counterpart of mouse mammary tumor gene int-3,” Genomics, vol. 23, no. 2, pp. 408–419, 1994. View at Publisher · View at Google Scholar · View at Scopus
  36. B. I. Hudson, A. M. Carter, and A. M. Carter, “Identification, classification, and expression of RAGE gene splice variants,” The FASEB Journal, vol. 22, no. 5, pp. 1572–1580, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  37. G. Srikrishna, H. J. Huttunen, L. Johansson, B. Weigle, Y. Yamaguchi, H. Rauvala, and H. H. Freeze, “N-glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth,” Journal of Neurochemistry, vol. 80, no. 6, pp. 998–1008, 2002. View at Publisher · View at Google Scholar · View at Scopus
  38. R. Wilton, M. A. Yousef, P. Saxena, M. Szpunar, and F. J. Stevens, “Expression and purification of recombinant human receptor for advanced glycation endproducts in Escherichia coli,” Protein Expression and Purification, vol. 47, no. 1, pp. 25–35, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  39. M. Osawa, Y. Yamamoto, and Y. Yamamoto, “De-N-glycosylation or G82S mutation of RAGE sensitizes its interaction with advanced glycation endproducts,” Biochimica et Biophysica Acta, vol. 1770, no. 10, pp. 1468–1474, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  40. P. Malherbe, J. G. Richards, H. Gaillard, A. Thompson, C. Diener, A. Schuler, and G. Huber, “cDNA cloning of a novel secreted isoform of the human receptor for advanced glycation end products and characterization of cells co-expressing cell-surface scavenger receptors and Swedish mutant amyloid precursor protein,” Molecular Brain Research, vol. 71, no. 2, pp. 159–170, 1999. View at Publisher · View at Google Scholar · View at Scopus
  41. H. Yonekura, Y. Yamamoto, and Y. Yamamoto, “Novel splice variants of the receptor for advanced glycation end-products expressed in human vascular endothelial cells and pericytes, and their putative roles in diabetes-induced vascular injury,” Biochemical Journal, vol. 370, no. 3, pp. 1097–1109, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  42. C. Schlueter, S. Hauke, A. M. Flohr, P. Rogalla, and J. Bullerdiek, “Tissue-specific expression patterns of the RAGE receptor and its soluble forms—a result of regulated alternative splicing?” Biochimica et Biophysica Acta, vol. 1630, no. 1, pp. 1–6, 2003. View at Publisher · View at Google Scholar · View at Scopus
  43. S. T. Buckley and C. Ehrhardt, “The receptor for advanced glycation end products (RAGE) and the lung,” Journal of Biomedicine & Biotechnology, vol. 2010, Article ID 917108, 11 pages, 2010. View at Publisher · View at Google Scholar · View at PubMed
  44. Q. Ding and J. N. Keller, “Splice variants of the receptor for advanced glycosylation end products (RAGE) in human brain,” Neuroscience Letters, vol. 373, no. 1, pp. 67–72, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  45. A. Galichet, M. Weibel, and C. W. Heizmann, “Calcium-regulated intramembrane proteolysis of the RAGE receptor,” Biochemical and Biophysical Research Communications, vol. 370, no. 1, pp. 1–5, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  46. A. Raucci, S. Cugusi, and S. Cugusi, “A soluble form of the receptor for advanced glycation endproducts (RAGE) is produced by proteolytic cleavage of the membrane-bound form by the sheddase a disintegrin and metalloprotease 10 (ADAM10),” The FASEB Journal, vol. 22, no. 10, pp. 3716–3727, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  47. L. Zhang, M. Bukulin, and M. Bukulin, “Receptor for advanced glycation end products is subjected to protein ectodomain shedding by metalloproteinases,” The Journal of Biological Chemistry, vol. 283, no. 51, pp. 35507–35516, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  48. E. Emanuele, A. D'Angelo, and A. D'Angelo, “Circulating levels of soluble receptor for advanced glycation end products in Alzheimer disease and vascular dementia,” Archives of Neurology, vol. 62, no. 11, pp. 1734–1736, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  49. I. Nozaki, T. Watanabe, and T. Watanabe, “Reduced expression of endogenous secretory receptor for advanced glycation endproducts in hippocampal neurons of Alzheimer's disease brains,” Archives of Histology and Cytology, vol. 70, no. 5, pp. 279–290, 2007. View at Publisher · View at Google Scholar · View at Scopus
  50. E. Kojro and R. Postina, “Regulated proteolysis of RAGE and AbetaPP as possible link between type 2 diabetes mellitus and Alzheimer's disease,” Journal of Alzheimer's Disease, vol. 16, no. 4, pp. 865–878, 2009. View at Google Scholar · View at Scopus
  51. H. Koyama, H. Yamamoto, and Y. Nishizawa, “RAGE and soluble RAGE: potential therapeutic targets for cardiovascular diseases,” Molecular Medicine, vol. 13, no. 11-12, pp. 625–635, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  52. F. Santilli, N. Vazzana, L. G. Bucciarelli, and G. Davì, “Soluble forms of RAGE in human diseases: clinical and therapeutical implications,” Current Medicinal Chemistry, vol. 16, no. 8, pp. 940–952, 2009. View at Publisher · View at Google Scholar · View at Scopus
  53. P. Tesařová, M. Kalousová, M. Jáchymová, O. Mestek, L. Petruzelka, and T. Zima, “Receptor for advanced glycation end products (RAGE)—soluble form (sRAGE) and gene polymorphisms in patients with breast cancer,” Cancer Investigation, vol. 25, no. 8, pp. 720–725, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  54. K. Nakamura, S.-I. Yamagishi, and S.-I. Yamagishi, “Serum levels of soluble form of receptor for advanced glycation end products (sRAGE) are positively associated with circulating AGEs and soluble form of VCAM-1 in patients with type 2 diabetes,” Microvascular Research, vol. 76, no. 1, pp. 52–56, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  55. A. Bierhaus and P. P. Nawroth, “Multiple levels of regulation determine the role of the receptor for AGE (RAGE) as common soil in inflammation, immune responses and diabetes mellitus and its complications,” Diabetologia, vol. 52, no. 11, pp. 2251–2263, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  56. L. R. Ling, C. Gooch, and C. Gooch, “RAGE: a journey from the complications of diabetes to disorders of the nervous system—striking a fine balance between injury and repair,” Restorative Neurology and Neuroscience, vol. 23, no. 5-6, pp. 355–365, 2005. View at Google Scholar · View at Scopus
  57. L. R. Ling, W. Trojaborg, and W. Trojaborg, “Antagonism of RAGE suppresses peripheral nerve regeneration,” The FASEB Journal, vol. 18, no. 15, pp. 1812–1817, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  58. L. L. Rong, S.-F. Yan, and S.-F. Yan, “RAGE modulates peripheral nerve regeneration via recruitment of both inflammatory and axonal outgrowth pathways,” The FASEB Journal, vol. 18, no. 15, pp. 1818–1825, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  59. M. A. Hofmann, S. Drury, and S. Drury, “RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides,” Cell, vol. 97, no. 7, pp. 889–901, 1999. View at Publisher · View at Google Scholar · View at Scopus
  60. B. M. Dattilo, G. Fritz, E. Leclerc, C. W. Vander Kooi, C. W. Heizmann, and W. J. Chazin, “The extracellular region of the receptor for advanced glycation end products is composed of two independent structural units,” Biochemistry, vol. 46, no. 23, pp. 6957–6970, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  61. T. Ostendorp, E. Leclerc, and E. Leclerc, “Structural and functional insights into RAGE activation by multimeric S100B,” The EMBO Journal, vol. 26, no. 16, pp. 3868–3878, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  62. E. Leclerc, G. Fritz, M. Weibel, C. W. Heizmann, and A. Galichet, “S100B and S100A6 differentially modulate cell survival by interacting with distinct RAGE (receptor for advanced glycation end products) immunoglobulin domains,” The Journal of Biological Chemistry, vol. 282, no. 43, pp. 31317–31331, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  63. J. Xie, S. Reverdatto, A. Frolov, R. Hoffmann, D. S. Burz, and A. Shekhtman, “Structural basis for pattern recognition by the receptor for advanced glycation end products (RAGE),” The Journal of Biological Chemistry, vol. 283, no. 40, pp. 27255–27269, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  64. T. Kislinger, C. Fu, and C. Fu, “Nε-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression,” The Journal of Biological Chemistry, vol. 274, no. 44, pp. 31740–31749, 1999. View at Publisher · View at Google Scholar · View at Scopus
  65. E. Uetz-Von Allmen, M. Koch, G. Fritz, and D. F. Legler, “V domain of RAGE interacts with AGEs on prostate carcinoma cells,” Prostate, vol. 68, no. 7, pp. 748–758, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  66. F. A. Monteiro, I. Cardoso, M. M. Sousa, and M. J. Saraiva, “In vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE),” FEBS Letters, vol. 580, no. 14, pp. 3451–3456, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  67. G. Thinakaran and E. H. Koo, “Amyloid precursor protein trafficking, processing, and function,” The Journal of Biological Chemistry, vol. 283, no. 44, pp. 29615–29619, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  68. W. L. Klein, “Aβ toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets,” Neurochemistry International, vol. 41, no. 5, pp. 345–352, 2002. View at Publisher · View at Google Scholar · View at Scopus
  69. K. N. Dahlgren, A. M. Manelli, W. Blaine Stine Jr., L. K. Baker, G. A. Krafft, and M. J. Ladu, “Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability,” The Journal of Biological Chemistry, vol. 277, no. 35, pp. 32046–32053, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  70. C. A. McLean, R. A. Cherny, and R. A. Cherny, “Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease,” Annals of Neurology, vol. 46, no. 6, pp. 860–866, 1999. View at Publisher · View at Google Scholar · View at Scopus
  71. J. P. Cleary, D. M. Walsh, J. J. Hofmeister, G. M. Shankar, M. A. Kuskowski, D. J. Selkoe, and K. H. Ashe, “Natural oligomers of the amyloid-β protein specifically disrupt cognitive function,” Nature Neuroscience, vol. 8, no. 1, pp. 79–84, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  72. D. M. Walsh, I. Klyubin, and I. Klyubin, “Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo,” Nature, vol. 416, no. 6880, pp. 535–539, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  73. M. P. Lambert, A. K. Barlow, and A. K. Barlow, “Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 11, pp. 6448–6453, 1998. View at Google Scholar · View at Scopus
  74. T. H. J. Huang, D.-S. Yang, P. E. Fraser, and A. Chakrabartty, “Alternate aggregation pathways of the Alzheimer β-amyloid peptide: an in vitro model of preamyloid,” The Journal of Biological Chemistry, vol. 275, no. 46, pp. 36436–36440, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  75. D. M. Walsh, I. Klyubin, J. V. Fadeeva, M. J. Rowan, and D. J. Selkoe, “Amyloid-β oligomers: their production, toxicity and therapeutic inhibition,” Biochemical Society Transactions, vol. 30, no. 4, pp. 552–557, 2002. View at Publisher · View at Google Scholar · View at Scopus
  76. D. M. Hartley, D. M. Walsh, and D. M. Walsh, “Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons,” Journal of Neuroscience, vol. 19, no. 20, pp. 8876–8884, 1999. View at Google Scholar · View at Scopus
  77. A. Deshpande, E. Mina, C. Glabe, and J. Busciglio, “Different conformations of amyloid β induce neurotoxicity by distinct mechanisms in human cortical neurons,” Journal of Neuroscience, vol. 26, no. 22, pp. 6011–6018, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  78. M. Wogulis, S. Wright, D. Cunningham, T. Chilcote, K. Powell, and R. E. Rydel, “Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death,” Journal of Neuroscience, vol. 25, no. 5, pp. 1071–1080, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  79. P. I. Moreira, A. I. Duarte, M. S. Santos, A. C. Rego, and C. R. Oliveira, “An integrative view of the role of oxidative stress, mitochondria and insulin in Alzheimer's disease,” Journal of Alzheimer's Disease, vol. 16, no. 4, pp. 741–761, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  80. V. P. Reddy, X. Zhu, G. Perry, and M. A. Smith, “Oxidative stress in diabetes and Alzheimer's disease,” Journal of Alzheimer's Disease, vol. 16, no. 4, pp. 763–774, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  81. A. Hadding, B. Kaltschmidt, and C. Kaltschmidt, “Overexpression of receptor of advanced glycation end products hypersensitizes cells for amyloid beta peptide-induced cell death,” Biochimica et Biophysica Acta, vol. 1691, no. 1, pp. 67–72, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  82. A. Y. Hsia, E. Masliah, and E. Masliah, “Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 6, pp. 3228–3233, 1999. View at Publisher · View at Google Scholar · View at Scopus
  83. O. Arancio, H. P. Zhang, and H. P. Zhang, “RAGE potentiates Aβ-induced perturbation of neuronal function in transgenic mice,” The EMBO Journal, vol. 23, no. 20, pp. 4096–4105, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  84. I. Vodopivec, A. Galichet, M. Knobloch, A. Bierhaus, C. W. Heizmann, and R. M. Nitsch, “RAGE does not affect amyloid pathology in transgenic arcAβ mice,” Neurodegenerative Diseases, vol. 6, no. 5-6, pp. 270–280, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  85. M. Knobloch, M. Farinelli, U. Konietzko, R. M. Nitsch, and I. M. Mansuy, “Aβ oligomer-mediated long-term potentiation impairment involves protein phosphatase 1-dependent mechanisms,” Journal of Neuroscience, vol. 27, no. 29, pp. 7648–7653, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  86. R. Dearie, A. Sagare, and B. V. Zlokovic, “The role of the cell surface LRP and soluble LRP in blood-brain barrier Aβ clearance in Alzheimer's disease,” Current Pharmaceutical Design, vol. 14, no. 16, pp. 1601–1605, 2008. View at Publisher · View at Google Scholar · View at Scopus
  87. B. W. Moore, “A soluble protein characteristic of the nervous system,” Biochemical and Biophysical Research Communications, vol. 19, no. 6, pp. 739–744, 1965. View at Google Scholar · View at Scopus
  88. K. Bell, D. Shokrian, C. Potenzieri, and P. M. Whitaker-Azmitia, “Harm avoidance, anxiety, and response to novelty in the adolescent S-100β transgenic mouse: role of serotonin and relevance to down syndrome,” Neuropsychopharmacology, vol. 28, no. 10, pp. 1810–1816, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  89. H. Nishiyama, M. Takemura, T. Takeda, and S. Itohara, “Normal development of serotonergic neurons in mice lacking S100B,” Neuroscience Letters, vol. 321, no. 1-2, pp. 49–52, 2002. View at Publisher · View at Google Scholar · View at Scopus
  90. R. H. Dyck, I. I. Bogoch, A. Marks, N. R. Melvin, and G. C. Teskey, “Enhanced epileptogenesis in S100B knockout mice,” Molecular Brain Research, vol. 106, no. 1-2, pp. 22–29, 2002. View at Publisher · View at Google Scholar · View at Scopus
  91. M. C. Schaub and C. W. Heizmann, “Calcium, troponin, calmodulin, S100 proteins: from myocardial basics to new therapeutic strategies,” Biochemical and Biophysical Research Communications, vol. 369, no. 1, pp. 247–264, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  92. I. Marenholz, C. W. Heizmann, and G. Fritz, “S100 proteins in mouse and man: from evolution to function and pathology (including an update of the nomenclature),” Biochemical and Biophysical Research Communications, vol. 322, no. 4, pp. 1111–1122, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  93. J. Krebs and C. W. Heizmann, “Calcium-binding proteins and the EF-hand principle,” in Calcium: A Matter of Life or Death, J. Krebs and M. Michalak, Eds., pp. 51–93, Elsevier, Amsterdam, The Netherlands, 2007. View at Google Scholar
  94. J. L. Gifford, M. P. Walsh, and H. J. Vogel, “Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs,” Biochemical Journal, vol. 405, no. 2, pp. 199–221, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  95. J. Baudier, N. Glasser, and D. Gerard, “Ions binding to S100 proteins. I. Calcium- and zinc-binding properties of bovine brain S100 alpha alpha, S100a (alpha beta), and S100b (beta beta) protein: Zn2+ regulates Ca2+ binding on S100b protein,” The Journal of Biological Chemistry, vol. 261, no. 18, pp. 8192–8203, 1986. View at Google Scholar · View at Scopus
  96. G. Fritz and C. W. Heizmann, “3D structures of the calcium and zinc binding S100 proteins,” in Handbook of Metalloproteins, A. Messerschmidt, W. Bode, and M. Cygler, Eds., vol. 3, pp. 529–540, John Wiley & Sons, Chichester, UK, 2004. View at Google Scholar
  97. S. Z. Senior, L. L. Mans, H. D. VanGuilder, K. A. Kelly, M. P. Hendrich, and T. E. Elgren, “Catecholase activity associated with copper-S100B,” Biochemistry, vol. 42, no. 15, pp. 4392–4397, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  98. C. W. Heizmann, G. Fritz, and B. W. Schäfer, “S100 proteins: structure, functions and pathology,” Frontiers in Bioscience, vol. 7, pp. d1356–d1368, 2002. View at Google Scholar · View at Scopus
  99. T. Nishikawa, I. S. M. Lee, N. Shiraishi, T. Ishikawa, Y. Ohta, and M. Nishikimi, “Identification of S100b protein as copper-binding protein and its suppression of copper-induced cell damage,” The Journal of Biological Chemistry, vol. 272, no. 37, pp. 23037–23041, 1997. View at Publisher · View at Google Scholar · View at Scopus
  100. R. Donato, G. Sorci, and G. Sorci, “S100B's double life: intracellular regulator and extracellular signal,” Biochimica et Biophysica Acta, vol. 1793, no. 6, pp. 1008–1022, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  101. L. Santamaria-Kisiel, A. C. Rintala-Dempsey, and G. S. Shaw, “Calcium-dependent and -independent interactions of the S100 protein family,” Biochemical Journal, vol. 396, no. 2, pp. 201–214, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  102. O. V. Moroz, G. G. Dodson, K. S. Wilson, E. Lukanidin, and I. B. Bronstein, “Multiple structural states of S100A12: a key to its functional diversity,” Microscopy Research and Technique, vol. 60, no. 6, pp. 581–592, 2003. View at Google Scholar · View at Scopus
  103. N. Leukert, T. Vogl, K. Strupat, R. Reichelt, C. Sorg, and J. Roth, “Calcium-dependent tetramer formation of S100A8 and S100A9 is essential for biological activity,” Journal of Molecular Biology, vol. 359, no. 4, pp. 961–972, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  104. K. Kizawa, H. Takahara, H. Troxler, P. Kleinert, U. Mochida, and C. W. Heizmann, “Specific citrullination causes assembly of a globular S100A3 homotetramer: a putative Ca2+ modulator matures human hair cuticle,” The Journal of Biological Chemistry, vol. 283, no. 8, pp. 5004–5013, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  105. D. Foell, H. Wittkowski, T. Vogl, and J. Roth, “S100 proteins expressed in phagocytes: a novel group of damage-associated molecular pattern molecules,” Journal of Leukocyte Biology, vol. 81, no. 1, pp. 28–37, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  106. D. B. Zimmer and L. J. Van Eldik, “Analysis of the calcium-modulated proteins, S100 and calmodulin, and their target proteins during C6 glioma cell differentiation,” Journal of Cell Biology, vol. 108, no. 1, pp. 141–151, 1989. View at Google Scholar · View at Scopus
  107. G. E. Davey, P. Murmann, and C. W. Heizmann, “Intracellular Ca2+ and Zn2+ levels regulate the alternative cell density-dependent secretion of S100B in human glioblastoma cells,” The Journal of Biological Chemistry, vol. 276, no. 33, pp. 30819–30826, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  108. M. Rothermundt, M. Peters, J. H. Prehn, and V. Arolt, “S100B in brain damage and neurodegeneration,” Microscopy Research and Technique, vol. 60, no. 6, pp. 614–632, 2003. View at Google Scholar · View at Scopus
  109. M. Rothermundt, G. Ponath, and V. Arolt, “S100B in schizophrenic psychosis,” International Review of Neurobiology, vol. 59, pp. 445–470, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  110. A. Hauschild, G. Engel, W. Brenner, R. Gläser, H. Mönig, E. Henze, and E. Christophers, “S100B protein detection in serum is a significant prognostic factor in metastatic melanoma,” Oncology, vol. 56, no. 4, pp. 338–344, 1999. View at Publisher · View at Google Scholar · View at Scopus
  111. S. Torabian and M. Kashani-Sabet, “Biomarkers for melanoma,” Current Opinion in Oncology, vol. 17, no. 2, pp. 167–171, 2005. View at Publisher · View at Google Scholar · View at Scopus
  112. L. J. Van Eldik and D. B. Zimmer, “Secretion of S-100 from rat C6 glioma cells,” Brain Research, vol. 436, no. 2, pp. 367–370, 1987. View at Google Scholar · View at Scopus
  113. R. Gerlach, G. Demel, and G. Demel, “Active secretion of S100B from astrocytes during metabolic stress,” Neuroscience, vol. 141, no. 4, pp. 1697–1701, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  114. R. Ciccarelli, P. Di Iorio, and P. Di Iorio, “Activation of A1 adenosine or mGlu3 metabotropic glutamate receptors enhances the release of nerve growth factor and S-100beta protein from cultured astrocytes,” Glia, vol. 27, no. 3, pp. 275–281, 1999. View at Google Scholar · View at Scopus
  115. P. M. Whitaker-Azmitia, R. Murphy, and E. C. Azmitia, “Stimulation of astroglial 5-HT1A receptors releases the serotonergic growth factor, protein S-100, and alters astroglial morphology,” Brain Research, vol. 528, no. 1, pp. 155–158, 1990. View at Google Scholar
  116. M. M. Edwards and S. R. Robinson, “TNF alpha affects the expression of GFAP and S100B: implications for Alzheimer's disease,” Journal of Neural Transmission, vol. 113, no. 11, pp. 1709–1715, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  117. D. F. de Souza, M. C. Leite, and M. C. Leite, “S100B secretion is stimulated by IL-1β in glial cultures and hippocampal slices of rats: likely involvement of MAPK pathway,” Journal of Neuroimmunology, vol. 206, no. 1-2, pp. 52–57, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  118. L. A. Peña, C. W. Brecher, and D. R. Marshak, “β-amyloid regulates gene expression of glial trophic substance S100β in C6 glioma and primary astrocyte cultures,” Molecular Brain Research, vol. 34, no. 1, pp. 118–126, 1995. View at Publisher · View at Google Scholar · View at Scopus
  119. T. Iuvone, G. Esposito, and G. Esposito, “Cannabinoid CB1 receptor stimulation affords neuroprotection in MPTP-induced neurotoxicity by attenuating S100B up-regulation in vitro,” Journal of Molecular Medicine, vol. 85, no. 12, pp. 1379–1392, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  120. S. S. Pinto, C. Gottfried, and C. Gottfried, “Immunocontent and secretion of S100B in astrocyte cultures from different brain regions in relation to morphology,” FEBS Letters, vol. 486, no. 3, pp. 203–207, 2000. View at Publisher · View at Google Scholar · View at Scopus
  121. L. M. de Almeida, C. C. Piñeiro, and C. C. Piñeiro, “Resveratrol increases glutamate uptake, glutathione content, and S100B secretion in cortical astrocyte cultures,” Cellular and Molecular Neurobiology, vol. 27, no. 5, pp. 661–668, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  122. R. T. Abib, A. Quincozes-Santos, P. Nardin, S. T. Wofchuk, M. L. Perry, C.-A. Gonçalves, and C. Gottfried, “Epicatechin gallate increases glutamate uptake and S100B secretion in C6 cell lineage,” Molecular and Cellular Biochemistry, vol. 310, no. 1-2, pp. 153–158, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  123. D. Kligman and D. R. Marshak, “Purification and characterization of a neurite extension factor from bovine brain,” Proceedings of the National Academy of Sciences of the United States of America, vol. 82, no. 20, pp. 7136–7139, 1985. View at Google Scholar · View at Scopus
  124. R. H. Selinfreund, S. W. Barger, W. J. Pledger, and L. J. Van Eldik, “Neurotrophic protein S100β stimulates glial cell proliferation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 88, no. 9, pp. 3554–3558, 1991. View at Google Scholar · View at Scopus
  125. F. Tramontina, S. Conte, and S. Conte, “Developmental changes in S100B content in brain tissue, cerebrospinal fluid, and astrocyte cultures of rats,” Cellular and Molecular Neurobiology, vol. 22, no. 3, pp. 373–378, 2002. View at Publisher · View at Google Scholar · View at Scopus
  126. H. J. Huttunen, J. Kuja-Panula, G. Sorci, A. L. Agneletti, R. Donato, and H. Rauvala, “Coregulation of neurite outgrowth and cell survival by amphoterin and S100 proteins through receptor for advanced glycation end products (RAGE) activation,” The Journal of Biological Chemistry, vol. 275, no. 51, pp. 40096–40105, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  127. D. Kögel, M. Peters, and M. Peters, “S100B potently activates p65/c-Rel transcriptional complexes in hippocampal neurons: clinical implications for the role of S100B in excitotoxic brain injury,” Neuroscience, vol. 127, no. 4, pp. 913–920, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  128. C. Reali, F. Scintu, R. Pillai, R. Donato, F. Michetti, and V. Sogos, “S100B counteracts effects of the neurotoxicant trimethyltin on astrocytes and microglia,” Journal of Neuroscience Research, vol. 81, no. 5, pp. 677–686, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  129. R. Businaro, S. Leone, C. Fabrizi, G. Sorci, R. Donato, G. M. Lauro, and L. Fumagalli, “S100B protects LAN-5 neuroblastoma cells against Aβ amyloid-induced neurotoxicity via RAGE engagement at low doses but increases Aβ amyloid neurotoxicity at high doses,” Journal of Neuroscience Research, vol. 83, no. 5, pp. 897–906, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  130. G. Ponath, C. Schettler, F. Kaestner, B. Voigt, D. Wentker, V. Arolt, and M. Rothermundt, “Autocrine S100B effects on astrocytes are mediated via RAGE,” Journal of Neuroimmunology, vol. 184, no. 1-2, pp. 214–222, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  131. L. Feng, C. Matsumoto, A. Schwartz, A. M. Schmidt, D. M. Stern, and J. Pile-Spellman, “Chronic vascular inflammation in patients with type 2 diabetes: endothelial biopsy and RT-PCR analysis,” Diabetes Care, vol. 28, no. 2, pp. 379–384, 2005. View at Publisher · View at Google Scholar · View at Scopus
  132. S. Man, E. E. Ubogu, and R. M. Ransohoff, “Inflammatory cell migration into the central nervous system: a few new twists on an old tale,” Brain Pathology, vol. 17, no. 2, pp. 243–250, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  133. D. R. Marshak, S. A. Pesce, L. C. Stanley, and W. S. T. Griffin, “Increased S100β neurotrophic activity in Alzheimer's disease temporal lobe,” Neurobiology of Aging, vol. 13, no. 1, pp. 1–7, 1992. View at Publisher · View at Google Scholar · View at Scopus
  134. E. R. Peskind, W. S. T. Griffin, K. T. Akama, M. A. Raskind, and L. J. Van Eldik, “Cerebrospinal fluid S100B is elevated in the earlier stages of Alzheimer's disease,” Neurochemistry International, vol. 39, no. 5-6, pp. 409–413, 2001. View at Publisher · View at Google Scholar · View at Scopus
  135. M. L. Chaves, A. L. Camozzato, and A. L. Camozzato, “Serum levels of S100B and NSE proteins in Alzheimer's disease patients,” Journal of Neuroinflammation, vol. 7, article 6, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  136. W. S. T. Griffin, J. G. Sheng, and J. G. Sheng, “Life-long overexpression of S100β in Down's syndrome: implications for Alzheimer pathogenesis,” Neurobiology of Aging, vol. 19, no. 5, pp. 401–405, 1998. View at Publisher · View at Google Scholar · View at Scopus
  137. A. Petzold, R. Jenkins, and R. Jenkins, “Cerebrospinal fluid S100B correlates with brain atrophy in Alzheimer's disease,” Neuroscience Letters, vol. 336, no. 3, pp. 167–170, 2003. View at Publisher · View at Google Scholar · View at Scopus
  138. J. M. Craft, D. M. Watterson, A. Marks, and L. J. Van Eldik, “Enhanced susceptibility of S-100B transgenic mice to neuroinflammation and neuronal dysfunction induced by intracerebroventricular infusion of human β-amyloid,” Glia, vol. 51, no. 3, pp. 209–216, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  139. T. Mori, N. Koyama, G. W. Arendash, Y. Horikoshi-Sakuraba, J. Tan, and T. Town, “Overexpression of human S100B exacerbates cerebral amyloidosis and gliosis in the Tg2576 mouse model of Alzheimer's disease,” Glia, vol. 58, no. 3, pp. 300–314, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  140. J. Baudier and R. D. Cole, “Interactions between the microtubule-associated tau proteins and S100B regulate tau phosphorylation by the Ca2+/calmodulin-dependent protein kinase II,” The Journal of Biological Chemistry, vol. 263, no. 12, pp. 5876–5883, 1988. View at Google Scholar · View at Scopus
  141. G. Esposito, C. Scuderi, and C. Scuderi, “S100B induces tau protein hyperphosphorylation via Dickopff-1 up-regulation and disrupts the Wnt pathway in human neural stem cells,” Journal of Cellular and Molecular Medicine, vol. 12, no. 3, pp. 914–927, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  142. S. Mruthinti, A. Sood, C. L. Humphrey, S. Swamy-Mruthinti, and J. J. Buccafusco, “The induction of surface β-amyloid binding proteins and enhanced cytotoxicity in cultured PC-12 and IMR-32 cells by advanced glycation end products,” Neuroscience, vol. 142, no. 2, pp. 463–473, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  143. J. Gasic-Milenkovic, S. Dukic-Stefanovic, W. Deuther-Conrad, U. Gärtner, and G. Münch, “β-amyloid peptide potentiates inflammatory responses induced by lipopolysaccharide, interferon -gamma and 'advanced glycation endproducts' in a murine microglia cell line,” European Journal of Neuroscience, vol. 17, no. 4, pp. 813–821, 2003. View at Google Scholar · View at Scopus
  144. L. Perrone, G. Peluso, and M. A. B. Melone, “RAGE recycles at the plasma membrane in S100B secretory vesicles and promotes Schwann cells morphological changes,” Journal of Cellular Physiology, vol. 217, no. 1, pp. 60–71, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  145. H.-L. Hsieh, B. W. Schäfer, B. Weigle, and C. W. Heizmann, “S100 protein translocation in response to extracellular S100 is mediated by receptor for advanced glycation endproducts in human endothelial cells,” Biochemical and Biophysical Research Communications, vol. 316, no. 3, pp. 949–959, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  146. J. H. Boyd, B. Kan, H. Roberts, Y. Wang, and K. R. Walley, “S100A8 and S100A9 mediate endotoxin-induced cardiomyocyte dysfunction via the receptor for advanced glycation end products,” Circulation Research, vol. 102, no. 10, pp. 1239–1246, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  147. S. Ghavami, I. Rashedi, and I. Rashedi, “S100A8/A9 at low concentration promotes tumor cell growth via RAGE ligation and MAP kinase-dependent pathway,” Journal of Leukocyte Biology, vol. 83, no. 6, pp. 1484–1492, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  148. A. M. Schmidt, S. D. Yan, S. F. Yan, and D. M. Stern, “The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses,” Journal of Clinical Investigation, vol. 108, no. 7, pp. 949–955, 2001. View at Publisher · View at Google Scholar · View at Scopus
  149. P. Westermark, M. D. Benson, and M. D. Benson, “A primer of amyloid nomenclature,” Amyloid, vol. 14, no. 3, pp. 179–183, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  150. M. M. Sousa, S. D. Yan, R. Fernandas, A. Guimarães, D. Stern, and M. J. Saraiva, “Familial amyloid polyneuropathy: receptor for advanced glycation end products-dependent triggering of neuronal inflammatory and apoptotic pathways,” Journal of Neuroscience, vol. 21, no. 19, pp. 7576–7586, 2001. View at Google Scholar · View at Scopus
  151. A. L. Schwarzman, M. Tsiper, H. Wente, A. Wang, M. P. Vitek, V. Vasiliev, and D. Goldgaber, “Amyloidogenic and anti-amyloidogenic properties of recombinant transthyretin variants,” Amyloid, vol. 11, no. 1, pp. 1–9, 2004. View at Publisher · View at Google Scholar · View at Scopus
  152. C. D. Link, “Expression of human β-amyloid peptide in transgenic Caenorhabditis elegans,” Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 20, pp. 9368–9372, 1995. View at Publisher · View at Google Scholar · View at Scopus
  153. T. D. Stein, N. J. Anders, C. DeCarli, S. L. Chan, M. P. Mattson, and J. A. Johnson, “Neutralization of transthyretin reverses the neuroprotective effects of secreted amyloid precursor protein (APP) inAPPSw mice resulting in tau phosphorylation and loss of hippocampal neurons: support for the amyloid hypothesis,” Journal of Neuroscience, vol. 24, no. 35, pp. 7707–7717, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  154. P. Ehlermann, K. Eggers, and K. Eggers, “Increased proinflammatory endothelial response to S100A8/A9 after preactivation through advanced glycation end products,” Cardiovascular Diabetology, vol. 5, pp. 6–15, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  155. N. A. Calcutt, M. E. Cooper, T. S. Kern, and A. M. Schmidt, “Therapies for hyperglycaemia-induced diabetic complications: from animal models to clinical trials,” Nature Reviews Drug Discovery, vol. 8, no. 5, pp. 417–429, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  156. B. V. Zlokovic, “New therapeutic targets in the neurovascular pathway in Alzheimer's disease,” Neurotherapeutics, vol. 5, no. 3, pp. 409–414, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus