About this Journal Submit a Manuscript Table of Contents
Journal of Biomedicine and Biotechnology
Volume 2012 (2012), Article ID 728178, 8 pages
http://dx.doi.org/10.1155/2012/728178
Research Article

Proteomic Characterization of a Mouse Model of Familial Danish Dementia

1Dipartimento di Biochimica e Biotecnologie Mediche, Università degli Studi di Napoli Federico II, 80131 Napoli, Italy
2CEINGE Biotecnologie Avanzate, 80145 Napoli, Italy
3Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, 80147 Napoli, Italy
4Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10462, USA

Received 30 December 2011; Accepted 2 February 2012

Academic Editor: Monica Fedele

Copyright © 2012 Monica Vitale 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. G. T. Plant, T. Revesz, R. O. Barnard, A. E. Harding, and P. C. Gautier-Smith, “Familial cerebral amyloid angiopathy with nonneuritic amyloid plaque formation,” Brain, vol. 113, no. 3, pp. 721–747, 1990. View at Scopus
  2. R. Vidal, T. Révész, A. Rostagno et al., “A decamer duplication in the 3′ region of the BRI gene originates an amyloid peptide that is associated with dementia in a Danish kindred,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 9, pp. 4920–4925, 2000. View at Scopus
  3. J. L. Holton, T. Lashley, J. Ghiso et al., “Familial Danish dementia: a novel form of cerebral amyloidosis associated with deposition of both amyloid-Dan and amyloid-Beta,” Journal of Neuropathology and Experimental Neurology, vol. 61, no. 3, pp. 254–267, 2002. View at Scopus
  4. R. Vidal, B. Franglone, A. Rostagno et al., “A stop-codon mutation in the BRI gene associated with familial British dementia,” Nature, vol. 399, no. 6738, pp. 776–781, 1999. View at Publisher · View at Google Scholar
  5. J. Ghiso, A. Rostagno, Y. Tomidokoro et al., “Genetic alterations of the BRI2 gene: familial British and Danish dementias,” Brain Pathology, vol. 16, no. 1, pp. 71–79, 2006. View at Publisher · View at Google Scholar · View at Scopus
  6. J. L. Holton, J. Ghiso, T. Lashley et al., “Regional distribution of amyloid-Bri deposition and its association with neurofibrillary degeneration in familial British dementia,” American Journal of Pathology, vol. 158, no. 2, pp. 515–526, 2001. View at Scopus
  7. A. Rostagno, T. Revesz, T. Lashley et al., “Complement activation in chromosome 13 dementias: similarities with Alzheimer's disease,” The Journal of Biological Chemistry, vol. 277, no. 51, pp. 49782–49790, 2002. View at Publisher · View at Google Scholar · View at Scopus
  8. M. Tsachaki, J. Ghiso, and S. Efthimiopoulos, “BRI2 as a central protein involved in neurodegeneration,” Biotechnology Journal, vol. 3, no. 12, pp. 1548–1554, 2008. View at Publisher · View at Google Scholar · View at Scopus
  9. S. Matsuda, L. Giliberto, Y. Matsuda et al., “The familial dementia BRI2 gene binds the alzheimer gene amyloid-β precursor protein and inhibits amyloid-β production,” The Journal of Biological Chemistry, vol. 280, no. 32, pp. 28912–28916, 2005. View at Publisher · View at Google Scholar · View at Scopus
  10. S. Matsuda, L. Giliberto, Y. Matsuda, E. M. McGowan, and L. D'Adamio, “BRI2 inhibits amyloid β-peptide precursor protein processing by interfering with the docking of secretases to the substrate,” Journal of Neuroscience, vol. 28, no. 35, pp. 8668–8676, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. S. Matsuda, Y. Matsuda, E. L. Snapp, and L. D'Adamio, “Maturation of BRI2 generates a specific inhibitor that reduces APP processing at the plasma membrane and in endocytic vesicles,” Neurobiology of Aging, vol. 32, no. 8, pp. 1400–1408, 2011. View at Publisher · View at Google Scholar · View at Scopus
  12. A. Fotinopoulou, M. Tsachaki, M. Vlavaki et al., “BRI2 interacts with amyloid precursor protein (APP) and regulates amyloid β(Aβ) production,” The Journal of Biological Chemistry, vol. 280, no. 35, pp. 30768–30772, 2005. View at Publisher · View at Google Scholar · View at Scopus
  13. S. Matsuda, R. Tamayev, and L. D'Adamio, “Increased AβPP processing in familial danish dementia patients,” Journal of Alzheimer's Disease, vol. 27, no. 2, pp. 385–391, 2011. View at Publisher · View at Google Scholar
  14. H. J. Garringer, J. Murrell, L. D'Adamio, B. Ghetti, and R. Vidal, “Modeling familial British and Danish dementia,” Brain Structure and Function, vol. 214, no. 2-3, pp. 235–244, 2010. View at Publisher · View at Google Scholar · View at Scopus
  15. F. Pickford, J. Coomaraswamy, M. Jucker, and E. McGowan, “Modeling familial British dementia in transgenic mice,” Brain Pathology (Zurich, Switzerland), vol. 16, no. 1, pp. 80–85, 2006. View at Publisher · View at Google Scholar · View at Scopus
  16. R. Vidal, A. G. Barbeito, L. Miravalle, and B. Ghetti, “Cerebral amyloid angiopathy and parenchymal amyloid deposition in transgenic mice expressing the Danish mutant form of human BRI2,” Brain Pathology (Zurich, Switzerland), vol. 19, no. 1, pp. 58–68, 2009. View at Publisher · View at Google Scholar · View at Scopus
  17. J. Coomaraswamy, E. Kilger, H. Wölfing et al., “Modeling familial Danish dementia in mice supports the concept of the amyloid hypothesis of Alzheimer's disease,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 17, pp. 7969–7974, 2010. View at Publisher · View at Google Scholar · View at Scopus
  18. L. Giliberto, S. Matsuda, R. Vidal, and L. D'Adamio, “Generation and initial characterization of FDD knock in mice,” PLoS ONE, vol. 4, no. 11, Article ID e7900, 2009. View at Publisher · View at Google Scholar · View at Scopus
  19. R. Tamayev, S. Matsuda, M. Fà, O. Arancio, and L. D'Adamio, “Danish dementia mice suggest that loss of function and not the amyloid cascade causes synaptic plasticity and memory deficits,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 48, pp. 20822–20827, 2010. View at Publisher · View at Google Scholar · View at Scopus
  20. R. Tamayev, L. Giliberto, W. Li et al., “Memory deficits due to familial British dementia BRI2 mutation are caused by loss of BRI2 function rather than amyloidosis,” Journal of Neuroscience, vol. 30, no. 44, pp. 14915–14924, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. F. Talamo, C. D'Ambrosio, S. Arena et al., “Proteins from bovine tissues and biological fluids: defining a reference electrophoresis map for liver, kidney, muscle, plasma and red blood cells,” Proteomics, vol. 3, no. 4, pp. 440–460, 2003. View at Publisher · View at Google Scholar · View at Scopus
  22. G. S. Scippa, M. Rocco, M. Ialicicco et al., “The proteome of lentil (Lens culinaris Medik.) seeds: discriminating between landraces,” Electrophoresis, vol. 31, no. 3, pp. 497–506, 2010. View at Publisher · View at Google Scholar · View at Scopus
  23. W. J. Qian, T. Liu, M. E. Monroe et al., “Probability-based evaluation of peptide and protein identifications from tandem mass spectrometry and SEQUEST analysis: the human proteome,” Journal of Proteome Research, vol. 4, no. 1, pp. 53–62, 2005. View at Publisher · View at Google Scholar · View at Scopus
  24. D. Szklarczyk, A. Franceschini, M. Kuhn et al., “The STRING database in 2011: functional interaction networks of proteins, globally integrated and scored,” Nucleic Acids Research, vol. 39, supplement 1, pp. D561–D568, 2011. View at Publisher · View at Google Scholar
  25. D. W. Huang, B. T. Sherman, and R. A. Lempicki, “Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources,” Nature Protocols, vol. 4, no. 1, pp. 44–57, 2009. View at Publisher · View at Google Scholar · View at Scopus
  26. D. W. Huang, B. T. Sherman, and R. A. Lempicki, “Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists,” Nucleic Acids Research, vol. 37, no. 1, pp. 1–13, 2009. View at Publisher · View at Google Scholar · View at Scopus
  27. H. Husi, M. A. Ward, J. S. Choudhary, W. P. Blackstock, and S. G. N. Grant, “Proteomic analysis of NMDA receptor-adhesion protein signaling complexes,” Nature Neuroscience, vol. 3, no. 7, pp. 661–669, 2000. View at Publisher · View at Google Scholar · View at Scopus
  28. M. O. Collins, H. Husi, L. Yu et al., “Molecular characterization and comparison of the components and multiprotein complexes in the postsynaptic proteome,” Journal of Neurochemistry, vol. 97, supplement 1, pp. 16–23, 2006. View at Publisher · View at Google Scholar · View at Scopus
  29. E. Fernández, M. O. Collins, R. T. Uren et al., “Targeted tandem affinity purification of PSD-95 recovers core postsynaptic complexes and schizophrenia susceptibility proteins,” Molecular Systems Biology, vol. 5, article 269, 2009. View at Publisher · View at Google Scholar · View at Scopus
  30. E. Kim and M. Sheng, “PDZ domain proteins of synapses,” Nature Reviews Neuroscience, vol. 5, no. 10, pp. 771–781, 2004. View at Publisher · View at Google Scholar · View at Scopus
  31. A. Alexa, J. Varga, and A. Reményi, “Scaffolds are “active” regulators of signaling modules,” FEBS Journal, vol. 277, no. 21, pp. 4376–4382, 2010. View at Publisher · View at Google Scholar
  32. N. Guerreiro, M. Staufenbiel, and B. Gomez-Mancilla, “Proteomic 2-D DIGE profiling of APP23 transgenic mice brain from pre-plaque and plaque phenotypes,” Journal of Alzheimer's Disease, vol. 13, no. 1, pp. 17–30, 2008. View at Scopus
  33. V. Anggono, K. J. Smillie, M. E. Graham, V. A. Valova, M. A. Cousin, and P. J. Robinson, “Syndapin I is the phosphorylation-regulated dynamin I partner in synaptic vesicle endocytosis,” Nature Neuroscience, vol. 9, no. 6, pp. 752–760, 2006. View at Publisher · View at Google Scholar · View at Scopus
  34. K. I. Patterson, T. Brummer, P. M. O'Brien, and R. J. Daly, “Dual-specificity phosphatases: critical regulators with diverse cellular targets,” Biochemical Journal, vol. 418, no. 3, pp. 475–489, 2009. View at Publisher · View at Google Scholar · View at Scopus
  35. J. D. Sweatt, “Mitogen-activated protein kinases in synaptic plasticity and memory,” Current Opinion in Neurobiology, vol. 14, no. 3, pp. 311–317, 2004. View at Publisher · View at Google Scholar · View at Scopus