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Alzheimer’s Disease: Methods and Protocols

11th December 2006

Alzheimer’s Disease: Methods and Protocols

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A panel of highly skilled investigators describe in detail their state-of-the-art biochemical, cell biological, and molecular biological techniques for studying the molecular basis of Alzheimer’s disease. These readily reproducible, step-by-step methods focus on work with the amyloid precursor protein and the amyloidogenic peptide A?, but also include-with the recent identification of presenilin proteins-techniques for determining the structure and biological function of these proteins. In addition, there are chapters covering the tau protein and its role in Alzheimer’s disease, as well as an introductory discussion of the history of the disease, its genetic basis, and the currently available and possible future therapeutic agents. Cutting-edge and wide ranging, Alzheimer’s Disease: Methods and Protocols provides ready access to proven, reproducible methods for elucidating the molecular basis of this most common senile dementia. Ed. Hooper, Nigel

Table of Contents

    1. Introduction to Alzheimer???s Disease (pp. 1-22)
      Allsop, David
    2. The Genetics of Alzheimer???s Disease (pp. 23-44)
      Brindle, Nick; St. George-Hyslop, Peter
    3. Advances in Methodology and Current Prospects for Primary Drug Therapies for Alzheimer???s Disease (pp. 45-62)
      Knopman, David S.
    4. Production and Functional Assays of Recombinant Secreted Amyloid Precursor Protein (APP) (sAPPa) (pp. 63-78)
      Barger, Steven W.
    5. Quantifying A?В1-40 and A?В1-42 Using Sandwich-ELISA (pp. 79-90)
      Skovronsky, Daniel M.; Wang, Jun; Lee, Virginia M.-Y.; Doms, Robert W.
    6. Electrophoretic Separation and Immunoblotting of A?В1-40 and A?В1-42 (pp. 91-100)
      Staufenbiel, Matthias; Paganetti, Paolo A.
    7. A?В-Induced Proinflammatory Cytokine Release from Differentiated Human THP-1 Monocytes (pp. 101-112)
      Brunden, Kurt R.; Kocsis-Angle, June; Embury, Paula; Yates, Stephen L.
    8. Effects of the ?В-Amyloid Peptide on Membrane Ion Permeability (pp. 113-138)
      Pearson, Hugh A.
    9. Analysis of ?В-Amyloid Peptide Degradation In Vitro (pp. 139-148)
      Cordell, Barbara; Naidu, Asha
    10. Posttranslational Modifications of Amyloid Precursor Protein: Ectodomain Phosphorylation and Sulfation (pp. 149-168)
      Walter, Jochen; Haass, Christian
    11. Posttranslational Modifications of the Amyloid Precursor Protein: Glycosylation (pp. 169-190)
      Liu, Chen; Rozmyslowicz, Tomasz; Stwora-Wojczyk, Magda; Wojczyk, Boguslaw; Spitalnik, Steven L.
    12. Using an Amyloid Precursor Protein (APP) Reporter to Characterize a-Secretase (pp. 191-202)
      Roberts, Susan Boseman
    13. Inhibition of a-Secretase by Zinc Metalloproteinase Inhibitors (pp. 203-216)
      Parvathy, S.; Turner, Anthony J.; Hooper, Nigel M.
    14. Development of Neoepitope Antibodies Against the ?В-Secretase Cleavage Site in the Amyloid Precursor Protein (pp. 217-228)
      Gray, Carol W.; Karran, Eric H.
    15. ?В-Secretase: Tissue Culture Studies of Sequence Specificity, Inhibitors, and Candidate Enzymes (pp. 229-238)
      Citron, Martin
    16. Using y-Secretase Inhibitors to Distinguish the Generation of the A?В Peptides Terminating at Val-40 and Ala-42 (pp. 239-248)
      Paganetti, Paolo A.; Staufenbiel, Matthias
    17. Designing Animal Models of Alzheimer???s Disease with Amyloid Precursor Protein (APP) Transgenes (pp. 249-270)
      Loring, Jeanne F.
    18. Phosphorylation of Amyloid Precursor Protein (APP) Family Proteins (pp. 271-282)
      Suzuki, Toshiharu; Ando, Kanae; Iijima, Ko-ichi; Oguchi, Shinobu; Takeda, Shizu
    19. Determining the Transmembrane Topology of the Presenilins (pp. 283-296)
      Thinakaran, Gopal; Doan, Andrew
    20. Normal Proteolytic Processing of the Presenilins (pp. 297-308)
      Hartmann, Henrike; Yankner, Bruce A.
    21. Apoptotic Proteolytic Cleavage of the Presenilins by Caspases (pp. 309-316)
      Kim, Tae-Wan
    22. The Phosphorylation of Presenilin Proteins (pp. 317-332)
      Walter, Jochen
    23. Interaction of the Presenilins with the Amyloid Precursor Protein (APP) (pp. 333-344)
      Weidemann, Andreas; Paliga, Krzysztof; Durrwang, Ulrike; Reinhard, Friedrich; Zhang, Dai; Sandbrink, Rupert; Evin, Genevieve; Masters, Colin L.; Beyreuther, Konrad
    24. Distribution of Presenilins and Amyloid Precursor Protein (APP) in Detergent-Insoluble Membrane Domains (pp. 345-360)
      Parkin, Edward T.; Turner, Anthony J.; Hooper, Nigel M.
    25. Characterization and Use of Monoclonal Antibodies to Tau and Paired Helical Filament Tau (pp. 361-374)
      Davies, Peter
    26. Tau Phosphorylation Both In Vitro and in Cells (pp. 375-394)
      Reynolds, C. Hugh; Gibb, Graham M.; Lovestone, Simon
    27. Transglutaminase-Catalyzed Formation of Alzheimer-Like Insoluble Complexes from Recombinant Tau (pp. 395-404)
      Balin, Brian J.; Appelt, Denah M.

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