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Related Publications White JA, Manelli AM, Holmberg KH, and MJ LaDu. Differential effects of oligomeric and fibrillar amyloid-β1-42 on glial-mediated inflammation. In press, Neurobiol Dis., 2005.
Manelli, A.M., Stine Jr., W.B., Van Eldik, L.J., and M.J. Ladu. ApoE and Aβ1-42 interactions: effects of isoform and conformation on structure and function. J Mol Neurosci. 23:235-246, Review, 2004.
Stine WB Jr, Dahlgren KN, Krafft GA, and MJ LaDu. In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis. J Biol Chem. 28;278(13):11612-22, 2003.
Dahlgren KN, Manelli AM, Stine WB Jr, Baker LK, Krafft GA, and MJ LaDu. Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability. J Biol Chem. 30;277(35):32046-53, 2002.
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Structure and Function of Aβ1-42 Assemblies Although Aβ peptide causes AD, the correlation between amyloid plaques and dementia is poor, in terms of timing, localization, and amount (Figure 1). Therefore, small soluble oligomers have been hypothesized to be the proximate cause of the neuronal loss associated with AD. We determined the conditions necessary to produce stable homogeneous preparations of several distinct conformational species of Aβ1-42, including oligomers and fibrils (Figure 2). Analysis of Oligomeric and Fibrillar Aβ1-42 by Atomic Force Microscopy (AFM)  [Stine, JBC, 2003] Figure 1. Amyloid-β Conformations: Distinct Assembly Pathways  Figure 2. In vitro, Aβ is neurotoxic and induces glial-mediated inflammation. Oligomeric forms of Aβ1-42 are more neurotoxic (Figure 3) and pro-inflammatory (Figure 4) than fibrillar forms. AFM Images of Amyloid-β1-42 Assembly Pathways  [Stine, JBC, 2003] Figure 3. Stereotaxic Injection of Aβ1-42 into Rat Hippocampus
 [Maxwell, J. Mol. Neurosci., 2004] Figure 4. em>In Vitro Glial Inflammatory Factors Induced by Aβ1-42:
 [White, NBD, 2005] Figure 5. LTP in ApoE3-TR Mice + Aβ-42  [Trommer, NBD, 2005] Figure 6. Related Publications White JA, Manelli AM, Holmberg KH, and MJ LaDu. Differential effects of oligomeric and fibrillar amyloid-β1-42 on glial-mediated inflammation. In press, Neurobiol Dis., 2005.
Manelli, A.M., Stine Jr., W.B., Van Eldik, L.J., and M.J. Ladu. ApoE and Aβ1-42 interactions: effects of isoform and conformation on structure and function. J Mol Neurosci. 23:235-246, Review, 2004.
Stine WB Jr, Dahlgren KN, Krafft GA, and MJ LaDu. In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis. J Biol Chem. 28;278(13):11612-22, 2003.
Dahlgren KN, Manelli AM, Stine WB Jr, Baker LK, Krafft GA, and MJ LaDu. Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability. J Biol Chem. 30;277(35):32046-53, 2002.
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