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Articles by Takeshi Iwatsubo
Total Records ( 3 ) for Takeshi Iwatsubo
  Takeshi Iwatsubo
  Japanese Alzheimer’s Disease Neuroimaging Initiative (J-ADNI) was launched in 2008, aiming at conducting a longitudinal workup of a standardized neuroimaging, biomarker and clinico-psychological surveys. The research protocol was designed to maximize compatibility with that of US-ADNI, including structural magnetic resonance imaging analysis for the evaluation of brain atrophy, fluorodeoxyglucose and amyloid positron emission tomography, cerebrospinal fluid sampling, APOE genotyping, together with a set of clinical and psychometric tests that were prepared to achieve the highest compatibility to those used in the United States. Japanese ADNI has recruited ~357 participants (142 amnestic mild cognitive impairment, ~134 normal aged and 72 mild Alzheimer’s disease (AD), as of April 15, 2010). World-wide ADNI activities will establish the rigorous quantitative descriptions of the natural course of AD in its very early stages. The data, as well as the methodologies and infrastructures, will facilitate the clinical trials of disease-modifying therapies for AD using surrogate biomarkers.
  Reisa A. Sperling , Paul S. Aisen , Laurel A. Beckett , Laurel A. Beckett , Suzanne Craft , Anne M. Fagan , Takeshi Iwatsubo , Clifford R. Jack , Jeffrey Kaye , Thomas J. Montine , Denise C. Park , Eric M. Reiman , Christopher C. Rowe , Eric Siemers , Yaakov Stern , Yaakov Stern , Maria C. Carrillo , Bill Thies , Marcelle Morrison- Bogorad , Molly V. Wagster and Creighton H. Phelps
  The National Institute on Aging and the Alzheimer‘s Association charged a workgroup with the task of developing criteria for the symptomatic predementia phase of Alzheimer‘s disease (AD), referred to in this article as mild cognitive impairment due to AD. The workgroup developed the following two sets of criteria: (1) core clinical criteria that could be used by healthcare providers without access to advanced imaging techniques or cerebrospinal fluid analysis, and (2) research criteria that could be used in clinical research settings, including clinical trials. The second set of criteria incorporate the use of biomarkers based on imaging and cerebrospinal fluid measures. The final set of criteria for mild cognitive impairment due to AD has four levels of certainty, depending on the presence and nature of the biomarker findings. Considerable work is needed to validate the criteria that use biomarkers and to standardize biomarker analysis for use in community settings.
  Kaoru Yamada , Tadafumi Hashimoto , Chiori Yabuki , Yusuke Nagae , Masanori Tachikawa , Dudley K. Strickland , Qiang Liu , Guojun Bu , Jacob M. Basak , David M. Holtzman , Sumio Ohtsuki , Tetsuya Terasaki and Takeshi Iwatsubo
  The metabolism of amyloid β peptide (Aβ) in the brain is crucial to the pathogenesis of Alzheimer disease. A body of evidence suggests that Aβ is actively transported from brain parenchyma to blood across the blood-brain barrier (BBB), although the precise mechanism remains unclear. To unravel the cellular and molecular mechanism of Aβ transport across the BBB, we established a new in vitro model of the initial internalization step of Aβ transport using TR-BBB cells, a conditionally immortalized endothelial cell line from rat brain. We show that TR-BBB cells rapidly internalize Aβ through a receptor-mediated mechanism. We also provide evidence that Aβ internalization is mediated by LRP1 (low density lipoprotein receptor-related protein 1), since administration of LRP1 antagonist, receptor-associated protein, neutralizing antibody, or small interference RNAs all reduced Aβ uptake. Despite the requirement of LRP1-dependent internalization, Aβ does not directly bind to LRP1 in an in vitro binding assay. Unlike TR-BBB cells, mouse embryonic fibroblasts endogenously expressing functional LRP1 and exhibiting the authentic LRP1-mediated endocytosis (e.g. of tissue plasminogen activator) did not show rapid Aβ uptake. Based on these data, we propose that the rapid LRP1-dependent internalization of Aβ occurs under the BBB-specific cellular context and that TR-BBB is a useful tool for analyzing the molecular mechanism of the rapid transport of Aβ across BBB.
 
 
 
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