Glypican-1 as an Aß binding HSPG in the human brain: its localization in DIG domains and possible roles in the pathogenesis of Alzheimer’s disease 1 NORIFUMI WATANABE 2 , WATARU ARAKI * , DE-HUA CHUI † , TAKAO MAKIFUCHI ‡ , YASUO IHARA § and TAKESHI TABIRA National Institute for Longevity Sciences, Morioka, Obu, Aichi; * Department of Demyelinating Disease and Aging, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Kodaira, Tokyo; † Laboratory for Alzheimer’s Disease, RIKEN Brain Science Institute, Wako-shi, Saitama; ‡ Department of Clinical Research, National Saigata Hospital, Ogata, Nakakubiki, Niigata; and § Department of Neuropathology, Faculty of Medicine, University of Tokyo, Bunkyo-ku, Tokyo, Japan 2 Correspondence: National Institute for Longevity Sciences, 36-3 Gengo, Morioka, Obu, Aichi 474-8522, Japan. E-mail: watanabn@nils.go.jp <h3>SPECIFIC AIMS</h3> The amyloid deposition whose major component is the 39-43 amino acid peptide, termed ß-amyloid protein (Aß), is considered to be important in Alzheimer’s disease (AD) pathology, but the precise mechanism of its accumulation in AD brain is unclear. Although there are studies of the association between Aß and heparan sulfate proteoglycans (HSPGs), they demonstrated colocalization in plaques or binding ability of HSPGs derived from tissues other than human brain. It
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