アルツハイマー病、他の認知症、老化 Alzheimer's Disease, Other Dementia, Aging
P2-2-192 アミロイド関連うつ病：老年期うつ病に対する[18F]Florbetapirによるアミロイドイメージング Amyloid associated depression: amyloid imaging with [18F]florbetapir in geriatric depression ○舘野周1, 坂寄健1, 樋口真人2, 須原哲也2, 佐藤英尊3, 石原圭一3, 汲田伸一郎3 ○Amane Tateno1, Takeshi Sakayori1, Makoto Higuchi2, Tetsuya Suhara2, Hidetaka Sato3, Keiichi Ishihara3, Shin-ichiro Kumita3 日本医科大学精神医学教室1, 放射線医学総合研究所分子イメージング研究センター2, 日本医科大学放射線医学3 Dept Neuropsychiatry, Nippon Medical School, Tokyo, Japan1, Molecular Imaging Center, National Institute of Radiological Sciences2, Dept Radiology, Nippon Meidcal School3 Purpose The association between Alzheimer's disease (AD) and depression is a complicated issue. A history of major depressive episode is known to be one of the high risks for AD, and depressive episode has been frequently observed among patients with AD. In this study we investigated the association between patients with a history of major depression and the accumulation of β-amyloid by amyloid positron emission tomography (PET). Method Twenty-three geriatric subjects (4 patients with AD, 2 patients with other type of dementia, 16 patients with mild cognitive impairment (MCI), and 1 healthy volunteer) participated. They were evaluated by Mini-Mental-State Exam and Alzheimer's Disease Assessment Scale-cognitive-component-Japanese version) for cognitive function, and Geriatric Depression Scale (GDS) for severity of depression. The amount of β-amyloid deposit was evaluated by [18F]florbetapir PET for standard uptake value ratios (SUVRs) and the cut-off SUVRs value of 1.099 for positive β-amyloid. Results Nine of the subjects (39.1%) were estimated as β-amyloid-positive. There were no significant differences between the β-amyloid-positive and β-amyloid-negative groups in terms of average age (77.9±4.2 versus 75.6±3.7), MMSE (22.3±5.8 versus 23.5±3.8), ADAS-Jcog (13.8±8.6 versus 12.8±8.2), and GDS (6.3±4.7 versus 7.9±3.9). The average age at onset of depression was significantly higher in the β-amyloid-positive group than the β-amyloid-negative group (73.0±7.7 versus 58.6±16.4, p=0.024). Discussion Our results showed that accumulation of β-amyloid was associated with geriatric depression. These results might indicate that a part of geriatric depression represented prodromal symptoms of AD, since β-amyloid pathology started 10-20 years before the onset of AD. Future study should determine whether the regional accumulation of β-amyloid is associated with geriatric depression as a prodromal symptom of AD.	P2-2-193 老化促進モデルマウスにおける記憶障害および酸化ストレスに対するノビレチンの改善効果 Beneficial effects of nobiletin on cognitive impairment and oxidative stress in SAMP8 mice ○中島晶1, 青山雄紀1山田亮之介1, 中井剛1, 永井拓1, 横須賀章人3, 三巻祥浩3, 大泉康4,5,6, 山田清文1 ○Akira Nakajima1, Yuki Aoyama1, Thuy-Ty Lan Nguyen2, Eun-Joo Shin2, Hyoung-Chun Kim2, Shinnosuke Yamada1, Tsuyoshi Nakai1, Taku Nagai1, Akihito Yokosuka3, Yoshihiro Mimaki3, Yasushi Ohizumi4,5,6, Kiyofumi Yamada11 名古屋大院・医・医療薬学・病院薬剤1, 江原大学・薬2, 東京薬大・薬3, 静岡県立大院・薬4, 横浜薬科大・薬5, 東北大院・工6 Dept. Neuropsychopharmacology and Hospital Pharmacy, Nagoya Univ. Grad. Sch. Med.1, College of Pharmacy, Kangwon National University, Korea2, Sch Pharm, Tokyo Univ of Pharmacy and Life Science3, Grad Sch Pharm Sci, Univ of Shizuoka4, Yokohama College of Pharmacy5, Graduate School of Engineering, Tohoku University6 Our recent studies have demonstrated that nobiletin, a citrus flavonoid, ameliorates learning and memory impairment in olfactory-bulbectomized mice, amyloid precursor protein transgenic mice, and NMDA receptor antagonist-treated mice. Here we present the evidence that this natural compound improves age-related cognitive impairment and reduces oxidative stress in the senescence-accelerated mouse prone 8 (SAMP8). Treatment with nobiletin (10 or 50 mg/kg) reversed the impairment of recognition memory and context-dependent fear memory in SAMP8 mice. Furthermore, nobiletin restored the decrease in the GSH/GSSG ratio in the brain of SAMP8 mice. In addition, increases in glutathione peroxidase and manganese-superoxide dismutase activities, as well as a decrease in protein carbonyl level, were observed in the brain of nobiletin-treated SAMP8 mice. These findings suggest that nobiletin improves cognitive impairment and reduces the brain oxidative stress in SAMP8 mice. Together, the markedly beneficial effects of nobiletin represent a potentially useful treatment for ameliorating the learning and memory deficits and oxidative stress in aging as well as age-related neurodegenerative diseases such as Alzheimer's disease.
P2-2-194 Withdrawn	P2-2-195 小胞体ストレスがタウオパチーに及ぼす影響 Involvement of endoplasmic reticulum stress in tauopathy ○阪上由香子1, 工藤喬1, 谷向仁1, 金山大祐1, 近江翼1, 大河内正康1, 今泉和則2, 武田雅俊1 ○Yukako Sakagami1, Takashi Kudo1, Hitoshi Tanimukai1, Daisuke Kanayama1, Tsubasa Omi1, Masayasu Okochi1, Kazunori Imaizumi2, Masatoshi Takeda1 大阪大院・医・精神医学1, 広島大院・医歯薬・分子細胞2 Dept Psy, Osaka Univ, Osaka1, Dept Biochem, Hiroshima Univ, Hiroshima2 Tauopathy is a pathological condition with an abnormal intracellular accumulation of tau protein in neurons and glias, which is a feature of Alzheimer's disease (AD) as well as frontotemporal lobar degenerations (FTLD). Recent reports showed that tauopathy occupies an important position for pathological process of dementia generally. Previously, we reported that endoplasmic reticulum (ER) stress has an influence on the onset of AD. In addition, some reports on brain autopsy findings suggest that ER stress is associated with AD and tauopathy. However, the mechanism underlying the association between ER stress and tauopathy is still unknown. Here, we show that ER stress, induced by glucose deprivation or chemicals, increases total endogenous tau protein in cultured neurons and primary cultured neurons. Under ER stress, no significant differences were observed in the transcription of tau, and no differences were observed in the translation of tau with or without the 5'-untranslated region (5'UTR) of tau. In contrast, the degradation rate of tau was decreased by 20% under ER stress. ER stress reduced the binding between tau and carboxyl terminus of Hsc70-interacting protein (CHIP), ubiquitin E3 ligase for tau. These results suggest that ER stress increases total tau protein and its mechanism is due to the decrease in the binding between tau and CHIP, which delays the degradation of tau protein through the ubiquitin-proteasome pathway. This mechanism may provide clue to treatment for tauopathy.
P2-2-196 Auraptenはγセクレターゼを活動化させることによりアミロイドβの生産を増加させる Aurapten increases the production of beta amyloid by increasing γ-secretase activity ○鄭且均1,2, 堀家裕史2三角吉代1, 飛田秀樹1, 道川誠3 ○Cha-Gyun Jung1,2, Hirofumi Horike2, Kyung-Ok Uhm2, Sachiyo Misumi1, Hideki Hida1, Makoto Michikawa3 名市大・医・脳神経生理学1, 国立長寿医療研究センター・アルツハイマー病研究部2, 名市大・医・病態生化学3 Dept. Neurophysiol and Brain Sci, Nagoya City Univ. Nagoya, Japan1, Dept. of Alzheimer's Disease Research, NCGG, Obu, Japan2, Dept. Biochemistry, Nagoya City Univ. Nagoya, Japan3 Beta-amyloid (Aβ) is a major pathogenic peptide for Alzheimer's disease (AD) and is generated via proteolytic processing of amyloid precursor protein (APP) by β- and γ-secretases. Aβ production is regulated by alternate cleavage of APP by the Α- and γ-secretases. In this study, we carried out that the effect of 118 natural compounds on Aβ production in the medium of HEK293T cells stably expressing human APP695 (HEK293T-APP) using Aβ40 and Aβ42 sandwich ELISAs. We found that auraptene, a coumarin derivative of citrus fruit, increased Aβ40 and Aβ42 production in a dose-dependent manner in HEK293T-APP cells and rat primary neurons without cell death. Auraptene did not alter the protein levels of APP, soluble APP, ADAM10 (Α-secreatse), BACE1 (β-secreatse) and PS1 (γ-secretase component), but it decreased APP C-terminal fragment-α (CTFα) in these cells. We also found that auraptene increased the level of intracellular domain of Notch (NICD) which is one of the substrates for g-secretase. We also carried out an in vitro γ-secretase activity assay using membrane fractions of primary neurons and found auraptene increase the γ-secretase activity. These results suggest that auraptene increases AΒ40 and AΒ42 production by increasing γ-secretase activity.	P2-2-197 CSF中APL1β28を用いてヒト脳内でのAβ42産生を推測する CSF APL1β28 is a possible surrogate marker for Aβ42 production in human brains ○水田直樹1, 大河内正康1, 田上真次1, 柳田寛太1, 児玉高志1, 田中稔久1, 森原剛史1, 工藤喬1, 武田雅俊1 ○Naoki Mizuta1, Masayasu Okochi1, Shinji Tagami1, Kanta Yanagida1, Takashi Kodama1, Toshihisa Tanaka1, Takashi Morihara1, Takashi Kudo1, Masatoshi Takeda1 大阪大学大学院医学系研究科精神医学教室1 Osaka University Graduate School of Medicine, Osaka1 Alzheimer's disease (AD) is the most common cause of dementia in the elderly. To date, therapeutic intervention after the disease onset has not been successful because irreversible and progressive neuronal death precedes clinical symptoms. Importantly, most of next generation anti-AD drugs inhibit progress of the pathological process and, thus, establishment of highly probable prediction of future AD onset is inseparable. To predict AD onset, it is necessary to detect how much Aβ is accumulating in the brain. Our recent discovery of APL1β28, a novel and highly sensitive biomarker for Aβ42 production in the human brain, may help in the development of early detection methods for AD. It is interesting that the ratio of APL1β28 to total APL1β is significantly increased not only in familial AD but also in sporadic AD cases. Our recent technical progress made us to need only one microL of CSF for its very precise measurement by using LC/MS/MS.
P2-2-198 APLP2はPresenilin1 FAD mutantによってβAPPやAPLP1と異なる切断を受ける Effects of presenilin1 mutants on APLP2 cleavage are different from those of βAPP and APLP1 ○柳田寛太1, 大河内正康1, 田上真次1, 児玉高志1, 水田直樹1, 田中稔久1, 森原剛史1, 工藤喬1, 武田雅俊1 ○Kanta Yanagida1, Masayasu Okochi1, Shinji Tagami1, Takashi Kodama1, Naoki Mizuta1, Toshihisa Tanaka1, Takashi Morihara1, Takashi Kudo1, Masatoshi Takeda1 大阪大学大学院・医学系研究科・内科系臨床医学専攻・情報統合医学講座・精神医学分野1 Psychiatry, Department of Integrated Medicine, Division of Internal Medicine, Osaka University Graduate School of Medicine1 Alzheimer disease (AD) amyloidβ (Aβ) peptide was generated from βAPP by β- and γ-secretases. APLP1 and APLP2 are homologue of βAPP. Previously, we identified Aβ-like peptides derived from APLP1 (ie, APL1Β) in human cerebrospinal fluid (CSF). We also reported that C-terminally elongated APL1β28, a surrogate marker for Aβ42, increased in CSF of AD patients. Here, we tried to detect APLP2-derived Aβ-like peptide from human CSF, and identified three species of peptides (APL2β35, ALP2β38 and APL2β39). APLP2 was shedded by only β-secretase in the brain, however, APLP2 overexpressed in cultured cells, was mainly cleaved by α-secretase. Interestingly, different from Aβ and APL1β, the levels of C-terminally elongated forms of APL2β (ALP2β38 and APL2β39) did not increase by presenilin1 familial AD mutants. Instead, we found that the relative ratios of C-terminally truncated APL2β species increased. We suggest that effects of presenilin1 mutants on APLP2 cleavage are different from those of βAPP and APLP1.	P2-2-199 タウオパチー神経変性疾患における異常リン酸化Tauの解析 Analysis of Tau phosphorylation in Tauopathy neurodegeneration using Phos-tag SDS-PAGE ○木村妙子1, 福島寛美1, 細川智永1, 初田裕幸2, 鈴掛雅美3, 斎藤太郎1, 秋山治彦3, 村山繁雄3, 長谷川成人2, 久永眞市1 ○Taeko Kimura1, Hiromi Fukushima1, Tomohisa Hosokawa1, Hiroyuki Hatsuta2, Masami Masuda-Suzukake3, Taro Saito1, Haruhiko Akiyama3, Shigeo Murayama3, Masato Hasegawa2, Shin-ichi Hisanaga1 首都大学東京　理工学研究科　生命科学専攻1, 東京都健康長寿医療センター研究所2, 東京都医学総合研究所3 Dept. of Biol. Sci., Tokyo Metro. Univ., Tokyo, Japan1, Tokyo Metropolitan Institute of Gerontology, Tokyo, Japan2, Department of Neuropathology and Cell Biology, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan3 A neuronal microtubule-associated protein, Tau is a major component of neurofillary tangle (NFTs), pathology in Alzheimer's disease (AD). Tau is also a causative gene of FTDP-17 neurodegenerative disease. NFT Tau and FTDP-17 mutant Tau are hyper-phosphorylated in disease brains. However, it is not known yet how Tau is hyper-phosphorylated and how hyper-phosphorylated Tau contributes development of disease. We thought there might be intermediate phosphorylation states, which reflect the early stage of diseases. Tau has many phosphorylation sites targeted by many protein kinases including GSK3 or Cdk5. Previous studies have mainly employed phosphor-specific antibodies to detect abnormal phosphorylation. It was useful but required many phosphor-specific antibodies. Here, we applied Phos-tag SDS-PAGE in analysis of tau phosphorylation. Phosphorylated proteins are delayed extraordinally in Phos-tag SDS-PAGE. We observed site-specific mobility shift of Tau phosphorylated by Cdk5 in vitro and in COS-7 cells. Tau was phosphorylated by Cdk5 mainly at Ser202, Ser235 and Ser404 in vitro, and specifically Ser235 and Ser404 in C0S-7 cells by coexpression with Cdk5-p35. Further, we detected slight difference in phosphorylation between Tau 3R and Tau 4R, that was not reported previously. R406W FTDP-17 mutant Tau was phosphorylated differently from other Tau mutants such as P301L. FTDP-17 mutant Tau transgenic mouse showed upward shift when Tau aggregates were formed. We are going to analyze phosphorylation of Tau in AD. We would like to evaluate Phos-tag SDS-PAGE as a method for analysis of hyper-phosphorylation of AD or FTDP-17 Tau.
P2-2-200 Calsyntenin-3 C-末端断片の蓄積は神経原線維変化ではなくAβ-アミロイドと関連する Calsyntenin-3 C-terminal fragment accumulates in dystrophic neurites surrounding Aβ plaques but not in neuropil threads in Alzheimer's disease brains ○内田洋子1, 五味不二也1 ○Yoko Uchida1, Fujiya Gomi1 東京都健康長寿医療センター研究所　老化脳神経科学チーム1 RT for Aging Neuroscience, Tokyo Metropolitan Institute of Gerontology1 Aβ may play an important role in early pathogenesis of Alzheimer's disease (AD), but molecular mechanisms of Aβ actions, which are responsible for neurotoxicity, are not fully understood. We have previously identified a synaptic membrane protein calsyntenin-3 (Cst-3) as an Aβ-induced molecule. Cst-3 undergoes two-step proteolytical processing like APP. The primary cleavage with α-secretase generates a long N-terminal ectodomain (sCst-3) and a short intracellular C-terminal fragment (CTF) containing the transmembrane region. CTF is subsequently cleaved into a short peptide p3 and an intracellular domain (ICD) by γ-secretase. In vitro transfection experiments with Cst-3 fragments revealed that only CTF is neurotoxic. In this study, we investigated whether full-length or CTF of Cst-3 accumulate in dystrophic neurites surrounding Aβ plaques in Tg2576 mouse and AD brains, and whether Cst-3 also accumulates in tau-positive neuropil threads in AD brain. Double immunolabeling with anti-Aβ and anti-cytoplasmic Cst-3, or anti-Cst-3 ectodomain and anti-Aβ antibodies revealed the accumulation of CTF but not full-length of Cst-3 in dystrophic neurites surrounding Aβ plaques in Tg2576 mice. In AD brain, Cst-3-CTF was accumulated in dystrophic neurites surrounding Aβ plaques but not in phosphorylated-tau (AT8)-positive neuropil threads, suggesting no association with Cst-3-CTF and tau accumulation. Taken together with neurotoxic CTF, Aβ may disrupt neuronal processes surrounding Aβ plaques via the accumulation of Cst-3-CTF under the suppression of γ-secretase.	P2-2-201 アミロイドβ蛋白質の細胞内動態を生体内で解析する新規モデル動物の開発 Development of new animal models of Alzheimer's diseases visualizing the intracellular dynamics of the amyloid β protein ○落石知世1, 戸井基道1, 志村秀樹2, 卜部貴夫2, 服部信孝3, 海老原達彦1 ○Tomoyo Ochiishi1, Motomichi Doi1, Hideki Shimura2, Takao Urabe2, Nobutaka Hattori3, Tatsuhiko Ebihara1 独立行政法人産業技術総合研究所バイオメディカル研究部門1, 順天堂大学医学部附属浦安病院脳神経内科2, 順天堂大学医学部脳神経内科3 Biomedical Res Inst, Natl Inst of Advanced Industrial Sci and Technol (AIST), Ibaraki, Japan1, Dept of Neurol, Juntendo Univ Urayasu Hospital, Chiba, Japan2, Dept of Neurol, Juntendo Univ Sch of Med, Tokyo, Japan3 The pathology of Alzheimer's disease (AD) is characterized by the extracellular accumulation of amyroid-β (Aβ) peptide and the intraneuronal aggregation of hyperphosphorylated tau protein. In the "β-Amyloid Hypothesis", the extracellular deposit of Aβ peptide plays the central role in the pathogenesis of AD. However, recent studies have suggested that the intraneuronal Aβ peptide is more toxic than extracellular form of it. There are many examples of AD model transgenic animals and most of them overexpress the amyloid precursor protein (APP). Because APP is cleaved into several physiologically active protein fragments including Aβ peptide in vivo, they are not rigorous models corresponding to the amyloidosis. Alternatively, direct observation of the process of deposition and disaggregation of Aβ peptide in vivo is quite important for the evaluation of candidate molecules in drug discovery research. With the aim of drug screening by analyzing the intracellular dynamics of Aβ peptide and toxicity in vivo, we have developed the new animal models of AD, an Aβ-GFP mouse and Aβ-GFP C. elegans, which express an Aβ1-42 peptide fused with GFP in neuronal cells. Observation of Aβ dynamics as GFP fused protein is not easy because the aggregation of Aβ inhibits the fluorescence of fused GFP. However, we succeeded to visualize the Aβ dynamics by arranging the linker sequence between Aβ and GFP. Using a fusion protein with long linker, the intracellular Aβ1-42 was clearly observed as a various sized aggregates in the cultured neurons from Aβ-GFP mouse and also in the adult brain tissues. Using a fusion protein with the short linker, we could monitor the status of Aβ dynamic in Aβ-GFP C. elegans in vivo. Now we are analyzing the age-dependent characteristic changes of neurons expressing intracellular Aβ.
P2-2-202 LC/MSとELISAによる脳脊髄液(CSF)中でのAPl1βペプチドの定量 Determination of APL1βPeptide Concentration in Cerebrospinal Fluid (CSF) by ELISA ○児玉高志1, 大河内正康1, 田上真次1, 柳田寛太1, 水田直樹1, 田中稔久1, 森原剛史1, 工藤喬1, 武田雅俊1 ○Takashi Kodama1, Masayasu Okochi1, Shinji Tagami1, Kanta Yanagida1, Naoki Mizuta1, Toshihisa Tanaka1, Takashi Morihara1, Takashi Kudo1, Masatoshi Takeda1 大阪大院・医・精神医学1 Dept Psychiatry, Osaka Univ, Osaka1 Amyloid-beta (Aβ) peptide, especially Aβ42, deposition into insoluble plaques is a pathological hallmark of Alzheimer disease. Therefore, Aβ42 peptide has been thought to be a candidate biomarker for AD. However, Aβ42 peptide shows high aggregability and its use as a biomarker for Aβ generation mechanism is probably limited. Using liquid chromatography-mass spectrometry (LC/MS/MS). we recently identified three Aβ-like peptides (APL1β-25, 27, 28) that are soluble and brain-derived peptides produced through the same type of sequential intramembrane endoproteolysis of an APP family protein APLP1. The ratio of APL1β28 to total APL1β is significantly increased both in familial AD and sporadic AD cases. To measure the levels of the APL1β peptides in more conventional method, we tried to develop ELISA systems which can specifically detect each peptide species. In this study, we compared the two different methods and investigated whether the ELISA system can be used instead of LC/MS/MS system. The study was performed with Osaka University Hospital ethics committee approval (No. 07139, 07212).	P2-2-203 Puromycin-sensitive aminopeptidase のタウ蛋白分解への関与について Involvement of Puromycin-sensitive aminopeptidase in degradation process of tau by N-terminal modification ○田中稔久1, 丸山大輔1, 佐藤真広1, 寺田美幸1, 武田雅俊1 ○Toshihisa Tanaka1, Daisuke Maruyama1, Masahiro Sato1, Miyuki Terada1, Masatoshi Takeda1 大阪大学大学院　医学系研究科　精神医学1 Dept Psychiatry, Osaka Univ Grad Sch Med, Osaka1 The microtubule associated protein tau is a major component of neurofibrillary tangles in brains suffering from tauopathies including Alzheimer disease, frontotemporal dementia, and FTDP-17 (frontotemporal dementia and parkinsonism linked to chromosome 17). In tauopathies, tau protein is accumulated in brains, however mechanisms of the accumulation are still unclear. Previously we showed that among several proteases, puromycin-sensitive aminopeptidase (PSA) was found as a predominant regulator of degradation of tau protein. However whether PSA degrades tau protein directly or not, is controversial. PSA is known as amino-terminal peptidase, therefore the following experiments were designed to clarify the activity of PSA on tau degradation. PAC-22, a specific inhibitor of PSA, was added in culture medium of SH-SY5Y human neuroblastoma cells, and amounts of tau in the cells were monitored by Western blot. After addition of PAC-22 in the culture medium, increased amounts of tau in the cells were observed. Next an site-specific antibody against N-terminl tau was raised, and degradation process of tau by PSA in vitro, was monitored by Western blot employing the site-specific antibody and a general anti-tau antibody. After incubation of tau with PSA in vitro, the imunoreactivity of the site-specific antibody against N-terminal tau was decreased, however the imunoreactivity of the general anti-tau antibody was not altered. These results suggest that PSA is involved in tau metabolism in cells, and that it degrades only N-terminal of tau, not total tau. Probably PSA regulates degradation of tau not by direct complete digestion, but by unknown indirect mechanism., and N-terminal cleaved tau might be prone to be degraded by some unidentified proteases in cells.
P2-2-204 神経科学ブレインバンクネットワーク2012年次報告 Annual Report of Japanese Brain Bank Network for Neuroscience Research ○小幡真希1, 村山繁雄2, 齊藤祐子3, 高尾昌樹4, 赤津博康5 ○Maki Obata1, Shigeo Murayama2, Yuko Saito3, Masaki Takao4, Hiroyasu Akatsu5 東京都健康長寿医療センター高齢者バイオリソースセンター1, 東京都健康長寿医療センター高齢者ブレインバンク2, 国立精神・神経医療研究センター病院臨床検査部3, 美原記念病院ブレインバンク4, 福祉村病院ブレインバンク5 Bioresource Center for Aging Research, Tokyo Metropolitan Geriatric Hospital & Institute of Gerontology1, Department of Neuropathology, Tokyo Metropolitan Geriatric Hospital & Institute of Gerontology2, Department of Pathology and Laboratory Medicine, National Center for Neurology and Psychiatry, Kodaira, Tokyo, Japan3, Mihara Memorial Hospital Brain Bank, Isezaki, Gunma, Japan4, Fukushimura Brain Bank, Toyohashi, Aichi, Japan5 Brain Bank was established in 1960's in United States and Europe as a basic infrastructure for human neuroscience research. In Japan, institutional collections represented major repository of postmortem brains as in Brain Research Institute, Niigata University. Brain bank movement officially started in 2001 as the Brain Bank for Aging Research (BBAR) in Tokyo Metropolitan Geriatric Hospital and Institute of Gerontology (TMGHIG). Simultaneously, Research Resource Network and Brain Bank with patients'living will started in National Center for Neurology and Psychiatry (NCNP). A brain bank for psychiatric disorders also started in Fukushima University. Japanese Society of Neuropathology (JSNP) appreciated establishement of Japanese brain bank network as one of its major goals and the Brain Bank Committee workd as a task force. In 2010, Japanese Brain Bank Network for Neuroscience Research (JBBNNR) was funded by Comprehensive Brain Science Network from the Ministry of Education, Culture, Sports, Science and Technology of Japan. BBAR is also taking position of the pathology core of JADNI (Japanese Alzheimer Disease Neuroimage Initiative) and National Surveylance, Creutzfeldt Jakob disease and resumed affiliation with National Center for Geriatric and Gerontology. The standard of JBBNNR was as follows: 1. brain bank was approved by IRB with consensus of cinical and pathological branches in the institute; 2. brain bank accepted brain donors with living will and clinically follow the brain donors; 3. brain bank resource was quality controlled and its information was transmitted to researcher. JBBNNR included NCNP bank, Mihara Memorial Hopsital Brain Bank, Fukushimura Brain Bank and NCNP brain bank. We are trying to select and provide best human tissues for researchers to study human postmortem brain.

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