Two types of α-synuclein accumulated abnormal terminals in the α-synuclein transgenic mice (original) (raw)

Abstract

s S245 affected by this molecule. Resveratrol reduced lipid peroxide in serum, lipid droplets in hepatocytes, and activated phagocytosis of Kupffer cells. In the CNS, resveratrol reduced the appearance of lipofuscin granules, a marker for the aging, enhanced expressions of synaptophysin, superoxide dismutase, Bcl-2 and Bcl-xL connected with activation of neuronal function, and decreased neurofilament proteins, GFAP and Bax involved in aging/neurodegeneration. Together, resveratrol may function as beneficial to the CNS and protecting neurons from aging or degeneration. doi:10.1016/j.neures.2009.09.1385 P3-l10 Rhizoma (Senkyu), one of various components of Yokukansan reduced the ER stress induced cell toxicity resulting in the good effect on the Alzheimer disease associated cell death Toru Hiratsuka1, Shinsuke Matsuzaki2, Shingo Miyata1, Taiichi Katayama2, Masaya Tohyama1,2 1 Dept. Anat&Neurosci, University of Osaka, Osaka, Japan; 2 United Grad. Sch. of Child Develop, Osaka Univ., Kanazawa University, Hamamatsu Univ. Sch. of Med., Osaka, Japan Yokukansan has been administrated to the persons who show such symptoms as nervousness etc. Yokukansan is focused as the one of the possible therapies for Alzheimer’s disease (AD). ER stress plays an important role in the pathogenesis of AD. Thus, we examined the effect of yokukansan on the ER stress induced neurotoxicity and the familial AD-linked PS1 mutation ( E9) associated cell death to investigate the effects of yokukansan on the AD linked cell death. As results, we elucidated that yokukansan should upregulate the expression of GRP78 and reduce the expression of CHOP resulting in the reduction of ER stress induced cell death and the AD-linked associated cell death. These results suggest that yokukansan and Rhizoma should be potential medicine to the AD and our findings cast new light on the development of therapy for the AD. doi:10.1016/j.neures.2009.09.1386 P3-l11 Aged Alzheimer mice bear the increased expression of diazepam binding inhibitor in activated glial cells Kota Kimura, Mayu Shimatani, Jun Kaneko, Kaori Taniguchi, Ken Aizawa, Tatsuhiro Hisatsune Dept. Integrated., The University of Tokyo, Tokyo, Japan In Alzheimer disease, the change in glial functions has become a current attention in terms of both pathogenesis and therapeutic applications. In a related study, we also report the increased proliferation of astroglial cells at the dentate gyrus of hippocampal formation in the transgenic mice B6C3-Tg(APPswe,PSEN1dE9)85Dbo/J as a model for Alzheimer disease. In this study, we evaluated the expression of diazepam biding inhibitor (DBI) in the activated astroglial cells. A recent report showed that the over-expression of DBI caused the cognitive decline as assessed by hippocampal dependent behavior task and the deficit in LTP function of hippocampal circuit (Siiskonen et al., 2007). Very interestingly, we observed the increased expression of DBI in astroglial cells at the hilar region of Alzheimer transgenic mice, but not in those of control wild-type littermate, after 12 months of ages. Our results may suggest that the functional changes in hippocampal glial cells would be involved in the cognitive deficit in Alzheimer disease. doi:10.1016/j.neures.2009.09.1387 P3-l12 Identification of protein targets for 15-deoxy12,14prostaglandin J2 in neuronal plasma membranes Tatsurou Yagami, Kenkichi Takase, Yasuhiro Yamamoto Dept. Physiol., Facult. Pharmath. Sci., Himeji Dokkyo Univ., Himeji, Japan Deposits of amyloid protein (A ) are generally assumed to contribute to progressive neurodegeneration in the Alzheimer’s disease (AD). In primary cultures of cortical neurons, A significantly generated prostaglandin D2 (PGD2) before cell death. Although PGD2 induced neuronal cell death, specific binding sites of [H]PGD2 were not detected in plasma membranes. Without enzymes, PGD2 was metabolized to 15-deoxy12,14-prostaglandin J2 (15d-PGJ2). 15d-PGJ2 was more neurotoxic than PGD2. The specific binding sites of [3H]15d-PGJ2 were abundant in plasma membranes. A proteomic approach was used to identify protein targets for 15d-PGJ2 in neuronal plasma membranes. By using biotinylated 15d-PGJ2, 21 proteins were identified as biotin-positive targets. They were classified into cytoskeltal proteins, glycolytic enzymes and molecular chaperones. Some of these targets have been reported to interact with A and associate with AD. doi:10.1016/j.neures.2009.09.1388 P3-l13 Molecular mechanisms to form insoluble complex in a mouse model of multiple system atrophy (MSA) Kimiko Nakayama, Yasuyo Suzuki, Ikuru Yazawa Laboratory of Research Resources, National Center for Geriatrics and Geron-