naa a22 4500 510745903 CHVBK 20180411083046.0 cr unu---uuuuu 180411e20131101xx s 000 0 eng 10.1007/s12192-013-0428-9 doi (NATIONALLICENCE)springer-10.1007/s12192-013-0428-9 Overexpression of Hsp27 ameliorates symptoms of Alzheimer's disease in APP/PS1 mice [Elektronische Daten] [Melinda Tóth, Viktor Szegedi, Edina Varga, Gábor Juhász, János Horváth, Emőke Borbély, Balázs Csibrány, Róbert Alföldi, Nikolett Lénárt, Botond Penke, Miklós Sántha] Hsp27 belongs to the small heat shock protein family, which are ATP-independent chaperones. The most important function of Hsp27 is based on its ability to bind non-native proteins and inhibit the aggregation of incorrectly folded proteins maintaining them in a refolding-competent state. Additionally, it has anti-apoptotic and antioxidant activities. To study the effect of Hsp27 on memory and synaptic functions, amyloid-β (Aβ) accumulation, and neurodegeneration, we generated transgenic mice overexpressing human Hsp27 protein and crossed with APPswe/PS1dE9 mouse strain, a mouse model of Alzheimer's disease (AD). Using different behavioral tests, we found that spatial learning was impaired in AD model mice and was rescued by Hsp27 overexpression. Electrophysiological recordings have revealed that excitability of neurons was significantly increased, and long-term potentiation (LTP) was impaired in AD model mice, whereas they were normalized in Hsp27 overexpressing AD model mice. Using anti-amyloid antibody, we counted significantly less amyloid plaques in the brain of APPswe/PS1dE9/Hsp27 animals compared to AD model mice. These results suggest that overexpression of Hsp27 protein might ameliorate certain symptoms of AD. Cell Stress Society International, 2013 Heat shock proteins nationallicence Transgenic mice nationallicence Mouse model nationallicence Alzheimer's disease nationallicence Amyloid plaques nationallicence Behavior tests nationallicence Electrophysiological recordings nationallicence Real-time Q-PCR nationallicence Tóth Melinda Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Ave. 62, 6726, Szeged, Hungary aut Szegedi Viktor Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Ave. 62, 6726, Szeged, Hungary aut Varga Edina Deparment of Medical Chemistry, Faculty of Medicine, University of Szeged, Dóm Square 11, Szeged, Hungary aut Juhász Gábor Deparment of Medical Chemistry, Faculty of Medicine, University of Szeged, Dóm Square 11, Szeged, Hungary aut Horváth János Deparment of Medical Chemistry, Faculty of Medicine, University of Szeged, Dóm Square 11, Szeged, Hungary aut Borbély Emőke Deparment of Medical Chemistry, Faculty of Medicine, University of Szeged, Dóm Square 11, Szeged, Hungary aut Csibrány Balázs Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Ave. 62, 6726, Szeged, Hungary aut Alföldi Róbert Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Ave. 62, 6726, Szeged, Hungary aut Lénárt Nikolett Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Ave. 62, 6726, Szeged, Hungary aut Penke Botond Deparment of Medical Chemistry, Faculty of Medicine, University of Szeged, Dóm Square 11, Szeged, Hungary aut Sántha Miklós Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Ave. 62, 6726, Szeged, Hungary aut Cell Stress and Chaperones Springer Netherlands 18/6(2013-11-01), 759-771 1355-8145 18:6<759 2013 18 12192 https://doi.org/10.1007/s12192-013-0428-9 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s12192-013-0428-9 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Tóth Melinda Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Ave. 62, 6726, Szeged, Hungary aut NATIONALLICENCE 700 1- Szegedi Viktor Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Ave. 62, 6726, Szeged, Hungary aut NATIONALLICENCE 700 1- Varga Edina Deparment of Medical Chemistry, Faculty of Medicine, University of Szeged, Dóm Square 11, Szeged, Hungary aut NATIONALLICENCE 700 1- Juhász Gábor Deparment of Medical Chemistry, Faculty of Medicine, University of Szeged, Dóm Square 11, Szeged, Hungary aut NATIONALLICENCE 700 1- Horváth János Deparment of Medical Chemistry, Faculty of Medicine, University of Szeged, Dóm Square 11, Szeged, Hungary aut NATIONALLICENCE 700 1- Borbély Emőke Deparment of Medical Chemistry, Faculty of Medicine, University of Szeged, Dóm Square 11, Szeged, Hungary aut NATIONALLICENCE 700 1- Csibrány Balázs Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Ave. 62, 6726, Szeged, Hungary aut NATIONALLICENCE 700 1- Alföldi Róbert Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Ave. 62, 6726, Szeged, Hungary aut NATIONALLICENCE 700 1- Lénárt Nikolett Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Ave. 62, 6726, Szeged, Hungary aut NATIONALLICENCE 700 1- Penke Botond Deparment of Medical Chemistry, Faculty of Medicine, University of Szeged, Dóm Square 11, Szeged, Hungary aut NATIONALLICENCE 700 1- Sántha Miklós Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Ave. 62, 6726, Szeged, Hungary aut NATIONALLICENCE 773 0- Cell Stress and Chaperones Springer Netherlands 18/6(2013-11-01), 759-771 1355-8145 18:6<759 2013 18 12192 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer