Počet záznamů: 1
In vitro study of interaction of 17 beta-hydroxysteroid dehydrogenase type 10 and cyclophilin D and its potential implications for Alzheimer's disease
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SYSNO ASEP 0518381 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název In vitro study of interaction of 17 beta-hydroxysteroid dehydrogenase type 10 and cyclophilin D and its potential implications for Alzheimer's disease Tvůrce(i) Hemmerová, Erika (URE-Y)
Špringer, Tomáš (URE-Y)
Krištofiková, Z. (CZ)
Homola, Jiří (URE-Y) RIDCelkový počet autorů 4 Číslo článku 16700 Zdroj.dok. Scientific Reports. - : Nature Publishing Group - ISSN 2045-2322
-, č. 9 (2019)Poč.str. 12 s. Forma vydání Tištěná - P Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova Surface-plasmon resonance ; A beta ; Mitochondrial dysfunction Vědní obor RIV CE - Biochemie Obor OECD Biochemistry and molecular biology CEP NV16-27611A GA MZd - Ministerstvo zdravotnictví Způsob publikování Open access Institucionální podpora URE-Y - RVO:67985882 UT WOS 000496129600049 DOI 10.1038/s41598-019-53157-7 Anotace In early stages of Alzheimer's disease (AD), amyloid-beta (A beta) accumulates in neuronal mitochondria where it interacts with a number of biomolecules including 17beta-hydroxysteroide dehydrogenase 10 (17 beta-HSD10) and cyclophilin D (cypD). It has been hypothesized that 17 beta-HSD10 interacts with cypD preventing it from opening mitochondrial permeability transition pores and that its regulation during AD may be affected by the accumulation of A beta. In this work, we demonstrate for the first time that 17 beta-HSD10 and cypD form a stable complex in vitro. Furthermore, we show that factors, such as pH, ionic environment and the presence of A beta, affect the ability of 17 beta-HSD10 to bind cypD. We demonstrate that K+ and Mg2+ ions present at low levels may facilitate this binding. We also show that different fragments of A beta (A beta(1-40) and A beta(1-42)) affect the interaction between 17 beta-HSD10 and cypD differently and that A beta(1-42) (in contrast to A beta(1-40)) is capable of simultaneously binding both 17 beta-HSD10 and cypD in a tricomplex. Pracoviště Ústav fotoniky a elektroniky Kontakt Petr Vacek, vacek@ufe.cz, Tel.: 266 773 413, 266 773 438, 266 773 488 Rok sběru 2020 Elektronická adresa https://www.nature.com/articles/s41598-019-53157-7
Počet záznamů: 1