In vitro study of interaction of 17 beta-hydroxysteroid dehydrogenase type 10 and cyclophilin D and its potential implications for Alzheimer's disease

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985882%3A_____%2F19%3A00518381" target="_blank" >RIV/67985882:_____/19:00518381 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.nature.com/articles/s41598-019-53157-7" target="_blank" >https://www.nature.com/articles/s41598-019-53157-7</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41598-019-53157-7" target="_blank" >10.1038/s41598-019-53157-7</a>

Jazyk výsledku

angličtina

Název v původním jazyce

In vitro study of interaction of 17 beta-hydroxysteroid dehydrogenase type 10 and cyclophilin D and its potential implications for Alzheimer's disease

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

In vitro study of interaction of 17 beta-hydroxysteroid dehydrogenase type 10 and cyclophilin D and its potential implications for Alzheimer's disease

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/NV16-27611A" target="_blank" >NV16-27611A: Interakce intracelulárního amyloidu beta a diagnostika Alzheimerovy nemoci</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Scientific Reports

ISSN

2045-2322

e-ISSN

—

Svazek periodika

—

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

12

Strana od-do

16700

Kód UT WoS článku

000496129600049

EID výsledku v databázi Scopus

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