In vitro study of interaction of 17β-hydroxysteroid dehydrogenase type 10 and cyclophilin D and its potential implications for Alzheimer’s disease
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00023752%3A_____%2F19%3A43920020" target="_blank" >RIV/00023752:_____/19:43920020 - isvavai.cz</a>
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
In vitro study of interaction of 17β-hydroxysteroid dehydrogenase type 10 and cyclophilin D and its potential implications for Alzheimer’s disease
Original language description
In early stages of Alzheimer’s disease (AD), amyloid-β (Aβ) accumulates in neuronal mitochondria where it interacts with a number of biomolecules including 17beta-hydroxysteroide dehydrogenase 10 (17β-HSD10) and cyclophilin D (cypD). It has been hypothesized that 17β-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 Aβ. In this work, we demonstrate for the first time that 17β-HSD10 and cypD form a stable complex in vitro. Furthermore, we show that factors, such as pH, ionic environment and the presence of Aβ, affect the ability of 17β-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 Aβ (Aβ1–40 and Aβ1–42) affect the interaction between 17β-HSD10 and cypD differently and that Aβ1–42 (in contrast to Aβ1–40) is capable of simultaneously binding both 17β-HSD10 and cypD in a tri-complex.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/NV16-27611A" target="_blank" >NV16-27611A: Interactions of intracellular amyloid beta and diagnosis of Alzheimer disease</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Scientific Reports
ISSN
2045-2322
e-ISSN
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Volume of the periodical
9
Issue of the periodical within the volume
1
Country of publishing house
GB - UNITED KINGDOM
Number of pages
12
Pages from-to
"Article Number: 16700"
UT code for WoS article
000496129600049
EID of the result in the Scopus database
2-s2.0-85074961050