All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

In vitro study of interaction of 17 beta-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%2F67985882%3A_____%2F19%3A00518381" target="_blank" >RIV/67985882:_____/19:00518381 - 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 17 beta-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-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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • 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

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

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

  • Volume of the periodical

  • Issue of the periodical within the volume

    9

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    12

  • Pages from-to

    16700

  • UT code for WoS article

    000496129600049

  • EID of the result in the Scopus database