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Interactions of 17 beta-Hydroxysteroid Dehydrogenase Type 10 and Cyclophilin D in Alzheimer's Disease

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11130%2F20%3A10410861" target="_blank" >RIV/00216208:11130/20:10410861 - isvavai.cz</a>

  • Alternative codes found

    RIV/00064203:_____/20:10410861

  • Result on the web

    <a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=mrGHBDlnGi" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=mrGHBDlnGi</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s11064-020-02970-y" target="_blank" >10.1007/s11064-020-02970-y</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Interactions of 17 beta-Hydroxysteroid Dehydrogenase Type 10 and Cyclophilin D in Alzheimer's Disease

  • Original language description

    The nucleus-encoded 17 beta-hydroxysteroid dehydrogenase type 10 (17 beta-HSD10) regulates cyclophilin D (cypD) in the mitochondrial matrix. CypD regulates opening of mitochondrial permeability transition pores. Both mechanisms may be affected by amyloid beta peptides accumulated in mitochondria in Alzheimer&apos;s disease (AD). In order to clarify changes occurring in brain mitochondria, we evaluated interactions of both mitochondrial proteins in vitro (by surface plasmon resonance biosensor) and detected levels of various complexes of 17 beta-HSD10 formed in vivo (by sandwich ELISA) in brain mitochondria isolated from the transgenic animal model of AD (homozygous McGill-R-Thy1-APP rats) and in cerebrospinal fluid samples of AD patients. By surface plasmon resonance biosensor, we observed the interaction of 17 beta-HSD10 and cypD in a direct real-time manner and determined, for the first time, the kinetic parameters of the interaction (k(a) 2.0 x 10(5) M(1)s(-1), k(d) 5.8 x 10(4) s(-1), and K-D 3.5 x 10(-10) M). In McGill-R-Thy1-APP rats compared to controls, levels of 17 beta-HSD10-cypD complexes were decreased and those of total amyloid beta increased. Moreover, the levels of 17 beta-HSD10-cypD complexes were decreased in cerebrospinal fluid of individuals with AD (in mild cognitive impairment as well as dementia stages) or with Frontotemporal lobar degeneration (FTLD) compared to cognitively normal controls (the sensitivity of the complexes to AD dementia was 92.9%, that to FTLD 73.8%, the specificity to AD dementia equaled 91.7% in a comparison with the controls but only 26.2% with FTLD). Our results demonstrate the weakened ability of 17 beta-HSD10 to regulate cypD in the mitochondrial matrix probably via direct effects of amyloid beta. Levels of 17 beta-HSD10-cypD complexes in cerebrospinal fluid seem to be the very sensitive indicator of mitochondrial dysfunction observed in neurodegeneration but unfortunately not specific to AD pathology. We do not recommend it as the new biomarker of AD.

  • 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

    30103 - Neurosciences (including psychophysiology)

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

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Neurochemical Research

  • ISSN

    0364-3190

  • e-ISSN

  • Volume of the periodical

    45

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    13

  • Pages from-to

    915-927

  • UT code for WoS article

    000510110200001

  • EID of the result in the Scopus database

    2-s2.0-85078782550