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Pentacyclic triterpenoid ursolic acid interferes with mast cell activation via a lipid-centric mechanism affecting Fc epsilon RI signalosome functions

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F22%3A00565125" target="_blank" >RIV/68378050:_____/22:00565125 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.1016/j.jbc.2022.102497" target="_blank" >https://doi.org/10.1016/j.jbc.2022.102497</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.jbc.2022.102497" target="_blank" >10.1016/j.jbc.2022.102497</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Pentacyclic triterpenoid ursolic acid interferes with mast cell activation via a lipid-centric mechanism affecting Fc epsilon RI signalosome functions

  • Original language description

    Pentacyclic triterpenoids, including ursolic acid (UA), are bioactive compounds with multiple biological activities involving anti-inflammatory effects. However, the mode of their action on mast cells, key players in the early stages of allergic inflammation, and underlying molecular mechanisms remain enigmatic. To better understand the effect of UA on mast cell signaling, here we examined the consequences of short-term treatment of mouse bone marrow-derived mast cells with UA. Using IgE-sensitized and antigen-or thapsigargin-activated cells, we found that 15 min exposure to UA inhibited high affinity IgE receptor (FceRI)-mediated degranulation, calcium response, and extracellular calcium uptake. We also found that UA inhibited migration of mouse bone marrow-derived mast cells toward antigen but not toward prostaglandin E2 and stem cell factor. Compared to control antigen-activated cells, UA enhanced the production of tumor necrosis factor-alpha at the mRNA and protein levels. However, secretion of this cytokine was inhibited. Further analysis showed that UA enhanced tyrosine phosphorylation of the SYK kinase and several other proteins involved in the early stages of FceRI signaling, even in the absence of antigen activation, but inhibited or reduced their further phosphorylation at later stages. In addition, we show that UA induced changes in the properties of detergent-resistant plasma membrane microdomains and reduced antibody-mediated clustering of the FceRI and glycosylphosphatidylinositol-anchored protein Thy1. Finally, UA inhibited mobility of the FceRI and cholesterol. These combined data suggest that UA exerts its effects, at least in part, via lipid-centric plasma membrane perturbations, hence affecting the functions of the FceRI signalosome.

  • 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

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2022

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Biological Chemistry

  • ISSN

    0021-9258

  • e-ISSN

    1083-351X

  • Volume of the periodical

    28

  • Issue of the periodical within the volume

    11

  • Country of publishing house

    CZ - CZECH REPUBLIC

  • Number of pages

    17

  • Pages from-to

    102497

  • UT code for WoS article

    000886086000009

  • EID of the result in the Scopus database