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Co-localization of Interleukin-1 alpha and Annexin A2 at the plasma membrane in response to oxidative stress

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F20%3A10414160" target="_blank" >RIV/00216208:11310/20:10414160 - isvavai.cz</a>

  • Result on the web

    <a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=.VfEFZ4XCG" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=.VfEFZ4XCG</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.cyto.2020.155141" target="_blank" >10.1016/j.cyto.2020.155141</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Co-localization of Interleukin-1 alpha and Annexin A2 at the plasma membrane in response to oxidative stress

  • Original language description

    Interleukin-1 alpha (IL-1 alpha) and Annexin A2 (AnxA2) are pleiotropic molecules with both intracellular and extracellular roles. They share several characteristics including unconventional secretion aided by S100 proteins, anchoring of the externalized proteins at the outer surface of the plasma membrane and response to oxidative stress. Although IL-1 alpha and AnxA2 have been implicated in a variety of biological processes, including cancer, little is known about the mechanisms of their cellular release. In the present study, employing the non-cancerous breast epithelial MCF10A cells, we demonstrate that IL-1 alpha and AnxA2 establish a close association in response to oxidative stress. Stress conditions lead to translocation of both proteins towards lamellipodia rich in vimentin and association of full-length IL-1 alpha and Tyr23 phosphorylated AnxA2 with the plasma membrane at peripheral sites depleted of F-actin. Notably, membrane-associated IL-1 alpha and AnxA2 preferentially localize to the outer edges of the MCF10A cell islands, suggesting that the two proteins participate in the communication of these epithelial cells with their neighboring cells. Similarly, in U2OS osteosarcoma cell line both endogenous IL-1 alpha and transiently produced IL-1 alpha/EGFP associate with the plasma membrane. While benign MFC10A cells present membrane-associated IL-1 alpha and AnxA2 at the edges of their cell islands, the aggressive cancerous U2OS cells communicate in such manner also with distant cells.

  • 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

    10600 - Biological sciences

Result continuities

  • Project

    <a href="/en/project/LM2015062" target="_blank" >LM2015062: National Infrastructure for Biological and Medical Imaging</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>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

    Cytokine

  • ISSN

    1043-4666

  • e-ISSN

  • Volume of the periodical

    133

  • Issue of the periodical within the volume

    September

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    13

  • Pages from-to

    155141

  • UT code for WoS article

    000554002300019

  • EID of the result in the Scopus database

    2-s2.0-85086946959