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Quantification of cellular protein and redox imbalance using SILAC-iodoTMT methodology

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00179906%3A_____%2F19%3A10395027" target="_blank" >RIV/00179906:_____/19:10395027 - isvavai.cz</a>

  • Alternative codes found

    RIV/68378050:_____/19:00506176

  • Result on the web

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

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.redox.2019.101227" target="_blank" >10.1016/j.redox.2019.101227</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Quantification of cellular protein and redox imbalance using SILAC-iodoTMT methodology

  • Original language description

    Under normal conditions, the cellular redox status is maintained in a steady state by reduction and oxidation processes. These redox alterations in the cell are mainly sensed by protein thiol residues of cysteines thus regulating protein function. The imbalance in redox homeostasis may therefore regulate protein turnover either directly by redox modulating of transcription factors or indirectly by the degradation of damaged proteins due to oxidation. A new analytical method capable of simultaneously assessing cellular protein expression and cysteine oxidation would provide a valuable tool for the field of cysteine-targeted biology. Here, we show a workflow based on protein quantification using metabolic labeling and determination of cysteine oxidation using reporter ion quantification. We applied this approach to determine protein and redox changes in cells after 5-min, 60-min and 32-h exposure to H2O2, respectively. Based on the functional analysis of our data, we confirmed a biological relevance of this approach and its applicability for parallel mapping of cellular proteomes and redoxomes under diverse conditions. In addition, we revealed a specific pattern of redox changes in peroxiredoxins in a short time-interval cell exposure to H2O2. Overall, our present study offers an innovative, versatile experimental approach to the multifaceted assessment of cellular proteome and its redox status, with broad implications for biomedical research towards a better understanding of organismal physiology and diverse disease conditions.

  • 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/GA15-03379S" target="_blank" >GA15-03379S: Role of oxidative stress in the interplay between cellular senescence and apoptosis</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

    Redox Biology

  • ISSN

    2213-2317

  • e-ISSN

  • Volume of the periodical

    24

  • Issue of the periodical within the volume

    Jun

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    7

  • Pages from-to

    101227

  • UT code for WoS article

    000471255400054

  • EID of the result in the Scopus database

    2-s2.0-85066265432