IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v11y2020i1d10.1038_s41467-020-19928-x.html
   My bibliography  Save this article

Analysis of inositol phosphate metabolism by capillary electrophoresis electrospray ionization mass spectrometry

Author

Listed:
  • Danye Qiu

    (Institute of Organic Chemistry, University of Freiburg)

  • Miranda S. Wilson

    (Medical Research Council, Laboratory for Molecular Cell Biology, University College London)

  • Verena B. Eisenbeis

    (Institute of Organic Chemistry, University of Freiburg)

  • Robert K. Harmel

    (Leibniz-Forschungsinstitut für Molekulare Pharmakologie)

  • Esther Riemer

    (Institute of Crop Science and Resource Conservation, Department of Plant Nutrition, Rheinische Friedrich-Wilhelms-University Bonn)

  • Thomas M. Haas

    (Institute of Organic Chemistry, University of Freiburg)

  • Christopher Wittwer

    (Institute of Organic Chemistry, University of Freiburg)

  • Nikolaus Jork

    (Institute of Organic Chemistry, University of Freiburg)

  • Chunfang Gu

    (Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health)

  • Stephen B. Shears

    (Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health)

  • Gabriel Schaaf

    (Institute of Crop Science and Resource Conservation, Department of Plant Nutrition, Rheinische Friedrich-Wilhelms-University Bonn)

  • Bernd Kammerer

    (Institute of Organic Chemistry, University of Freiburg)

  • Dorothea Fiedler

    (Leibniz-Forschungsinstitut für Molekulare Pharmakologie)

  • Adolfo Saiardi

    (Medical Research Council, Laboratory for Molecular Cell Biology, University College London)

  • Henning J. Jessen

    (Institute of Organic Chemistry, University of Freiburg
    CIBSS - Centre for Integrative Biological Signalling Studies, University of Freiburg)

Abstract

The analysis of myo-inositol phosphates (InsPs) and myo-inositol pyrophosphates (PP-InsPs) is a daunting challenge due to the large number of possible isomers, the absence of a chromophore, the high charge density, the low abundance, and the instability of the esters and anhydrides. Given their importance in biology, an analytical approach to follow and understand this complex signaling hub is desirable. Here, capillary electrophoresis (CE) coupled to electrospray ionization mass spectrometry (ESI-MS) is implemented to analyze complex mixtures of InsPs and PP-InsPs with high sensitivity. Stable isotope labeled (SIL) internal standards allow for matrix-independent quantitative assignment. The method is validated in wild-type and knockout mammalian cell lines and in model organisms. SIL-CE-ESI-MS enables the accurate monitoring of InsPs and PP-InsPs arising from compartmentalized cellular synthesis pathways, by feeding cells with either [13C6]-myo-inositol or [13C6]-D-glucose. In doing so, we provide evidence for the existence of unknown inositol synthesis pathways in mammals, highlighting the potential of this method to dissect inositol phosphate metabolism and signalling.

Suggested Citation

  • Danye Qiu & Miranda S. Wilson & Verena B. Eisenbeis & Robert K. Harmel & Esther Riemer & Thomas M. Haas & Christopher Wittwer & Nikolaus Jork & Chunfang Gu & Stephen B. Shears & Gabriel Schaaf & Bernd, 2020. "Analysis of inositol phosphate metabolism by capillary electrophoresis electrospray ionization mass spectrometry," Nature Communications, Nature, vol. 11(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19928-x
    DOI: 10.1038/s41467-020-19928-x
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-020-19928-x
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-020-19928-x?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Huanchen Wang & Lalith Perera & Nikolaus Jork & Guangning Zong & Andrew M. Riley & Barry V. L. Potter & Henning J. Jessen & Stephen B. Shears, 2022. "A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    2. Lingmin Yuan & Fei Gao & Zongyang Lv & Digant Nayak & Anindita Nayak & Priscila dos Santos Bury & Kristin E. Cano & Lijia Jia & Natalia Oleinik & Firdevs Cansu Atilgan & Besim Ogretmen & Katelyn M. Wi, 2022. "Crystal structures reveal catalytic and regulatory mechanisms of the dual-specificity ubiquitin/FAT10 E1 enzyme Uba6," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19928-x. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.