JAN 18, 2018 07:00 AM PST

WEBINAR: Mass Spectrometry-based Protein Tests: Opportunities and Challenges for Laboratory Medicine

C.E. CREDITS: P.A.C.E. CE | Florida CE
  • Professor of Clinical Chemistry and Laboratory Medicine Department of Clinical Chemistry and Laboratory Medicine Leiden University Medical Center (LUMC), Leiden (NL)
      Christa Cobbaert is Professor of Clinical Chemistry and Laboratory Medicine at the University of Leiden. She is heading the Department of Clinical Chemistry and Laboratory Medicine of the Leiden University Medical Center.
      Her scientific research focuses on standardization, harmonization and trueness verification of medical test results, for the sake of better of patient care. Her scientific work is done in close collaboration with the Dutch External Quality Assessment Scheme organizer (SKML) and with international colleagues which collaborate in joint working groups. Her efforts resulted in ca. 150 original publications and several appointments on (inter)national positions because of her expertise on metrological traceability of test results.
      She is vice chair of the International Federation of Clinical Chemistry (IFCC) Scientific Division EC and member of ISO TC 212/ working group 2. She also chairs the European Federation of Laboratory Medicine (EFLM) working group on Test Evaluation. At the national level she is heading the Dutch Calibration 2.000 initiative. Currently, she moved to research on the selection, development and standardization of protein biomarkers using quantitative clinical chemistry proteomics, as a promising alternative for flawed and hardly standardized immunoassays. In that context, she leads the IFCC working group on standardization of serum apolipoproteins by mass spectrometry.


    DATE: January 18, 2018
    TIME: 7:00 AM PST, 10:00 AM EST

    Tandem mass spectrometry (MS) is advertised as a detection and quantification method that alleviates most of the flaws inherent to immunoassays. In 2012, MS-based targeted proteomics was declared method of the year as it allows quantification of either specific proteoforms* or specific subsets of proteins of interest. MS-based targeted proteomics can also be used in a highly multiplexed format and allows for precise molecular characterization of the measurands.

    Targeted proteomics is frequently performed using a typical MRM-workflow consisting of five steps: defining the protein set of interest based on the clinical or biological question; selecting appropriate peptides which are proteotypic and have suitable LC/MS properties; selecting transitions based on their intensity; analytically validating the transitions to prevent interferences and quantitating the specific protein(s) by calibration using either value-assigned peptide or matrix-based calibrators.

    The most critical step for absolute quantification of proteins in body fluids is the sample preparation, and more specifically the (trypsin) digestion step.

    MS-based targeted proteomics will be presented which have great potential as an alternative technology to antibody-based protein assays in hypothesis driven clinical trials. Our research has shown that from a standardization viewpoint, major advantages of MRM coupled to MS are its potential to unequivocally measure specific molecular entities, to assess directly the compounds of interest, and the lack of non-selectivity if transitions are well selected.

    Learning Objectives:

    • Understanding test purpose and test role of MS-based protein tests
    • Understanding a targeted proteomics workflow for quantification of MS-based protein tests, as well as the critical steps for standardization
    • Understanding the challenges which have to be overcome during development and routine operation of MS-based protein tests.

    For Research Use Only. Not for use in diagnostic procedures.

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