ArticleClinical chemistry and laboratory medicine2021
Development of novel methods for non-canonical myeloma protein analysis with an innovative adaptation of immunofixation electrophoresis, native top-down mass spectrometry, and middle-down
Article in Clinical chemistry and laboratory medicine, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Endogenous monoclonal immunoglobulins analyzed using the EXENT® solution and LC-MS.Journal of mass spectrometry and advances in the clinical lab · 2024Article
- Direct Mass Spectrometry-Based Detection and Antibody Sequencing of Monoclonal Gammopathy of Undetermined Significance from Patient Serum: A Case Study.Journal of proteome research · 2023Article
- Advances in Ultra-High-Resolution Mass Spectrometry for Pharmaceutical Analysis.Molecules (Basel, Switzerland) · 2023Review
- The changing landscape of relapsed and/or refractory multiple myeloma (MM): fundamentals and controversies.Biomarker research · 2022Review
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Authors and funding
15 authors at 5 institutions in 2 countries.
Funding
Abstract
objectivesMultiple myeloma (MM) is a malignant plasma cell neoplasm, requiring the integration of clinical examination, laboratory and radiological investigations for diagnosis. Detection and isotypic identification of the monoclonal protein(s) and measurement of other relevant biomarkers in serum and urine are pivotal analyses. However, occasionally this approach fails to characterize complex protein signatures. Here we describe the development and application of next generation mass spectrometry (MS) techniques, and a novel adaptation of immunofixation, to interrogate non-canonical monoclonal immunoproteins.
methodsImmunoprecipitation immunofixation (IP-IFE) was performed on a Sebia Hydrasys Scan2. Middle-down
resultsWe adapted a novel variation of immunofixation electrophoresis (IFE) with an antibody-specific immunosubtraction step, providing insight into the clonal signature of gamma-zone monoclonal immunoglobulin (M-protein) species. We developed and applied advanced mass spectrometric techniques such as middle-down
conclusionsNext generation proteomic solutions offer great potential for characterizing complex protein structures and may eventually replace current electrophoretic approaches for the identification and quantification of M-proteins. They can also contribute to greater understanding of MM pathogenesis, enabling classification of patients into new subtypes, improved risk stratification and the potential to inform decisions on future personalized treatment modalities.
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