Academic Journal

A sensitive high-resolution mass spectrometry method for quantifying intact M-protein light chains in patients with multiple myeloma

التفاصيل البيبلوغرافية
العنوان: A sensitive high-resolution mass spectrometry method for quantifying intact M-protein light chains in patients with multiple myeloma
المؤلفون: Muccio, Stéphane, Hirtz, Christophe, Descloux, Sandrine, Fedeli, Olivier, Macé, Sandrine, Lehmann, Sylvain, Vialaret, Jérôme
المساهمون: SANOFI Recherche, Institut des Neurosciences de Montpellier (INM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Cellules Souches, Plasticité Cellulaire, Médecine Régénératrice et Immunothérapies (IRMB), Centre Hospitalier Régional Universitaire Montpellier (CHRU Montpellier)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Ecole Supérieure de Commerce de Paris (ESCP Europe), Sanofi Aventis R&D Chilly-Mazarin
المصدر: ISSN: 0009-8981 ; Clinica Chimica Acta ; https://hal.science/hal-04649675 ; Clinica Chimica Acta, 2024, 552, pp.117634. ⟨10.1016/j.cca.2023.117634⟩.
بيانات النشر: HAL CCSD
Elsevier
سنة النشر: 2024
المجموعة: Université de Montpellier: HAL
مصطلحات موضوعية: High-resolution mass spectrometry, Interference, Light chain, Minimal residual disease, Monoclonal immunoglobulin, Multiple myeloma, MESH: Humans, MESH: Multiple Myeloma, MESH: Neoplasm, Residual, MESH: Mass Spectrometry, MESH: Immunoglobulin Light Chains, MESH: Antibodies, Monoclonal, MESH: Blood Proteins, [SDV]Life Sciences [q-bio]
الوصف: International audience ; To determine the disease status and the response to treatment for patients with multiple myeloma, measuring serum M-protein levels is a widely used alternative to invasive punctures to count malignant plasma cells in the bone marrow. However, the quantification of this monoclonal antibody, which varies from patient to patient, poses significant analytical challenges. This paper describes a sensitive and specific mass spectrometry assay that addresses two objectives: to overcome the potential interference of biotherapeutics in the measurement of M-proteins, and to determine the depth of response to treatment by assessing minimal residual disease. After immunocapture of immunoglobulins and free light chains in serum, heavy and light chains were dissociated by chemical reduction and separated by liquid chromatography. M-proteins were analyzed by high-resolution mass spectrometry using a method combining a full MS scan for isotyping and identification and a targeted single ion monitoring scan for quantification. This method was able to discriminate M-protein from the therapeutic antibody in all patient samples analyzed and allowed quantification of M-protein with a LLOQ of 2.0 to 3.5 µg/ml in 5 out of 6 patients. This methodology appears to be promising for assessing minimal residual disease with sufficient sensitivity, specificity, and throughput.
نوع الوثيقة: article in journal/newspaper
اللغة: English
Relation: info:eu-repo/semantics/altIdentifier/pmid/37980975; PUBMED: 37980975; WOS: 001121646500001
DOI: 10.1016/j.cca.2023.117634
الاتاحة: https://hal.science/hal-04649675
https://doi.org/10.1016/j.cca.2023.117634
رقم الانضمام: edsbas.B9B57E15
قاعدة البيانات: BASE
الوصف
DOI:10.1016/j.cca.2023.117634