{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T22:28:27Z","timestamp":1772231307763,"version":"3.50.1"},"reference-count":41,"publisher":"Walter de Gruyter GmbH","issue":"8","license":[{"start":{"date-parts":[[2024,2,9]],"date-time":"2024-02-09T00:00:00Z","timestamp":1707436800000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,7,26]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec id=\"j_cclm-2023-1189_abs_001\">\n                    <jats:title>Objectives<\/jats:title>\n                    <jats:p>Multiple myeloma (MM) is a plasma cell malignancy characterized by a monoclonal expansion of plasma cells that secrete a characteristic M-protein. This M-protein is crucial for diagnosis and monitoring of MM in the blood of patients. Recent evidence has emerged suggesting that N-glycosylation of the M-protein variable (Fab) region contributes to M-protein pathogenicity, and that it is a risk factor for disease progression of plasma cell disorders. Current methodologies lack the specificity to provide a site-specific glycoprofile of the Fab regions of M-proteins. Here, we introduce a novel glycoproteogenomics method that allows detailed M-protein glycoprofiling by integrating patient specific Fab region sequences (genomics) with glycoprofiling by glycoproteomics.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec id=\"j_cclm-2023-1189_abs_002\">\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>\n                      Glycoproteogenomics was used for the detailed analysis of\n                      <jats:italic>de novo<\/jats:italic>\n                      N-glycosylation sites of M-proteins. First, Genomic analysis of the M-protein variable region was used to identify\n                      <jats:italic>de novo<\/jats:italic>\n                      N-glycosylation sites. Subsequently glycopeptide analysis with LC-MS\/MS was used for detailed analysis of the M-protein glycan sites.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec id=\"j_cclm-2023-1189_abs_003\">\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>Genomic analysis uncovered a more than two-fold increase in the Fab Light Chain N-glycosylation of M-proteins of patients with Multiple Myeloma compared to Fab Light Chain N-glycosylation of polyclonal antibodies from healthy individuals. Subsequent glycoproteogenomics analysis of 41 patients enrolled in the IFM 2009 clinical trial revealed that the majority of the Fab N-glycosylation sites were fully occupied with complex type glycans, distinguishable from Fc region glycans due to high levels of sialylation, fucosylation and bisecting structures.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec id=\"j_cclm-2023-1189_abs_004\">\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>\n                      Together, glycoproteogenomics is a powerful tool to study\n                      <jats:italic>de novo<\/jats:italic>\n                      Fab N-glycosylation in plasma cell dyscrasias.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1515\/cclm-2023-1189","type":"journal-article","created":{"date-parts":[[2024,2,9]],"date-time":"2024-02-09T02:50:18Z","timestamp":1707447018000},"page":"1626-1635","source":"Crossref","is-referenced-by-count":8,"title":["N-linked glycosylation of the M-protein variable region: glycoproteogenomics reveals a new layer of personalized complexity in multiple myeloma"],"prefix":"10.1515","volume":"62","author":[{"given":"Pieter","family":"Langerhorst","sequence":"first","affiliation":[{"name":"Department of Laboratory Medicine , Radboud University Medical Center , Nijmegen , The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Melissa","family":"Baerenfaenger","sequence":"additional","affiliation":[{"name":"Department of Neurology , Donders Institute for Brain, Cognition, and Behavior, Radboud University Medical Center , Nijmegen , The Netherlands"},{"name":"Division of BioAnalytical Chemistry , Vrije Universiteit Amsterdam , Amsterdam , The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Purva","family":"Kulkarni","sequence":"additional","affiliation":[{"name":"Department of Laboratory Medicine , Radboud University Medical Center , Nijmegen , The Netherlands"},{"name":"Department of Medical BioSciences , Radboud University Medical Center , Nijmegen , The Netherlands"},{"name":"Department of Human Genetics , Radboud University Medical Center , Nijmegen , The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0748-0284","authenticated-orcid":false,"given":"Simon","family":"Nadal","sequence":"additional","affiliation":[{"name":"CY Cergy Paris Universit\u00e9, CNRS, BioCIS , Cergy-Pontoise , France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9057-8751","authenticated-orcid":false,"given":"Charissa","family":"Wijnands","sequence":"additional","affiliation":[{"name":"Department of Laboratory Medicine , Radboud University Medical Center , Nijmegen , The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Merel A.","family":"Post","sequence":"additional","affiliation":[{"name":"Department of Neurology , Donders Institute for Brain, Cognition, and Behavior, Radboud University Medical Center , Nijmegen , The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Somayya","family":"Noori","sequence":"additional","affiliation":[{"name":"Department of Neurology , Erasmus University Medical Center , Rotterdam , The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6654-994X","authenticated-orcid":false,"given":"Martijn M.","family":"vanDuijn","sequence":"additional","affiliation":[{"name":"Department of Neurology , Erasmus University Medical Center , Rotterdam , The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Irma","family":"Joosten","sequence":"additional","affiliation":[{"name":"Department of Laboratory Medicine , Radboud University Medical Center , Nijmegen , The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thomas","family":"Dejoie","sequence":"additional","affiliation":[{"name":"Biochemistry Laboratory , Centre Hospitalier Universitaire (CHU) , Nantes , France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alain J.","family":"van Gool","sequence":"additional","affiliation":[{"name":"Department of Laboratory Medicine , Radboud University Medical Center , Nijmegen , The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jolein","family":"Gloerich","sequence":"additional","affiliation":[{"name":"Department of Laboratory Medicine , Radboud University Medical Center , Nijmegen , The 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Multiple myeloma. Lancet 2015;385:2197\u2013208. https:\/\/doi.org\/10.1016\/s0140-6736(14)60493-1.","DOI":"10.1016\/S0140-6736(14)60493-1"},{"key":"2024071605441124988_j_cclm-2023-1189_ref_002","doi-asserted-by":"crossref","unstructured":"Willrich, MAV, Murray, DL, Kyle, RA. Laboratory testing for monoclonal gammopathies: focus on monoclonal gammopathy of undetermined significance and smoldering multiple myeloma. Clin Biochem 2018;51:38\u201347. https:\/\/doi.org\/10.1016\/j.clinbiochem.2017.05.001.","DOI":"10.1016\/j.clinbiochem.2017.05.001"},{"key":"2024071605441124988_j_cclm-2023-1189_ref_003","doi-asserted-by":"crossref","unstructured":"Langerhorst, P, Brinkman, AB, VanDuijn, MM, Wessels, HJCT, Groenen, PJTA, Joosten, I, et al.. Clonotypic features of rearranged immunoglobulin genes yield personalized biomarkers for minimal residual disease monitoring in multiple myeloma. Clin Chem 2021;67:867\u201375. https:\/\/doi.org\/10.1093\/clinchem\/hvab017.","DOI":"10.1093\/clinchem\/hvab017"},{"key":"2024071605441124988_j_cclm-2023-1189_ref_004","doi-asserted-by":"crossref","unstructured":"Di Noia, JM, Neuberger, MS. Molecular mechanisms of antibody somatic hypermutation. Ann Rev Biochem 2007;76:1\u201322. https:\/\/doi.org\/10.1146\/annurev.biochem.76.061705.090740.","DOI":"10.1146\/annurev.biochem.76.061705.090740"},{"key":"2024071605441124988_j_cclm-2023-1189_ref_005","doi-asserted-by":"crossref","unstructured":"Barnidge, DR, Tschumper, RC, Theis, JD, Snyder, MR, Jelinek, DF, Katzmann, JA, et al.. Monitoring M-proteins in patients with multiple myeloma using heavy-chain variable region clonotypic peptides and LC-MS\/MS. 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