Evidence map›Paper›PMID 41310581›Full record

ArticleBMC cancer2025

Therapy-induced remodeling of IgG and plasma N-glycans in breast cancer.

Martina Maričić Vrban, Barbara Radovani Trbojević, David Visentin, Katarina Ramljak, Iva Kirac, Mihaela Gaće, Ivan Milas, Gordan Lauc, Dragan Primorac, Ivan Gudelj

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Article in BMC cancer, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

10 authors.

Martina Maričić Vrban *University Hospital for Tumors, Sestre Milosrdnice University Hospital Center, Zagreb, Croatia.
Barbara Radovani Trbojević *Genos Glycoscience Research Laboratory, Zagreb, Croatia.
David VisentinFaculty of Biotechnology and Drug Development, University of Rijeka, Rijeka, Croatia.
Katarina RamljakFaculty of Medicine, University of Rijeka, Rijeka, Croatia.
Iva KiracUniversity Hospital for Tumors, Sestre Milosrdnice University Hospital Center, Zagreb, Croatia.
Mihaela GaćeUniversity Hospital for Tumors, Sestre Milosrdnice University Hospital Center, Zagreb, Croatia.
Ivan MilasUniversity Hospital for Tumors, Sestre Milosrdnice University Hospital Center, Zagreb, Croatia.
Gordan LaucGenos Glycoscience Research Laboratory, Zagreb, Croatia.
Dragan PrimoracFaculty of Dental Medicine and Health, Josip Juraj Strossmayer University of Osijek, Osijek, Croatia. draganprimorac2@gmail.com.
Ivan GudeljGenos Glycoscience Research Laboratory, Zagreb, Croatia. ivan.gudelj@uniri.hr.

Funding

HORIZON EUROPE Framework Programme 101159018
6 · The paper itself

Abstract

backgroundProtein N-glycosylation plays a key role in cancer biology and may offer insights into tumor behavior and treatment response. This study investigated changes in N-glycosylation of immunoglobulin G (IgG) and total plasma proteins in patients with breast cancer undergoing neoadjuvant chemotherapy.

methodsA prospective cohort of 34 women with early-stage or locally advanced breast cancer was recruited. Plasma samples were collected before and after neoadjuvant chemotherapy. IgG was isolated by immunoaffinity chromatography, and IgG and total plasma N-glycans were enzymatically released, fluorescently labeled, and analyzed using ultra-high performance liquid chromatography. Glycan traits were expressed as relative abundances and summarized into derived structural features. Longitudinal changes were assessed using linear mixed-effects models adjusted for age and body mass index.

resultsChemotherapy induced significant decrease in IgG core fucosylation. This effect varied by treatment: anthracycline-based regimen led to decreased core fucosylation and digalactosylation and increased monogalactosylation. The greatest reduction in core fucosylation was observed in patients treated with docetaxel and cyclophosphamide. HER2-targeted therapy was associated with decreased bisecting N-acetylglucosamine. Plasma glycosylation remained largely stable, though oligomannose glycans increased in patients following chemotherapy. Tumor size was significantly associated with several plasma glycan traits, particularly digalactosylation and oligomannosylation.

conclusionsIgG glycosylation patterns change in a treatment-specific manner during chemotherapy, potentially reflecting immune modulation. Plasma glycan traits are more stable but may reflect tumor burden. These results support the potential of glycan profiling as a biomarker for monitoring the impact of therapy and disease progression in breast cancer.

Indexed as

Breast NeoplasmsImmunoglobulin GPolysaccharidesAdultAgedAntineoplastic Combined Chemotherapy ProtocolsFemaleGlycosylationHumansMiddle AgedNeoadjuvant TherapyProspective StudiesImmunoglobulin GPolysaccharidesBreast cancerGlycan biomarkersGlycoprofilingImmunoglobulin GNeoadjuvant chemotherapyN-glycosylationPlasma proteins

Identifiers

PMID41310581
PMCPMC12781513

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