IgG and IgM glycosylation patterns in patients undergoing image-guided tumor ablation

Breen, Lucas; Pučić‐Baković, Maja; Vučković, Frano; Reiding, Karli R.; Trbojević‐Akmačić, Irena; Gajdošik, Martina Šrajer; Cook, Madeleine I.; Lopez, Michael J.; Wuhrer, Manfred; Camara, Lila; Andjelković, Uroš; Dupuy, Damian E.; Josić, Djuro

doi:10.1016/j.bbagen.2016.01.011

Cited by 14 publications

(13 citation statements)

References 37 publications

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Section: Introductionmentioning

confidence: 97%

“…Few publications looked at serum glycosylation in relation to cancer treatment monitoring. Glycosylation on serum IgG and IgM was found not to be changed after tumour ablation (liver, renal and lung tumours) (Breen et al, 2016). Miyahara et al (2015) described high mannosylated glycan Man9 as potential serum N-glycan biomarker of gemcitabine treatment efficacy in patients with pancreatic cancer; high levels of Man9 were correlated with short time to tumour progression and overall survival.…”

Section: Introductionmentioning

confidence: 99%

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Serum N‐glycome alterations in breast cancer during multimodal treatment and follow‐up

et al. 2017

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Using our recently developed high‐throughput automated platform, N‐glycans from all serum glycoproteins from patients with breast cancer were analysed at diagnosis, after neoadjuvant chemotherapy, surgery, radiotherapy and up to 3 years after surgery. Surprisingly, alterations in the serum N‐glycome after chemotherapy were pro‐inflammatory with an increase in glycan structures associated with cancer. Surgery, on the other hand, induced anti‐inflammatory changes in the serum N‐glycome, towards a noncancerous phenotype. At the time of first follow‐up, glycosylation in patients with affected lymph nodes changed towards a malignant phenotype. C‐reactive protein showed a different pattern, increasing after first line of neoadjuvant chemotherapy, then decreasing throughout treatment until 1 year after surgery. This may reflect a switch from acute to chronic inflammation, where chronic inflammation is reflected in the serum after the acute phase response subsides. In conclusion, we here present the first time‐course serum N‐glycome profiling of patients with breast cancer during and after treatment. We identify significant glycosylation changes with chemotherapy, surgery and follow‐up, reflecting the host response to therapy and tumour removal.

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Section: Introductionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

Serum N‐glycome alterations in breast cancer during multimodal treatment and follow‐up

et al. 2017

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“…Enzymatic release of N ‐linked glycans from the rest (of mostly) both protein and peptide backbone is now a routine procedure , and use of enzyme to different solid matrices enables rapid, reproducible, and efficient separation of carbohydrate moieties from glycoproteins . After separation by hydrophilic‐interaction chromatography (HILIC) or capillary electrophoresis, glycans are identified by mass spectrometry . Identification of individual oligosaccharides by their retention time in HILIC, enables very fast analysis of glycome, especially in biological fluids such as serum plasma, or urine .…”

Section: Analytical Approachesmentioning

confidence: 99%

“…After separation by hydrophilic‐interaction chromatography (HILIC) or capillary electrophoresis, glycans are identified by mass spectrometry . Identification of individual oligosaccharides by their retention time in HILIC, enables very fast analysis of glycome, especially in biological fluids such as serum plasma, or urine . Profiling of both cell‐surface and intracellular glycans is more complicated and requires additional steps such as cell or tissue homogenization and fractionation .…”

Section: Analytical Approachesmentioning

confidence: 99%

Glycosylation and metastases

2018

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The change of cellular glycosylation is one of the key events in malignant transformation and neoplastic progression, and tumor‐related glycosylation alterations are promising targets in both tumor diagnosis and therapy. Both malignant transformation and neoplastic progression are the consequence of gene expression alterations and alterations in protein expression. Micro environmental factors such as extracellular matrix (ECM) also play an important role in their growth and metastasis. Tumor‐associated glycans are important biomarker candidates for cancer diagnosis and prognosis, and analytical methods for their detection were developed recently. Glycoproteomics that use mass spectrometry for identification of cancer antigens and structural analysis of glycans play a key role in the investigation of changes of glycosylation during malignant transformation and tumor development and metastasis. Deep understanding of glycan remodeling in cancer and the role of glycosyltransferases that are involved in this process will require a detailed profiling of glycosylation patterns of tumor cells, and corresponding analytical methods for their detection were developed.

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“…Chromatographic methods, on the other hand, provide a great platform for concurrent protein isolation, as was shown by Breen et al. who successfully isolated both IgG and IgM using protein A affinity chromatography followed by separation on a strong anion exchange columns . High‐throughput (HTP) fractionation of human plasma using the same approach allowed for the isolation of IgM from a large number of samples .…”

Section: Introductionmentioning

confidence: 99%

Affinity chromatography on monolithic supports for simultaneous and high‐throughput isolation of immunoglobulins from human serum

et al. 2017

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Posttranslational modifications of immunoglobulins have been a topic of great interest and have been repeatedly reported as a major factor in disease pathology. Cost-effective, reproducible, and high-throughput (HTP) isolation of immunoglobulins from human serum is vital for studying the changes in protein structure and the following understanding of disease development. Although there are many methods for the isolation of specific immunoglobulin classes, only a few of them are applicable for isolation of all subtypes and variants. Here, we present the development of a scheme for fast and simultaneous affinity purification of α (A), γ (G), and μ (M) immunoglobulins from human serum through affinity monolith chromatography. Affinity-based monolithic columns with immobilized protein A, G, or L were used for antibody isolation. Monolithic stationary phases have a high surface accessibility of binding sites, large flow-through channels, and can be operated at high flow rates, making them the ideal supports for HTP isolation of biopolymers. The presented method can be used for HTP screening of human serum in order to simultaneously isolate all three above-mentioned immunoglobulins and determine their concentration and changes in their glycosylation pattern as potential prognostic and diagnostic disease biomarkers.

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IgG and IgM glycosylation patterns in patients undergoing image-guided tumor ablation

Cited by 14 publications

References 37 publications

Serum N‐glycome alterations in breast cancer during multimodal treatment and follow‐up

Serum N‐glycome alterations in breast cancer during multimodal treatment and follow‐up

Glycosylation and metastases

Affinity chromatography on monolithic supports for simultaneous and high‐throughput isolation of immunoglobulins from human serum

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