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| http://dx.doi.org/10.1016/j.jaci.2017.06.021 | DOI Listing |
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Division of Stem Cell Transplantation and Cellular Immunotherapies, Department of Medicine II, University Medical Center Schleswig-Holstein and Christian-Albrechts-University Kiel, Kiel, Germany.
Tumor cell phagocytosis by macrophages is considered a relevant mechanism of action for many therapeutic IgG antibodies. However, tumor cells employ several mechanisms to evade immune recognition, including hypersialylation. Here, we describe how reduction of sialic acid exposure on tumor cells promotes antibody-dependent tumor cell phagocytosis (ADCP) by macrophages.
View Article and Find Full Text PDFImmunoglobulin G N-glycan markers of mild cognitive impairment in a Chinese population with cerebrovascular stenosis: A case-control study.
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School of Public Health, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan 250117, China; The Second Affiliated Hospital of Shandong First Medical University, Taian 271099, China; School of Public Health, Jining Medical College, Jining 272067, China. Electronic address:
Background: Immunoglobulin G (IgG) N-glycans have been shown to regulate the inflammatory response in the context of disease. In recent years, it has been found to be associated with several neurodegenerative disorders. In this study, we examined the relationship between IgG N-glycans and mild cognitive impairment (MCI) in a high-risk population for MCI, specifically patients with cerebrovascular stenosis.
View Article and Find Full Text PDFSialylated IgG restrains lung inflammation.
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Cellulose functionalized magnetic beads for high throughput glycosylation analysis in biotherapeutic modalities.
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Bioprocessing Technology Institute (BTI), Agency for Science, Technology and Research (A*STAR), 20 Biopolis Way, #06-01 Centros, Singapore, 138668, Republic of Singapore.
The increasing demand for biotherapeutics has necessitated the evaluation of their critical quality attributes, one of which is glycosylation, an essential post-translational modification found on many biological molecules. In particular, the purification of N-glycans after their release from the proteins and derivatization is important in ensuring the removal of the deglycosylated protein, excess labelling reagents and salts for subsequent analysis. However, current methods of N-glycans purification are either expensive, laborious, time-consuming or not catered for high throughput analysis.
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Department of Biomedical Science, Cheongju University, Cheongju 28160, Republic of Korea.
Article Synopsis
- - The glycosylation profile of therapeutic proteins, especially sialylation, is important for their effectiveness and stability, particularly in fusion proteins used to treat angiogenic disorders.
- - A mass spectrometry method was used to analyze sialylation levels in VEGFR-IgG fusion proteins by examining different fractions from production media, revealing varying sialylation levels.
- - The study found that the overall sialylation levels matched the expected results from the different fractions, emphasizing the importance of LC-MS/MS-based analysis for quality control and consistency in biosimilar development.
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