Publications by authors named "P Link-Lenczowski"

The modulation of the N-glycosylation status in immune checkpoints, particularly the PD-1/PD-L1 axis, has emerged as a promising approach to enhance cancer immunotherapies. While immune checkpoint inhibitors (ICIs) targeting PD-1 and PD-L1 have achieved significant clinical success, recent studies highlight the critical role of N-glycosylation in regulating their expression, stability, and function. Alterations in N-glycosylation might affect the efficacy of ICIs by modulating the interactions between immune checkpoints and antibodies used in therapy.

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The immune system is strictly regulated by glycosylation through the addition of highly diverse and dynamically changing sugar structures (glycans) to the majority of immune cell receptors. Although knowledge in the field of glycoimmunology is still limited, numerous studies point to the key role of glycosylation in maintaining homeostasis, but also in reflecting its disruption. Changes in oligosaccharide patterns can lead to impairment of both innate and acquired immune responses, with important implications in the pathogenesis of diseases, including autoimmunity.

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The -glycome of immunoglobulin G (IgG), the most abundant glycoprotein in human blood serum, reflects pathological conditions of autoimmunity and is sensitive to medicines applied in disease therapy. Due to the high sensitivity of -glycosylation, the IgG -glycan profile may serve as an indicator of an ongoing inflammatory process. The IgG structure and its effector functions are strongly dependent on the composition of -glycans attached to the Fc fragment, and the binding of antigens is regulated by Fab sugar moieties.

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Article Synopsis
  • Autoimmune diseases trigger alterations in protein glycosylation, significantly impacting both immune responses and affected tissues.
  • Notably, alterations like agalactosylation of immunoglobulin G (IgG) are commonly seen in diseases such as rheumatoid arthritis, systemic lupus erythematosus, inflammatory bowel disease, and multiple sclerosis.
  • Changes in IgG glycosylation, including decreased core fucosylation, serve as potential biomarkers for autoimmune conditions, influencing T cell activation and overall immune response.
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Article Synopsis
  • Hashimoto's thyroiditis (HT) is an autoimmune disorder that primarily causes inflammation of the thyroid gland and is the leading cause of hypothyroidism, though its exact mechanisms remain unclear.* -
  • The study used high-performance liquid chromatography and mass spectrometry to analyze serum N-glycans in HT patients, revealing changes in glycosylation patterns, particularly an increase in specific sialylated structures and a decrease in core fucosylation.* -
  • These glycosylation alterations may be linked to the chronic inflammation associated with HT, indicating that serum protein sialylation changes are characteristic of autoimmune processes in this condition.*
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