Immunoglobulin G glycosylation in aging and diseases

Gudelj, Ivan; Lauc, Gordan; Pezer, Marija

doi:10.1016/j.cellimm.2018.07.009

Cited by 330 publications

(388 citation statements)

References 283 publications

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“…2A). This trait is known to be dominated by IgG, and accordingly, decreased levels of IgG galactosylation with increasing age have been described in the literature, both at the level of total IgG glycans [28] and in a subclass-specific manner looking at Fc glycans of IgG1 and IgG2 [5,25,29] which is in accordance with the concept of inflammaging [6,30]. In addition, this IgG-related galactosylation trait was negatively associated with BMI ( Fig.…”

Section: N-glycome Associations With Age Sex and Bmisupporting

confidence: 71%

“…A high ratio between multibranched sialylated and galactosylated diantennary glycans in UC patients showed higher prognostic value than the two commonly used markers . In inflammatory diseases including IBD, the altered fucosylation and galactosylation of diantennary glycans can be attributed to changes in relative levels and the glycosylation of Igs, especially IgG , while the increased branching and sialylation were mostly caused by glycans derived from α1‐acid glycoprotein and other acute‐phase proteins released mainly by the liver (Fig. ).…”

Section: N‐glycomic Signatures Of Major Human Diseasesmentioning

confidence: 97%

“…Protein glycosylation has been described to change with many biological and pathological processes such as cellular (de‐)differentiation as well as in cellular degeneration in the course of malignancies . Consequently, glycosylation changes and/or signatures have been described for many diseases including various types of cancer, autoimmune diseases, and infectious diseases.…”

mentioning

confidence: 99%

“…Consequently, glycosylation changes and/or signatures have been described for many diseases including various types of cancer, autoimmune diseases, and infectious diseases. In addition, many physiological and behavioral parameters such as sex, age, body mass index (BMI), and smoking have been shown to be associated with protein glycosylation .…”

mentioning

confidence: 99%

“…Together with the often only partial occupancy of glycosylation sites (macroheterogeneity), this results in an immense complexity of the human glycoproteome. Protein glycosylation has been described to change with many biological and pathological processes such as cellular (de-)differentiation as well as in cellular degeneration in the course of malignancies [1,[3][4][5]. Consequently, glycosylation changes and/or signatures have been described for many diseases including N-glycome associations with genetic and common disease risk factors…”

mentioning

confidence: 99%

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N‐glycome signatures in human plasma: associations with physiology and major diseases

Dotz

Wuhrer

2019

FEBS Letters

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N‐glycome analysis in total plasma or serum yields information about the levels and glycosylation patterns of major plasma glycoproteins, including immunoglobulins, acute‐phase proteins, and apolipoproteins. Until recently, glycomic studies in disease settings largely suffered from small cohort sizes, poor analytical resolution, and poor comparability of results owing to the diversity of analytical techniques. Here, we report on recent advances in high‐throughput mass spectrometry glycomics technology that enabled elucidation of N‐glycome signatures in the plasma of patients with type 2 diabetes, inflammatory bowel disease, or colorectal cancer. Use of this technology revealed both commonalities and differences among disease fingerprints. Moreover, we summarize findings on glycomic signatures associated with age, sex, and body mass index. High‐throughput, high‐resolution glycomics technologies, together with robust data analysis workflows, will advance clinical translation.

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Section: N-glycome Associations With Age Sex and Bmisupporting

confidence: 71%

Section: N‐glycomic Signatures Of Major Human Diseasesmentioning

confidence: 97%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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N‐glycome signatures in human plasma: associations with physiology and major diseases

Dotz

Wuhrer

2019

FEBS Letters

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Glycans as a key factor in self and nonself discrimination: impact on the breach of immune tolerance

et al. 2022

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Glycans are carbohydrates that are made by all organisms and covalently conjugated to other biomolecules. Glycans cover the surface of both human cells and pathogens and are fundamental to defining the identity of a cell or an organism, thereby contributing to discriminating self from nonself. As such, glycans are a class of ‘Self‐Associated Molecular Patterns’ that can fine‐tune host inflammatory processes. In fact, glycans can be sensed and recognized by a variety of glycan‐binding proteins (GBP) expressed by immune cells, such as galectins, siglecs, and C‐type lectins, which recognize changes in the cellular glycosylation, instructing both pro‐inflammatory and anti‐inflammatory responses. In this review, we introduce glycans as cell‐identification structures, discussing how glycans modulate host–pathogen interactions and how they can fine‐tune inflammatory processes associated with infection, inflammation and autoimmunity. Finally, from the clinical standpoint, we discuss how glycoscience research can benefit life sciences and clinical medicine by providing a source of valuable biomarkers and therapeutic targets for immunity.

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Divergent Enzymatic Assembly of a Comprehensive 64‐Membered IgG N‐Glycan Library for Functional Glycomics

Ma,

Xu,

Jiang

et al. 2023

Advanced Science

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N‐Glycosylation, a main post‐translational modification of Immunoglobulin G (IgG), plays a significant role in modulating the immune functions of IgG. However, the precise function elucidation of IgG N‐glycosylation remains impeded due to the obstacles in obtaining comprehensive and well‐defined N‐glycans. Here, an easy‐to‐implement divergent approach is described to synthesize a 64‐membered IgG N‐glycan library covering all possible biantennary and bisected N‐glycans by reprogramming biosynthetic assembly lines based on the inherent branch selectivity and substrate specificity of enzymes. The unique binding specificities of 64 N‐glycans with different proteins are deciphered by glycan microarray technology. This unprecedented collection of synthetic IgG N‐glycans can serve as standards for N‐glycan structure identification in complex biological samples and the microarray data enrich N‐glycan glycomics to facilitate biomedical applications.

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Immunoglobulin G glycosylation in aging and diseases

Cited by 330 publications

References 283 publications

N‐glycome signatures in human plasma: associations with physiology and major diseases

N‐glycome signatures in human plasma: associations with physiology and major diseases

Glycans as a key factor in self and nonself discrimination: impact on the breach of immune tolerance

Divergent Enzymatic Assembly of a Comprehensive 64‐Membered IgG N‐Glycan Library for Functional Glycomics

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