ReviewThe Biochemical journal2025
The biology of interleukin-6 family cytokines is regulated by glycosylation.
Review in The Biochemical journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Overexpression of human interleukin 6 in NaCl inducible bacterial system and its characterization.Applied biochemistry and biotechnology · 2026Article
- The lithium-magnesium-zinc axis under stress: regulation of N-glycosylation-linked proteostasis and Alzheimer's disease.Inflammopharmacology · 2026Article
- Review
- Exercise, Exerkines, and Sarcopenia.Diabetes & metabolism journal · 2026Review
- Exercise-specific post-translational modification signatures: unveiling precise regulatory mechanisms of molecular exercise language and cellular adaptation.Frontiers in sports and active living · 2026Review
- Comparative analysis of adipose-, bone marrow-, and amniotic membrane-derived MSC secretomes and EVs reveals shared and source-specific therapeutic signatures for osteoarthritis.Extracellular vesicles and circulating nucleic acids · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytokines of the interleukin-6 (IL-6) family are important soluble mediators with crucial roles in developmental processes, tissue homeostasis, regeneration, and immune cell differentiation. Overshooting activities of IL-6 and other cytokines are found in all inflammatory diseases, making them attractive therapeutic targets for the treatment of patients with rheumatoid arthritis or inflammatory bowel disease. Multiple mechanisms exist that control cytokine activity and prevent excessive cytokine signaling under normal conditions. In this review, we summarize how the biology of IL-6 family cytokines is regulated by glycosylation, a process in which carbohydrate chains are covalently linked to protein molecules. The attached carbohydrates, which are generated and modified by enzymes located in the endoplasmic reticulum and/or the Golgi apparatus, can display huge structural diversity and are linked either via asparagine (N-glycans), serine and threonine (O-glycans), or tryptophan residues (C-glycans). We describe how glycosylation affects synthesis, receptor binding, signaling and plasma half-life of the cytokines and protein stability, transport to the cell surface, ligand binding, proteolysis, internalization, and recycling of their receptors. Finally, we discuss how knowledge about glycosylation can be used for the design of novel therapeutics targeting IL-6 family cytokines or their receptors.
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Registered trials
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