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Glycosaminoglycans bind human IL-27 and regulate its activity
Marie-Charlotte Cavé1, Solène Maillard2, Karen Hildenbrand3
1Sorbonne Université, INSERM, CNRS, Centre d'Immunologie et des Maladies Infectieuses (Cimi-Paris), Paris, France.
European Journal of Immunology
|June 3, 2020
Summary
Glycosaminoglycans (GAGs) regulate interleukin-27 (IL-27) activity. Soluble GAGs inhibit IL-27, while membrane-bound GAGs may enhance it, impacting immune responses and clinical treatments.
Area of Science:
- Immunology
- Biochemistry
- Molecular Biology
Background:
- Interleukin-27 (IL-27) is a cytokine crucial for immune regulation, hematopoiesis, angiogenesis, and bone formation.
- IL-27 signaling involves its receptor (IL-27Rα and gp130) activating the STAT pathway.
Purpose of the Study:
- To investigate the modulatory effects of glycosaminoglycans (GAGs) on human IL-27 activity.
- To elucidate the mechanisms by which GAGs interact with IL-27 and its receptor.
Main Methods:
- In vitro biochemical assays to study GAG-IL-27 binding and STAT signaling inhibition.
- In silico analyses to predict binding interactions.
- Assessment of IL-27 activity using STAT signaling and downstream biological effects.
Main Results:
- Soluble heparin and heparan sulfate significantly inhibit human IL-27 activity by preventing receptor binding.
- Membrane-bound heparan sulfate appears to positively regulate IL-27 activity.
- Murine IL-27 showed less inhibition by soluble GAGs compared to human IL-27.
- Clinical heparin derivatives had minimal impact on human IL-27 activity.
Conclusions:
- GAGs are novel regulators of human IL-27 activity, influencing immune responses.
- GAGs' interaction with IL-27 has potential physiological and clinical implications, particularly in patients treated with heparin.
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