ArticleThe Journal of biological chemistry2011
Heparan sulfate is essential for high mobility group protein 1 (HMGB1) signaling by the receptor for advanced glycation end products (RAGE).
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 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
56 citing papers in PubMed, 87 citations in OpenAlex.
- HMGB1-Platelet Interactions: Mechanisms and Targeted Therapy Strategies.Thrombosis and haemostasis · 2026Review
- The non-scaffold effects of natural polysaccharides in promoting organ regeneration: a review.Journal of biological engineering · 2026Review
- Multimodal Profiling Reveals Distinct Endothelial Activation Pathways Regulated by Flow and Heparan Sulfate.Cellular and molecular bioengineering · 2026Article
- Dendritic Polyglycerol Sulfate Reduces Inflammation Through Inhibition of the HMGB1/RAGE Axis in RAW 264.7 Macrophages.International journal of molecular sciences · 2025Article
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- RAGE engagement by SARS-CoV-2 enables monocyte infection and underlies COVID-19 severity.Cell reports. Medicine · 2023Article
- Using heparan sulfate octadecasaccharide (18-mer) as a multi-target agent to protect against sepsis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Glycosaminoglycan Analysis: Purification, Structural Profiling, and GAG-Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Targeting heparan sulfate-protein interactions with oligosaccharides and monoclonal antibodies.Frontiers in molecular biosciences · 2023Review
- Heparan sulfates and heparan sulfate binding proteins in sepsis.Frontiers in molecular biosciences · 2023Review
- Necrotic reshaping of the glioma microenvironment drives disease progression.Acta neuropathologica · 2022Review
- Heparin-Functionalized Adsorbents Eliminate Central Effectors of Immunothrombosis, including Platelet Factor 4, High-Mobility Group Box 1 Protein and Histones.International journal of molecular sciences · 2022Article
- Scavenger receptors in host defense: from functional aspects to mode of action.Cell communication and signaling : CCS · 2022Review
- Activated Platelets and Platelet-Derived Extracellular Vesicles Mediate COVID-19-Associated Immunothrombosis.Frontiers in cell and developmental biology · 2022Review
- A potential new pathway for heparin treatment of sepsis-induced lung injury: inhibition of pulmonary endothelial cell pyroptosis by blocking hMGB1-LPS-induced caspase-11 activation.Frontiers in cellular and infection microbiology · 2022Review
- The Heparanase Regulatory Network in Health and Disease.International journal of molecular sciences · 2021Review
- Role Played by Receptors for Advanced Glycosylation End Products in Corneal Endothelial Cells after HSV-1 Infection.International journal of molecular sciences · 2021Article
- Sialoglycan recognition is a common connection linking acidosis, zinc, and HMGB1 in sepsis.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A Systems View of the Heparan Sulfate Interactome.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2021Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In a proteomic search for heparan sulfate-binding proteins on monocytes, we identified HMGB1 (high mobility group protein B1). The extracellular role of HMGB1 as a cytokine has been studied intensively and shown to be important as a danger-associated molecular pattern protein. Here, we report that the activity of HMGB1 depends on heparan sulfate. Binding and competition studies demonstrate that HMGB1 interacts with CHO and endothelial cell heparan sulfate. By site-directed mutagenesis, we identified a loop region that connects the A-box and B-box domains of HMGB1 as responsible for heparan sulfate binding. HMGB1-induced Erk1/2 and p38 phosphorylation is abolished when endothelial heparan sulfate is removed or blocked pharmacologically, resulting in decreased HMGB1-induced endothelial sprouting. However, mutated HMGB1 that lacks the heparan sulfate-binding site retained its signaling activity. We show the major receptor for HMGB1, receptor for advanced glycation end products (RAGE), also binds to heparan sulfate and that RAGE and heparan sulfate forms a complex. Our data establishes that the functional receptor for HMGB1 consists of a complex of RAGE and cell surface heparan sulfate.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.