ArticleThe Journal of biological chemistry2011
Highly sulfated nonreducing end-derived heparan sulfate domains bind fibroblast growth factor-2 with high affinity and are enriched in biologically active fractions.
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 24 papers.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- Decoding the secretory blueprint of bone healing: from gradients to regeneration.Frontiers in cell and developmental biology · 2026Review
- Structure and unusual binding mechanism of the hyaluronan receptor LYVE-1 mediating leucocyte entry to lymphatics.Nature communications · 2025Article
- Specific Non-Reducing Ends in Heparins from Different Animal Origins: Building Blocks Analysis Using Reductive Amination Tagging by Sulfanilic Acid.Molecules (Basel, Switzerland) · 2020Article
- Characterization of Glycosaminoglycans in Gaping and Intact Connective Tissues of Farmed Atlantic Salmon (ACS omega · 2019Article
- Introduction to the Molecules Special Edition Entitled 'Molecules (Basel, Switzerland) · 2019Article
- A role for proteoglycans in vascular disease.Matrix biology : journal of the International Society for Matrix Biology · 2018Review
- Heparan Sulfate Domains Required for Fibroblast Growth Factor 1 and 2 Signaling through Fibroblast Growth Factor Receptor 1c.The Journal of biological chemistry · 2017Article
- Gas-Phase Analysis of the Complex of Fibroblast GrowthFactor 1 with Heparan Sulfate: A Traveling Wave Ion Mobility Spectrometry (TWIMS) and Molecular Modeling Study.Journal of the American Society for Mass Spectrometry · 2017Article
- Synthetic heparan sulfate dodecasaccharides reveal single sulfation site interconverts CXCL8 and CXCL12 chemokine biology.Chemical communications (Cambridge, England) · 2015Article
- Heparan sulfate and heparin interactions with proteins.Journal of the Royal Society, Interface · 2015Review
- Fell-Muir Lecture: Heparan sulphate and the art of cell regulation: a polymer chain conducts the protein orchestra.International journal of experimental pathology · 2015Article
- A liquid chromatography-mass spectrometry-based approach to characterize the substrate specificity of mammalian heparanase.The Journal of biological chemistry · 2014Article
- Transduction of extracellular cues into cell polarity: the role of the transmembrane proteoglycan NG2.Molecular neurobiology · 2014Review
- A computational framework for heparan sulfate sequencing using high-resolution tandem mass spectra.Molecular & cellular proteomics : MCP · 2014Article
- Deciphering the mechanism behind Fibroblast Growth Factor (FGF) induced biphasic signal-response profiles.Cell communication and signaling : CCS · 2014Article
- Fibroblast growth factor-based signaling through synthetic heparan sulfate blocks copolymers studied using high cell density three-dimensional cell printing.The Journal of biological chemistry · 2014Article
- Article
- Heparan sulfate-protein binding specificity.Biochemistry. Biokhimiia · 2013Review
- Glycosaminoglycan glycomics using mass spectrometry.Molecular & cellular proteomics : MCP · 2013Review
- Tandem mass spectrometry of heparan sulfate negative ions: sulfate loss patterns and chemical modification methods for improvement of product ion profiles.Journal of the American Society for Mass Spectrometry · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Human fibroblast growth factor-2 (FGF2) regulates cellular processes including proliferation, adhesion, motility, and angiogenesis. FGF2 exerts its biological function by binding and dimerizing its receptor (FGFR), which activates signal transduction cascades. Effective binding of FGF2 to its receptor requires the presence of heparan sulfate (HS), a linear polysaccharide with N-sulfated domains (NS) localized at the cell surface and extracellular matrix. HS acts as a platform facilitating the formation of a functional FGF-FGFR-HS ternary complex. Crystal structures of the signaling ternary complex revealed two conflicting architectures. In the asymmetrical model, two FGFs and two FGFRs bind a single HS chain. In contrast, the symmetrical model postulates that one FGF and one FGFR bind to the free end of the HS chain and dimerization require these ends to join, bringing the two half-complexes together. In this study, we screened a hexasaccharide HS library for compositions that are able to bind FGF2. The library was composed primarily of NS domains internal to the HS chain with minor presence of non-reducing end (NRE) NS. The binders were categorized into low versus high affinity binders. The low affinity fraction contained primarily hexasaccharides with low degree of sulfation that were internal to the HS chains. In contrast, the high affinity bound fraction was enriched in NRE oligosaccharides that were considerably more sulfated and had the ability to promote FGFR-mediated cell proliferation. The results suggest a role of the NRE of HS in FGF2 signaling and favor the formation of the symmetrical architecture on short NS domains.
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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.