ArticleThe Journal of biological chemistry2014
Fibroblast growth factor-based signaling through synthetic heparan sulfate blocks copolymers studied using high cell density three-dimensional cell printing.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 27 citations in OpenAlex.
- Structure and unusual binding mechanism of the hyaluronan receptor LYVE-1 mediating leucocyte entry to lymphatics.Nature communications · 2025Article
- Regional and disease-specific glycosaminoglycan composition and function in decellularized human lung extracellular matrix.Acta biomaterialia · 2023Article
- Glycosaminoglycans: What Remains To Be Deciphered?JACS Au · 2023Review
- Extracellular matrix dynamics: tracking in biological systems and their implications.Journal of biological engineering · 2022Review
- Advances in the preparation and synthesis of heparin and related products.Drug discovery today · 2020Review
- Potential Use of Anti-Inflammatory Synthetic Heparan Sulfate to Attenuate Liver Damage.Biomedicines · 2020Review
- Functional role of glycosaminoglycans in decellularized lung extracellular matrix.Acta biomaterialia · 2020Article
- Article
- Biomolecules Turn Self-Assembling Amphiphilic Block Co-polymer Platforms Into Biomimetic Interfaces.Frontiers in chemistry · 2018Review
- Engineered heparins as new anticoagulant drugs.Bioengineering & translational medicine · 2017Review
- Heparan Sulfate Domains Required for Fibroblast Growth Factor 1 and 2 Signaling through Fibroblast Growth Factor Receptor 1c.The Journal of biological chemistry · 2017Article
- Glycosaminoglycan-Based Biohybrid Hydrogels: A Sweet and Smart Choice for Multifunctional Biomaterials.Advanced materials (Deerfield Beach, Fla.) · 2016Review
- 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
- Sources, metabolism, and regulation of circulating sphingosine-1-phosphate.Journal of lipid research · 2015Review
- Can we produce heparin/heparan sulfate biomimetics using "mother-nature" as the gold standard?Molecules (Basel, Switzerland) · 2015Review
- Interactions of signaling proteins, growth factors and other proteins with heparan sulfate: mechanisms and mysteries.Connective tissue research · 2015Review
- Chemoenzymatic synthesis of heparan sulfate and heparin.Natural product reports · 2014Review
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
Four well-defined heparan sulfate (HS) block copolymers containing S-domains (high sulfo group content) placed adjacent to N-domains (low sulfo group content) were chemoenzymatically synthesized and characterized. The domain lengths in these HS block co-polymers were ~40 saccharide units. Microtiter 96-well and three-dimensional cell-based microarray assays utilizing murine immortalized bone marrow (BaF3) cells were developed to evaluate the activity of these HS block co-polymers. Each recombinant BaF3 cell line expresses only a single type of fibroblast growth factor receptor (FGFR) but produces neither HS nor fibroblast growth factors (FGFs). In the presence of different FGFs, BaF3 cell proliferation showed clear differences for the four HS block co-polymers examined. These data were used to examine the two proposed signaling models, the symmetric FGF2-HS2-FGFR2 ternary complex model and the asymmetric FGF2-HS1-FGFR2 ternary complex model. In the symmetric FGF2-HS2-FGFR2 model, two acidic HS chains bind in a basic canyon located on the top face of the FGF2-FGFR2 protein complex. In this model the S-domains at the non-reducing ends of the two HS proteoglycan chains are proposed to interact with the FGF2-FGFR2 protein complex. In contrast, in the asymmetric FGF2-HS1-FGFR2 model, a single HS chain interacts with the FGF2-FGFR2 protein complex through a single S-domain that can be located at any position within an HS chain. Our data comparing a series of synthetically prepared HS block copolymers support a preference for the symmetric FGF2-HS2-FGFR2 ternary complex model.
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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.