ArticleMatrix biology : journal of the International Society for Matrix Biology2018
Heparin-fibronectin interactions in the development of extracellular matrix insolubility.
Article in Matrix biology : journal of the International Society for Matrix Biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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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
19 citing papers in PubMed.
- Using Low-Speed Rotation in Heparin Immobilization Improved Antithrombogenicity of Tubular Acellular Vascular Scaffolds.Tissue engineering and regenerative medicine · 2026Article
- Article
- Fibronectin matrix assembly at a glance.Journal of cell science · 2025Review
- Increased basal fibronectin is sufficient to promote excess endothelial cell matrix assembly causing localized barrier dysfunction.Molecular biology of the cell · 2024Article
- Peptide location fingerprinting identifies structural alterations within basement membrane components in ageing kidney.Matrix biology : journal of the International Society for Matrix Biology · 2023Article
- Sulfated motifs in heparan sulfate inhibitProteoglycan research · 2023Article
- Heparin Mimetics and Their Impact on Extracellular Matrix Protein Assemblies.Pharmaceuticals (Basel, Switzerland) · 2023Article
- A new mechanism of fibronectin fibril assembly revealed by live imaging and super-resolution microscopy.Journal of cell science · 2022Article
- Coreceptor functions of cell surface heparan sulfate proteoglycans.American journal of physiology. Cell physiology · 2022Review
- Differential Regulation of Neurite Outgrowth and Growth Cone Morphology by 3D Fibronectin and Fibronectin-Collagen Extracellular Matrices.Molecular neurobiology · 2022Article
- Heparan sulfate is necessary for the early formation of nascent fibronectin and collagen I fibrils at matrix assembly sites.The Journal of biological chemistry · 2022Article
- Engineered ECM models: Opportunities to advance understanding of tumor heterogeneity.Current opinion in cell biology · 2021Review
- Engineering of Bio-Adhesive Ligand Containing Recombinant RGD and PHSRN Fibronectin Cell-Binding Domains in Fusion with a Colored Multi Affinity Tag: Simple Approach for Fragment Study from Expression to Adsorption.International journal of molecular sciences · 2021Article
- Spatially controlled glycocalyx engineering for growth factor patterning in embryoid bodies.Biomaterials science · 2021Article
- Article
- Elevated glucose alters global gene expression and tenascin-C alternative splicing in mesangial cells.Matrix biology plus · 2020Article
- Interaction with the host: the role of fibronectin and extracellular matrix proteins in the adhesion of Gram-negative bacteria.Medical microbiology and immunology · 2020Review
- Distinct Binding Interactions of αBiophysical journal · 2019Article
- Fibronectin matrix as a scaffold for procollagen proteinase binding and collagen processing.Molecular biology of the cell · 2019Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
During extracellular matrix (ECM) assembly, fibronectin (FN) fibrils are irreversibly converted into a detergent-insoluble form which, through FN's multi-domain structure, can interact with collagens, matricellular proteins, and growth factors to build a definitive matrix. FN also has heparin/heparan sulfate (HS) binding sites. Using HS-deficient CHO cells, we show that the addition of soluble heparin significantly increased the amount of FN matrix that these cells assemble. Sulfated HS glycosaminoglycan (GAG) mimetics similarly increased FN assembly and demonstrated a dependence on GAG sulfation. The length of the heparin chains also plays a role in assembly. Chains of sufficient length to bind to two FN molecules gave maximal stimulation of assembly whereas shorter heparin had less of an effect. Using a decellularized fibroblast matrix for proteolysis, detergent fractionation, and mass spectrometry, we found that the predominant domain within insoluble fibril fragments is FN's major heparin-binding domain HepII (modules III
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