ArticleJournal of cell science2010
The heparin-binding domain of HB-EGF mediates localization to sites of cell-cell contact and prevents HB-EGF proteolytic release.
Article in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 46 citations in OpenAlex.
- Heparan sulfate regulates amphiregulin programming of tissue reparative lung mesenchymal cells during influenza A virus infection in mice.Nature communications · 2025Article
- Low-affinity ligands of the epidermal growth factor receptor are long-range signal transmitters in collective cell migration of epithelial cells.Cell reports · 2024Article
- Evaluation of the Recombinant Bacterial Chitinases as Anti-proliferative and Anti-migratory Agents for the Human Breast Cancer Cell Line, MCF-7.Applied biochemistry and biotechnology · 2024Article
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- Redundant roles of EGFR ligands in the ERK activation waves during collective cell migration.Life science alliance · 2022Article
- Syndecan-3 contributes to the regulation of the microenvironment at the node of Ranvier following end-to‑side neurorrhaphy: sodium image analysis.Histochemistry and cell biology · 2021Article
- Article
- Glycosaminoglycan-based biomaterials for growth factor and cytokine delivery: Making the right choices.Journal of controlled release : official journal of the Controlled Release Society · 2019Review
- Heparin-Binding Epidermal Growth Factor-Like Growth Factor as a Critical Mediator of Tissue Repair and Regeneration.The American journal of pathology · 2018Review
- EGFR activation triggers cellular hypertrophy and lysosomal disease in NAGLU-depleted cardiomyoblasts, mimicking the hallmarks of mucopolysaccharidosis IIIB.Cell death & disease · 2018Article
- Recombinant Heparin-New Opportunities.Frontiers in medicine · 2018Review
- Heparin: Effects upon the Glycocalyx and Endothelial Cells.The journal of extra-corporeal technology · 2017Review
- Article
- Article
- Probing the impact of GFP tagging on Robo1-heparin interaction.Glycoconjugate journal · 2014Article
- Trafficking of the EGFR ligand Spitz regulates its signaling activity in polarized tissues.Journal of cell science · 2013Article
- Heparin and related drugs: beyond anticoagulant activity.ISRN pharmacology · 2013Article
- The SULFs, extracellular sulfatases for heparan sulfate, promote the migration of corneal epithelial cells during wound repair.PloS one · 2013Article
- YKL-40 acts as an angiogenic factor to promote tumor angiogenesis.Frontiers in physiology · 2013Article
- Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Heparin-binding EGF-like growth factor (HB-EGF) is a ligand for EGF receptor (EGFR) and possesses the ability to signal in juxtacrine, autocrine and/or paracrine mode, with these alternatives being governed by the degree of proteolytic release of the ligand. Although the spatial range of diffusion of released HB-EGF is restricted by binding heparan-sulfate proteoglycans (HSPGs) in the extracellular matrix and/or cellular glycocalyx, ascertaining mechanisms governing non-released HB-EGF localization is also important for understanding its effects. We have employed a new method for independently tracking the localization of the extracellular EGF-like domain of HB-EGF and the cytoplasmic C-terminus. A striking observation was the absence of the HB-EGF transmembrane pro-form from the leading edge of COS-7 cells in a wound-closure assay; instead, this protein localized in regions of cell-cell contact. A battery of detailed experiments found that this localization derives from a trans interaction between extracellular HSPGs and the HB-EGF heparin-binding domain, and that disruption of this interaction leads to increased release of soluble ligand and a switch in cell phenotype from juxtacrine-induced growth inhibition to autocrine-induced proliferation. Our results indicate that extracellular HSPGs serve to sequester the transmembrane pro-form of HB-EGF at the point of cell-cell contact, and that this plays a role in governing the balance between juxtacrine versus autocrine and paracrine signaling.
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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.