ArticleThe Journal of biological chemistry2015
Integrin α3β1 Binding to Fibronectin Is Dependent on the Ninth Type III Repeat.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.
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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
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.
- Effect of tumor microenvironment on pathogenesis of the head and neck squamous cell carcinoma: a systematic review.Molecular cancer · 2019Pooled it
- SPR interaction analysis of GM3 glycan with the integrin α5β1 head domain.Glycoconjugate journal · 2026Article
- Multiple ways to promote adult grass carp (Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2025Article
- Strain-dependent glutathionylation of fibronectin fibers impacts mechano-chemical behavior and primes an integrin switch.Nature communications · 2024Article
- LAMC2 is a potential prognostic biomarker for cholangiocarcinoma.Oncology letters · 2023Article
- Extracellular matrix regulates force transduction at VE-cadherin junctions.Molecular biology of the cell · 2022Article
- Recurrence of Papillary Thyroid Cancer: A Systematic Appraisal of Risk Factors.The Journal of clinical endocrinology and metabolism · 2022Article
- Receptor binding domain of SARS-CoV-2 is a functional αv-integrin agonist.bioRxiv : the preprint server for biology · 2022Article
- Key concepts in muscle regeneration: muscle "cellular ecology" integrates a gestalt of cellular cross-talk, motility, and activity to remodel structure and restore function.European journal of applied physiology · 2022Review
- Tissue factor potentiates adherence of breast cancer cells to human umbilical vein endothelial cells under static and flow conditions.Cell adhesion & migration · 2021Article
- Design and Evaluation of a Polypeptide that Mimics the Integrin Binding Site for EDA Fibronectin to Block Profibrotic Cell Activity.International journal of molecular sciences · 2021Article
- Article
- Fibronectin 1 activates WNT/β-catenin signaling to induce osteogenic differentiation via integrin β1 interaction.Laboratory investigation; a journal of technical methods and pathology · 2020Article
- Review of Integrin-Targeting Biomaterials in Tissue Engineering.Advanced healthcare materials · 2020Review
- Interactions at engineered graft-tissue interfaces: A review.APL bioengineering · 2020Review
- Engineering PEG-based hydrogels to foster efficient endothelial network formation in free-swelling and confined microenvironments.Biomaterials · 2020Article
- Article
- Targeting the Immune Microenvironment in the Treatment of Head and Neck Squamous Cell Carcinoma.Frontiers in oncology · 2019Review
- Material Strategies for Modulating Epithelial to Mesenchymal Transitions.ACS biomaterials science & engineering · 2018Article
- Hydrogels with precisely controlled integrin activation dictate vascular patterning and permeability.Nature materials · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
Fibronectin (Fn) is a promiscuous ligand for numerous cell adhesion receptors or integrins. The vast majority of Fn-integrin interactions are mediated through the Fn Arg-Gly-Asp (RGD) motif located within the tenth type III repeat. In the case of integrins αIIbβ3 and α5β1, the integrin binds RGD and the synergy site (PHSRN) located within the adjacent ninth type III repeat. Prior work has shown that these synergy-dependent integrins are exquisitely sensitive to perturbations in the Fn integrin binding domain conformation. Our own prior studies of epithelial cell responses to recombinant fragments of the Fn integrin binding domain led us to hypothesize that integrin α3β1 binding may also be modulated by the synergy site. To explore this hypothesis, we created a variety of recombinant variants of the Fn integrin binding domain: (i) a previously reported (Leu → Pro) stabilizing mutant (FnIII9'10), (ii) an Arg to Ala synergy site mutation (FnIII9(R)→(A)10), (iii) a two-Gly (FnIII9(2G)10) insertion, and (iv) a four-Gly (FNIII9(4G)10) insertion in the interdomain linker region and used surface plasmon resonance to determine binding kinetics of integrin α3β1 to the Fn fragments. Integrin α3β1 had the highest affinity for FnIII9'10 and FnIII9(2G)10. Mutation within the synergy site decreased integrin α3β1 binding 17-fold, and the four-Gly insertion decreased binding 39-fold compared with FnIII9'10. Cell attachment studies demonstrate that α3β1-mediated epithelial cell binding is greater on FnIII9'10 compared with the other fragments. These studies suggest that the presence and spacing of the RGD and synergy sites modulate integrin α3β1 binding to Fn.
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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.