ArticleThe Biochemical journal1998
Regulation of integrin function: evidence that bivalent-cation-induced conformational changes lead to the unmasking of ligand-binding sites within integrin alpha5 beta1.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 100 citations in OpenAlex.
- Magnesium Deficiency and Cardiometabolic Disease.Nutrients · 2023Review
- The βI domain promotes active β1 integrin clustering into mature adhesion sites.Life science alliance · 2023Article
- Sequential activation of M1 and M2 phenotypes in macrophages by Mg degradation from Ti-Mg alloy for enhanced osteogenesis.Biomaterials research · 2022Article
- Cell surface integrin α5ß1 clustering negatively regulates receptor tyrosine kinase signaling in colorectal cancer cells via glycogen synthase kinase 3.Integrative biology : quantitative biosciences from nano to macro · 2021Article
- Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells.International journal of molecular sciences · 2021Article
- The role of integrins in inflammation and angiogenesis.Pediatric research · 2021Review
- The Ric-8A/Gα13/FAK signalling cascade controls focal adhesion formation during neural crest cell migration inDevelopment (Cambridge, England) · 2018Article
- Ligand-induced Epitope Masking: DISSOCIATION OF INTEGRIN α5β1-FIBRONECTIN COMPLEXES ONLY BY MONOCLONAL ANTIBODIES WITH AN ALLOSTERIC MODE OF ACTION.The Journal of biological chemistry · 2016Article
- Relating conformation to function in integrin α5β1.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Epitopes in α8β1 and other RGD-binding integrins delineate classes of integrin-blocking antibodies and major binding loops in α subunits.Scientific reports · 2015Article
- Characterization of Endothelial Progenitor Cell Interactions with Human Tropoelastin.PloS one · 2015Article
- A D-amino acid containing peptide as a potent, noncovalent inhibitor of α5β1 integrin in human prostate cancer invasion and lung colonization.Clinical & experimental metastasis · 2014Article
- Talin and kindlin: the one-two punch in integrin activation.Frontiers of medicine · 2014Review
- Perlecan domain V inhibits amyloid-β induced brain endothelial cell toxicity and restores angiogenic function.Journal of Alzheimer's disease : JAD · 2014Article
- Divalent cations regulate the folding and activation status of integrins during their intracellular trafficking.Journal of cell science · 2011Article
- Heparin II domain of fibronectin mediates contractility through an alpha4beta1 co-signaling pathway.Experimental cell research · 2010Article
- Calcium-actin waves and oscillations of cellular membranes.Biophysical journal · 2009Article
- Clustering of syndecan-4 and integrin beta1 by laminin alpha 3 chain-derived peptide promotes keratinocyte migration.Molecular biology of the cell · 2009Article
- Therapeutic ultrasound bypasses canonical syndecan-4 signaling to activate rac1.The Journal of biological chemistry · 2009Article
- Cooperation between integrin alphavbeta3 and VEGFR2 in angiogenesis.Angiogenesis · 2009Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The molecular mechanisms that regulate integrin-ligand binding are unknown; however, bivalent cations are essential for integrin activity. According to recent models of integrin tertiary structure, sites involved in ligand recognition are located on the upper face of the seven-bladed beta-propeller formed by the N-terminal repeats of the alpha subunit and on the von Willebrand factor A-domain-like region of the beta subunit. The epitopes of function-altering monoclonal antibodies (mAbs) cluster in these regions of the alpha and beta subunits; hence these mAbs can be used as probes to detect changes in the exposure or shape of the ligand-binding sites. Bivalent cations were found to alter the apparent affinity of binding of the inhibitory anti-alpha5 mAbs JBS5 and 16, the inhibitory anti-beta1 mAb 13, and the stimulatory anti-beta1 mAb 12G10 to alpha5 beta1. Analysis of the binding of these mAbs to alpha5beta1 over a range of Mn2+, Mg2+ or Ca2+ concentrations demonstrated that there was a concordance between the ability of cations to elicit conformational changes and the ligand-binding potential of alpha5 beta1. Competitive ELISA experiments provided evidence that the domains of the alpha5 and beta1 subunits recognized by mAbs JBS5/16 and 13/12G10 are spatially close, and that the distance between these two domains is increased when alpha5 beta1 is occupied by bivalent cations. Taken together, our findings suggest that bivalent cations induce a conformational relaxation in the integrin that results in exposure of ligand-binding sites, and that these sites lie near an interface between the alpha subunit beta-propeller and the beta subunit putative A-domain.
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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.