ArticleThe Journal of biological chemistry2012
Mapping of potent and specific binding motifs, GLOGEN and GVOGEA, for integrin α1β1 using collagen toolkits II and III.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 73 citations in OpenAlex.
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- Diffusion model assisted designing self-assembling collagen mimetic peptides as biocompatible materials.Briefings in bioinformatics · 2024Article
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- Injectable, Drug-Eluting Nanocrystals Prevent Fibrosis and Stricture Formation In Vivo.Gastroenterology · 2023Article
- The Interplay between Integrins and Immune Cells as a Regulator in Cancer Immunology.International journal of molecular sciences · 2023Review
- Targeting integrin pathways: mechanisms and advances in therapy.Signal transduction and targeted therapy · 2023Review
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- Adjusting the physico-chemical properties of collagen scaffolds to accommodate primary osteoblasts and endothelial cells.Regenerative biomaterials · 2023Article
- Assessing a computational pipeline to identify binding motifs to theFrontiers in chemistry · 2023Article
- The interplay of fibroblasts, the extracellular matrix, and inflammation in scar formation.The Journal of biological chemistry · 2022Review
- Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022Review
- Selectivity of the collagen-binding integrin inhibitors, TC-I-15 and obtustatin.Toxicology and applied pharmacology · 2021Article
- Identification of HSP47 Binding Site on Native Collagen and Its Implications for the Development of HSP47 Inhibitors.Biomolecules · 2021Article
- Integrin α11β1 is a receptor for collagen XIII.Cell and tissue research · 2021Article
- Multimerin 1 supports platelet function in vivo and binds to specific GPAGPOGPX motifs in fibrillar collagens that enhance platelet adhesion.Journal of thrombosis and haemostasis : JTH · 2021Article
- Can the SARS-CoV-2 Spike Protein Bind Integrins Independent of the RGD Sequence?Frontiers in cellular and infection microbiology · 2021Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Integrins are well characterized cell surface receptors for extracellular matrix proteins. Mapping integrin-binding sites within the fibrillar collagens identified GFOGER as a high affinity site recognized by α2β1, but with lower affinity for α1β1. Here, to identify specific ligands for α1β1, we examined binding of the recombinant human α1 I domain, the rat pheochromocytoma cell line (PC12), and the rat glioma Rugli cell line to our collagen Toolkit II and III peptides using solid-phase and real-time label-free adhesion assays. We observed Mg(2+)-dependent binding of the α1 I domain to the peptides in the following rank order: III-7 (GLOGEN), II-28 (GFOGER), II-7 and II-8 (GLOGER), II-18 (GAOGER), III-4 (GROGER). PC12 cells showed a similar profile. Using antibody blockade, we confirmed that binding of PC12 cells to peptide III-7 was mediated by integrin α1β1. We also identified a new α1β1-binding activity within peptide II-27. The sequence GVOGEA bound weakly to PC12 cells and strongly to activated Rugli cells or to an activated α1 I domain, but not to the α2 I domain or to C2C12 cells expressing α2β1 or α11β1. Thus, GVOGEA is specific for α1β1. Although recognized by both α2β1 and α11β1, GLOGEN is a better ligand for α1β1 compared with GFOGER. Finally, using biosensor assays, we show that although GLOGEN is able to compete for the α1 I domain from collagen IV (IC(50) ∼3 μm), GFOGER is much less potent (IC(50) ∼90 μm), as shown previously. These data confirm the selectivity of GFOGER for α2β1 and establish GLOGEN as a high affinity site for α1β1.
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Registered trials
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