ArticleThe Journal of biological chemistry2012
Polydom/SVEP1 is a ligand for integrin α9β1.
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 53 papers.
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Who cites it
53 citing papers in PubMed, 86 citations in OpenAlex.
- Svep1 orchestrates distal airway patterning and alveolar differentiation in murine lung development.eLife · 2026Article
- A novel microprotein L3EMP triggers lung adenocarcinoma progression by catalysing the deubiquitination of SIRT1.British journal of cancer · 2026Article
- Sushi, von Willebrand Factor Type A, EGF and Pentraxin Domain-Containing Protein 1: A Novel Fibroblast-Derived Circulating Biomarker Reflecting Cardiac Fibrosis.Journal of the American Heart Association · 2026Article
- Novel Plasma Proteomic Markers and Risk of Venous Thromboembolism.Circulation · 2026Article
- Integrin α4 and α9 in trabecular meshwork and Schlemm's canal function: emerging regulators of intraocular pressure homeostasis.Frontiers in cell and developmental biology · 2026Review
- Low SVEP1 in intrahepatic cholangiocarcinoma mediates phenotype switching-driven metastasis by Jag2/Notch1/Hes5.Cell death & disease · 2025Article
- Piezo1 Activates an Autocrine Angiopoietin-2-Integrin Signaling Loop in Schlemm's Canal to Regulate Intraocular Pressure.bioRxiv : the preprint server for biology · 2025Article
- Article
- Chemical Synthesis of NICOL, A Coligand Secreted Protein Mediating Mammalian Male Reproductive Tract Trans-luminal Signaling.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Deep plasma and tissue proteome profiling of knockout mice reveals pathways associated withJournal of molecular and cellular cardiology plus · 2025Article
- Integrating plasma proteomics and genome-wide association data to identify therapeutic targets for retinal neurodegenerative diseases in Europeans.International journal of ophthalmology · 2025Article
- Article
- EGR1 transcriptionally regulates SVEP1 to promote proliferation and migration in human coronary artery smooth muscle cells.Molecular biology reports · 2024Article
- Proteomic Associations of NT-proBNP (N-Terminal Pro-B-Type Natriuretic Peptide) in Heart Failure With Preserved Ejection Fraction.Circulation. Heart failure · 2024Article
- Extracellular matrix molecules associated with lymphatic vessels in health and disease.Histology and histopathology · 2024Review
- Article
- The emerging Janus face of SVEP1 in development and disease.Trends in molecular medicine · 2023Review
- Polydom/SVEP1 binds to Tie1 and promotes migration of lymphatic endothelial cells.The Journal of cell biology · 2023Article
- Article
- SVEP1 is an endogenous ligand for the orphan receptor PEAR1.Nature communications · 2023Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A variety of proteins, including tenascin-C and osteopontin, have been identified as ligands for integrin α9β1. However, their affinities for integrin α9β1 are apparently much lower than those of other integrins (e.g. α3β1, α5β1, and α8β1) for their specific ligands, leaving the possibility that physiological ligands for integrin α9β1 still remain unidentified. In this study, we found that polydom (also named SVEP1) mediates cell adhesion in an integrin α9β1-dependent manner and binds directly to recombinant integrin α9β1 with an affinity that far exceeds those of the known ligands. Using a series of recombinant polydom proteins with N-terminal deletions, we mapped the integrin-binding site to the 21st complement control protein domain. Alanine-scanning mutagenesis revealed that the EDDMMEVPY sequence (amino acids 2636-2644) in the 21st complement control protein domain was involved in the binding to integrin α9β1 and that Glu(2641) was the critical acidic residue for the integrin binding. The importance of this sequence was further confirmed by integrin binding inhibition assays using synthetic peptides. Immunohistochemical analyses of mouse embryonic tissues showed that polydom colocalized with integrin α9 in the stomach, intestine, and other organs. Furthermore, in situ integrin α9β1 binding assays using frozen mouse tissues showed that polydom accounts for most, but not all, of the integrin α9β1 ligands in tissues. Taken together, the present findings indicate that polydom is a hitherto unknown ligand for integrin α9β1 that functions as a physiological ligand in vivo.
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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.