ArticleThe Journal of cell biology1994
Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C.
Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 230 citations in OpenAlex.
- Tenascin-C from the tissue microenvironment promotes muscle stem cell maintenance and function through Annexin A2.Communications biology · 2025Article
- Substrate-bound and soluble domains of tenascin-C regulate differentiation, proliferation and migration of neural stem and progenitor cells.Frontiers in cellular neuroscience · 2024Article
- Tenascin-C promotes bladder cancer progression and its action depends on syndecan-4 and involves NF-κB signaling activation.BMC cancer · 2022Article
- Tenascin-C fibronectin D domain is involved in the fine-tuning of glial response to CNS injuryFrontiers in cell and developmental biology · 2022Article
- The ANXA2/S100A10 Complex-Regulation of the Oncogenic Plasminogen Receptor.Biomolecules · 2021Review
- Elevated glucose alters global gene expression and tenascin-C alternative splicing in mesangial cells.Matrix biology plus · 2020Article
- Different Functions of Recombinantly Expressed Domains of Tenascin-C in Glial Scar Formation.Frontiers in immunology · 2020Article
- Signaling in the microenvironment of pancreatic cancer: Transmitting along the nerve.Pharmacology & therapeutics · 2019Review
- Hedgehog signaling stimulates Tenascin C to promote invasion of pancreatic ductal adenocarcinoma cells through Annexin A2.Cell adhesion & migration · 2017Article
- Integrative Modeling Reveals Annexin A2-mediated Epigenetic Control of Mesenchymal Glioblastoma.EBioMedicine · 2016Article
- Role of tenascins in the ECM of gliomas.Cell adhesion & migration · 2015Review
- Tenascin-C and integrins in cancer.Cell adhesion & migration · 2015Review
- Tenascin-C: Form versus function.Cell adhesion & migration · 2015Review
- Revisiting the matricellular concept.Matrix biology : journal of the International Society for Matrix Biology · 2014Review
- mTOR signal transduction pathways contribute to TN-C FNIII A1 overexpression by mechanical stress in osteosarcoma cells.Molecules and cells · 2014Article
- Dentin phosphoprotein binds annexin 2 and is involved in calcium transport in rat kidney ureteric bud cells.The Journal of biological chemistry · 2013Article
- Increased annexin A1 and A2 levels in bronchoalveolar lavage fluid are associated with resistance to respiratory disease in beef calves.Veterinary research · 2013Article
- Annexin A2: the importance of being redox sensitive.International journal of molecular sciences · 2013Article
- Annexin-phospholipid interactions. Functional implications.International journal of molecular sciences · 2013Article
- Dynamics and functional differences between dendroaspin and rhodostomin: insights into protein scaffolds in integrin recognition.Protein science : a publication of the Protein Society · 2012Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
We have investigated the binding of soluble tenascin-C (TN-C) to several cell lines using a radioligand binding assay. Specific binding was demonstrated to U-251MG human glioma cells and to a line of bovine aortic endothelial cells, but hamster fibroblasts showed no specific binding. Recombinant proteins corresponding to specific domains of TN-C were used to map the binding site(s) in TN-C. The alternatively spliced segment (TNfnA-D) inhibited the binding of native TN-C most strongly, and itself bound to glioma and endothelial cells. Scatchard analysis of TNfnA-D binding indicated 2-5 x 10(5) binding sites per cell, with an apparent 2 nM dissociation constant. The cell surface receptor for TNfnA-D was identified as a 35-kD protein on the basis of blot binding assays and affinity chromatography of membrane extracts on native TN-C and TNfnA-D columns. Protein sequencing indicated that this 35-kD receptor was annexin II. Annexin II is well characterized as a cytoplasmic protein, so it was surprising to find it as a presumably extracellular receptor for TN-C. To confirm that it was the 35-kD receptor, we obtained purified annexin II and demonstrated its binding to TNfnA-D and TN-C at nM concentrations. Antibodies to annexin II prominently stained the external surface of live endothelial cells and blocked the binding of TNfnA-D to the cells. Thus annexin II appears to be a receptor for the alternatively spliced segment of TN-C, and may mediate cellular responses to soluble TN-C in the extracellular matrix.
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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.