ArticleThe Journal of cell biology1995
The L1 adhesion molecule is a cellular ligand for VLA-5.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 146 citations in OpenAlex.
- Tumor Invasive Border Index (TIBI) in colorectal cancer: linking infiltrative morphology to molecular insights.The Journal of pathology · 2026Article
- The emerging role of human transmembrane RGD-based counter-receptors of integrins in health and disease.Cellular & molecular biology letters · 2025Review
- Microfluidic-Assisted Production of Gastro-Resistant Active-Targeted Diatomite Nanoparticles for the Local Release of Galunisertib in Metastatic Colorectal Cancer Cells.Advanced healthcare materials · 2023Article
- A fragment of cell adhesion molecule L1 reduces amyloid-β plaques in a mouse model of Alzheimer's disease.Cell death & disease · 2022Article
- Thyroid hormone-dependent oligodendroglial cell lineage genomic and non-genomic signaling through integrin receptors.Frontiers in pharmacology · 2022Review
- Case Report: Two NovelFrontiers in genetics · 2022Article
- Schwann cell interactions during the development of the peripheral nervous system.Developmental neurobiology · 2021Review
- Impact of Nischarin on EMT regulators in breast cancer cell lines.Oncology letters · 2020Article
- The functional role of integrins during intra- and extravasation within the metastatic cascade.Molecular cancer · 2019Review
- Integrin α5β1 expression on dopaminergic neurons is involved in dopaminergic neurite outgrowth on striatal neurons.Scientific reports · 2017Article
- Small-molecule inhibitors of FGFR, integrins and FAK selectively decrease L1CAM-stimulated glioblastoma cell motility and proliferation.Cellular oncology (Dordrecht, Netherlands) · 2016Article
- Overcoming barriers and thresholds - signaling of oligomeric Aβ through the prion protein to Fyn.Molecular neurodegeneration · 2013Review
- A phylogenetic analysis of the L1 family of neural cell adhesion molecules.Neurochemical research · 2013Article
- Influence of L1-CAM expression of breast cancer cells on adhesion to endothelial cells.Journal of cancer research and clinical oncology · 2013Article
- Downregulation of L1 perturbs neuronal migration and alters the expression of transcription factors in murine neocortex.Journal of neuroscience research · 2013Article
- L1 stimulation of human glioma cell motility correlates with FAK activation.Journal of neuro-oncology · 2011Article
- Integrins are necessary for the development and maintenance of the glial layers in the Drosophila peripheral nerve.Development (Cambridge, England) · 2011Article
- Review
- Circulating levels of cell adhesion molecule L1 as a prognostic marker in gastrointestinal stromal tumor patients.BMC cancer · 2011Article
- Perinatal asphyxia: current status and approaches towards neuroprotective strategies, with focus on sentinel proteins.Neurotoxicity research · 2011Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The L1 adhesion molecule is a member of the immunoglobulin superfamily shared by neural and immune cells. In the nervous system L1 can mediate cell binding by a homophilic mechanism. To analyze its function on leukocytes we studied whether L1 could interact with integrins. Here we demonstrate that VLA-5, an RGD-specific fibronectin receptor on a wide variety of cell types, can bind to murine L1. Mouse ESb-MP cells expressing VLA-5 and L1 could be induced to aggregate in the presence of specific mAbs to CD24 (heat-stable antigen), a highly and heterogeneously glycosylated glycophosphatidylinositol-linked differentiation antigen of hematopoietic and neural cells. The aggregation was blocked by both mAbs to L1 and VLA-5, respectively. Aggregation was blocked also by a synthetic RGD-containing peptide derived from the Ig-domain VI of the L1 protein. ESb-MP subclones with low L1 expression could not aggregate. In heterotypic binding assays mouse bone marrow cells could adhere in an L1-dependent fashion to platelets that expressed VLA-5. Also purified L1 coated to polystyrene beads could bind to platelets. The binding of L1-beads was again inhibited by mAbs to L1 and VLA-5, by soluble L1 and the L1-RGD peptide in a dose-dependent manner. Thymocytes or human Nalm-6 tumor cells expressing VLA-5 could adhere to affinity-purified L1 and to the L1-derived RGD-containing peptide coated to glass slides. The adhesion was strongly enhanced in the presence of Mn(2+)-ions and blocked by mAbs to VLA-5. We also demonstrate a direct L1-VLA-5 protein interaction. Our results suggest a novel binding pathway, in which the VLA-5 integrin binds to L1 on adjacent cells. Given its rapid downregulation on lymphocytes after induction of cell proliferation, L1 may be important in integrin-mediated and activation-regulated cell-cell interactions.
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