ArticleThe Journal of biological chemistry2008
Basigin-2 is a cell surface receptor for soluble basigin ligand.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed.
- TCGA-Informed Spatial Profiling Reveals Peripheral CD147 Expression at the Invasive Tumor Front as a Prognostic Indicator in OSCC.International journal of molecular sciences · 2026Article
- Human placental trophoblast cells express and secrete basigin via a regulated process of extracellular vesicle release.Reproduction (Cambridge, England) · 2025Article
- Metabolic Function and Therapeutic Potential of CD147 for Hematological Malignancies: An Overview.International journal of molecular sciences · 2024Review
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- ADAM12-Generated Basigin Ectodomain Binds β1 Integrin and Enhances the Expression of Cancer-Related Extracellular Matrix Proteins.International journal of molecular sciences · 2024Article
- Exploring monocarboxylate transporter inhibition for cancer treatment.Exploration of targeted anti-tumor therapy · 2024Review
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- Hepatocellular carcinoma cell-derived small extracellular vesicle-associated CD147 serves as a diagnostic marker and promotes endothelial cell angiogenesis via the PI3K/Akt pathway.Extracellular vesicles and circulating nucleic acids · 2023Article
- Basigin is necessary for normal decidualization of human uterine stromal cells.Human reproduction (Oxford, England) · 2022Article
- Epigenetic underpinnings of inflammation: Connecting the dots between pulmonary diseases, lung cancer and COVID-19.Seminars in cancer biology · 2022Review
- Matrix Metalloproteinases and Their Inhibitors in Pulmonary Fibrosis: EMMPRIN/CD147 Comes into Play.International journal of molecular sciences · 2022Review
- Mini-Review: Can the Metastatic Cascade Be Inhibited by Targeting CD147/EMMPRIN to Prevent Tumor Recurrence?Frontiers in immunology · 2022Review
- Role of MMP-2 and CD147 in kidney fibrosis.Open life sciences · 2022Review
- Extracellular matrix metalloproteinase inducer in brain ischemia and intracerebral hemorrhage.Frontiers in immunology · 2022Review
- CD147 deficiency is associated with impairedsperm motility/acrosome reaction and offersa therapeutic target for asthenozoospermia.Molecular therapy. Nucleic acids · 2021Article
- High Glucose and Advanced Glycation End Products Induce CD147-Mediated MMP Activity in Human Adipocytes.Cells · 2021Article
- Inducing regulated necrosis and shifting macrophage polarization with anti-EMMPRIN antibody (161-pAb) and complement factors.Journal of leukocyte biology · 2021Article
- The Immunoglobulin Superfamily Member Basigin Is Required for Complex Dendrite Formation inFrontiers in cellular neuroscience · 2021Article
- Review
1 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The metastatic spread of a tumor is dependent upon the ability of the tumor to stimulate surrounding stromal cells to express enzymes required for tissue remodeling. The immunoglobulin superfamily protein basigin (EMMPRIN/CD147) is a cell surface glycoprotein expressed by tumor cells that stimulates matrix metalloproteinase and vascular endothelial growth factor expression in stromal cells. The ability of basigin to stimulate expression of molecules involved in tissue remodeling and angiogenesis makes basigin a potential target for the development of strategies to block metastasis. However, the identity of the cell surface receptor for basigin remains controversial. The goal of this study was to determine the identity of the receptor for basigin. Using a novel recombinant basigin protein (rBSG) corresponding to the extracellular domain of basigin, it was demonstrated that the native, nonglycosylated rBSG protein forms dimers in solution. Furthermore, rBSG binds to the surface of uterine fibroblasts, activates the ERK1/2 signaling pathway, and induces expression of matrix metalloproteinases 1, 2, and 3. Proteins that interact with rBSG were isolated using a biotin label transfer technique and sequenced by matrix-assisted laser desorption ionization tandem mass spectrophotometry. The results demonstrate that rBSG interacts with basigin expressed on the surface of fibroblasts and is subsequently internalized. During internalization, rBSG associates with a novel form of human basigin (basigin-3). It was concluded that cell surface basigin functions as a membrane receptor for soluble basigin and this homophilic interaction is not dependent upon glycosylation of the basigin ligand.
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