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10:23
Covalent Binding of BMP-2 on Surfaces Using a Self-assembled Monolayer Approach
Published on: August 26, 2013
Basigin-2 is a cell surface receptor for soluble basigin ligand
Robert J Belton1, Li Chen, Fernando S Mesquita
1Department of Animal Sciences, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. rbelton@uiuc.edu
The Journal of Biological Chemistry
|April 25, 2008
Summary
Tumor cell surface basigin (EMMPRIN/CD147) acts as a receptor for soluble basigin, stimulating tissue remodeling and angiogenesis. This homophilic interaction, crucial for metastasis, is independent of ligand glycosylation.
Area of Science:
- Oncology
- Cell Biology
- Biochemistry
Background:
- Tumor metastasis relies on stromal cell stimulation for tissue remodeling.
- Basigin (EMMPRIN/CD147), a tumor cell glycoprotein, promotes matrix metalloproteinase and VEGF expression in stromal cells.
- Basigin's role in tissue remodeling and angiogenesis makes it a target for anti-metastasis strategies, but its receptor is debated.
Purpose of the Study:
- To identify the cell surface receptor for basigin.
Main Methods:
- Utilized a novel recombinant basigin protein (rBSG) for extracellular domain studies.
- Employed biotin label transfer and mass spectrometry to identify interacting proteins.
- Investigated rBSG binding, ERK1/2 signaling activation, and matrix metalloproteinase induction in fibroblasts.
Main Results:
- Nonglycosylated rBSG forms dimers and binds to fibroblast surface basigin.
- rBSG activates ERK1/2 signaling and induces matrix metalloproteinases 1, 2, and 3.
- rBSG is internalized and associates with basigin-3, identifying cell surface basigin as the receptor.
Conclusions:
- Cell surface basigin functions as a membrane receptor for soluble basigin.
- This homophilic interaction is crucial for stimulating stromal cells and is not dependent on ligand glycosylation.
- Findings provide a target for anti-metastasis therapies by understanding basigin-basigin interactions.
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