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Angiomotin regulates endothelial cell-cell junctions and cell motility
Anders Bratt1, Olivier Birot, Indranil Sinha
1Department of Oncology and Pathology, Cancer Centrum Karolinska, Karolinska Institutet, R8:03 Karolinska University Hospital, 171 76 Stockholm, Sweden.
The Journal of Biological Chemistry
|July 27, 2005
Summary
Angiomotin, a protein involved in cell movement, also helps form endothelial cell junctions. Angiostatin binds angiomotin, inhibiting cell migration but not affecting cell permeability.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Angiomotin is identified for its role in binding angiostatin and mediating anti-angiogenic properties.
- Previous studies suggest angiomotin is crucial for endothelial cell motility.
Purpose of the Study:
- To investigate the interaction between angiostatin and angiomotin on the cell surface.
- To elucidate the role of angiomotin isoforms (p80 and p130) in endothelial cell junction formation and function.
Main Methods:
- Immunofluorescence analysis to determine angiomotin localization.
- Cell transfection to express angiomotin isoforms.
- Co-precipitation assays to identify interacting proteins.
- Paracellular permeability assays using fluorescein isothiocyanate-dextran.
- Boyden chamber assay to assess cell migration.
Main Results:
- Angiostatin binds to cell surface angiomotin.
- Both p80 and p130 angiomotin isoforms localize to cell-cell junctions.
- p130 angiomotin recruits ZO-1 to actin stress fibers.
- Expression of p80 and p130 angiomotin significantly reduced paracellular permeability.
- Angiostatin inhibited migration of angiomotin-expressing cells but not cell permeability.
Conclusions:
- Angiomotin plays a role in both endothelial cell motility and the assembly of endothelial cell-cell junctions.
- Angiomotin isoforms have distinct but complementary roles in regulating endothelial barrier function and cell migration.