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ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin
Claire Ham1, Bodo Levkau, Elaine W Raines
1British Heart Foundation Laboratories, Department of Medicine, University College London, London, United Kingdom.
Experimental Cell Research
|September 24, 2002
Summary
ADAM15 protein localizes to adherens junctions, particularly with VE-cadherin, suggesting a role in endothelial cell adhesion. VE-cadherin expression drives ADAM15 surface presence, indicating a novel junctional function.
Area of Science:
- Cell biology
- Molecular biology
- Biochemistry
Background:
- ADAM15 (a disintegrin and metalloprotease domain protein) is involved in cell adhesion and shedding.
- Its precise localization and function in cell junctions remain unclear.
Purpose of the Study:
- To investigate the localization of ADAM15 within adherens junctions.
- To determine the relationship between ADAM15 and VE-cadherin in cell-cell contacts.
- To explore the role of VE-cadherin in regulating ADAM15 surface expression.
Main Methods:
- Immunofluorescence microscopy to visualize protein localization.
- Co-expression studies in CHO cells using ADAM15 and VE-cadherin.
- Analysis of ADAM15 surface expression via flow cytometry and western blotting.
Main Results:
- ADAM15 colocalizes with vascular endothelial (VE)-cadherin at adherens junctions.
- ADAM15 accumulation at cell contacts is preceded by VE-cadherin-mediated junction formation.
- VE-cadherin coexpression significantly enhances ADAM15 surface expression.
Conclusions:
- ADAM15 is a novel component of adherens junctions.
- VE-cadherin drives the surface expression of ADAM15.
- ADAM15 may play a significant role in endothelial cell functions mediated by adherens junctions.