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Published on: October 17, 2014
Vascular endothelial cadherin (VE-cadherin): cloning and role in endothelial cell-cell adhesion
1Department of Cell Physiology and Immunology, Rockefeller University, New York, USA.
Insights
Researchers identified vascular endothelial cadherin (VE-cadherin) as key for endothelial cell junction integrity. This cell adhesion molecule promotes calcium-dependent homophilic cell-cell adhesion, crucial for maintaining endothelial monolayer integrity.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Intercellular junction integrity is vital for endothelial cell function.
- Identifying specific proteins involved in these junctions is crucial for understanding vascular biology.
Purpose of the Study:
- To identify proteins responsible for intercellular junction integrity in human umbilical vein endothelial cells (HUVEC).
- To characterize and clone the identified endothelial cell-specific protein for functional studies.
Main Methods:
- Production of a monoclonal antibody recognizing an endothelial cell-specific protein.
- Immunofluorescence and immunoprecipitation to determine antigen size and distribution.
- Cloning and transfection of the antigen into cell lines to assess its role in cell-cell adhesion and growth.
Main Results:
- Monoclonal antibody hec1 recognizes VE-cadherin, an endothelial cell-restricted cell adhesion molecule.
- VE-cadherin localizes to endothelial cell borders, mediating calcium-dependent homophilic adhesion.
- Transfection of VE-cadherin into fibroblasts confers adhesion properties without affecting growth rate.
Conclusions:
- VE-cadherin functions as a classic cadherin, mediating calcium-dependent homophilic cell adhesion.
- VE-cadherin plays a significant role in maintaining the integrity of endothelial cell monolayers.
Objective:
To identify proteins responsible for intercellular junction integrity in human umbilical vein endothelial cells (HUVEC), we produced a monoclonal antibody that recognized an endothelial cell-specific, junctionally restricted protein. We characterized and cloned the antigen to study its functional properties.
Methods:
The size and cellular distribution of the antigen were determined by immunofluorescence and immunoprecipitation. The molecule was cloned and transfected into cell lines, and its role in cell-cell adhesion and growth rate was determined.
Results:
Monoclonal antibody hec1 recognizes VE-cadherin, an endothelial cell-restricted cell adhesion molecule. VE-cadherin is localized to the borders between apposing endothelial cells but is diffusely distributed on subconfluent or migrating cells. Transfection of fibroblasts with VE-cadherin imparts to them the ability to adhere to each other in a calcium-dependent homophilic manner. Expression of VE-cadherin over a several-log range does not change the growth rate of these cells.
Conclusions:
Despite the fact that VE-cadherin is a "nonclassical" cadherin by structure, it functions as a classic cadherin by imparting to cells the ability to adhere in a calcium-dependent, homophilic manner. On HUVEC it appears to play a role in maintaining monolayer integrity.
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