The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
ADAM10 Regulates Endothelial Permeability and T-Cell Transmigration by Proteolysis of Vascular Endothelial Cadherin
Open accessAbstract
Vascular endothelial (VE)-cadherin is the major adhesion molecule of endothelial adherens junctions. It plays an essential role in controlling endothelial permeability, vascular integrity, leukocyte transmigration, and angiogenesis. Elevated levels of soluble VE-cadherin are associated with diseases like coronary atherosclerosis. Previous data showed that the extracellular domain of VE-cadherin is released by an unknown metalloprotease activity during apoptosis. In this study, we used gain-of-function analyses, inhibitor studies, and RNA interference experiments to analyze the proteolytic release of VE-cadherin in human umbilical vein endothelial cells (HUVECs). We found that VE-cadherin is specifically cleaved by the disintegrin and metalloprotease ADAM10 in its ectodomain, releasing a soluble fragment and generating a carboxyl-terminal membrane-bound stub, which is a substrate for a subsequent γ-secretase cleavage. This ADAM10-mediated proteolysis could be induced by Ca 2+ influx and staurosporine treatment, indicating that ADAM10-mediated VE-cadherin cleavage contributes to the dissolution of adherens junctions during endothelial cell activation and apoptosis, respectively. In contrast, protein kinase C activation or inhibition did not modulate VE-cadherin processing. Increased ADAM10 expression was functionally associated with an increase in endothelial permeability. Remarkably, our data indicate that ADAM10 activity also contributes to the thrombin-induced decrease of endothelial cell–cell adhesion. Moreover, knockdown of ADAM10 in HUVECs as well as in T cells by small interfering RNA impaired T-cell transmigration. Taken together, our data identify ADAM10 as a novel regulator of vascular permeability and demonstrate a hitherto unknown function of ADAM10 in the regulation of VE-cadherin–dependent endothelial cell functions and leukocyte transendothelial migration.
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Cited by
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The physiology of the β‐amyloid precursor protein intracellular domain AICD
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Extracellular matrix dynamics in vascular remodeling
Ma, Z., Mao, C., Jia, Y., Fu, Y., & Kong, W. (2020) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00147.2020 · Cited by 129
Metadata
- Authors
- Schulz, B., Pruessmeyer, J., Maretzky, T., Ludwig, A., Blobel, C. P., Saftig, P., & Reiss, K.
- Venue
- Circulation Research
- Published
- 2008-05-23
- Volume
- 102
- Issue
- 10
- Pages
- 1192-1201
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- OpenAlex
- W1997642891
- Cited by
- 301
- References
- 34
- FWCI
- 11.25
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: ADAM10 Regulates Endothelial Permeability and T-Cell Transmigration by Proteolysis of Vascular Endothelial Cadherin. https://app.cochat.ai/papers/10.1161/circresaha.107.169805
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- Schulz, B., Pruessmeyer, J., Maretzky, T., Ludwig, A., Blobel, C. P., Saftig, P., & Reiss, K. (2008). ADAM10 Regulates Endothelial Permeability and T-Cell Transmigration by Proteolysis of Vascular Endothelial Cadherin. Circulation Research. https://doi.org/10.1161/circresaha.107.169805
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