ADAM10 Regulates Endothelial Permeability and T-Cell Transmigration by Proteolysis of Vascular Endothelial Cadherin

By B. Schulz, J. Pruessmeyer, Thorsten Maretzky, A. Ludwig, C. Blobel, P. Saftig, K. Reiss. 2008

321 citations recorded by the source corpus.

Subfields: Immunology and Allergy, Molecular Biology

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In Immunology and Allergy

1. S. Zhong
2. R. Khalil

In Molecular Biology

1. M. Handsley
2. D. Edwards
3. S. Zhong
4. R. Khalil
5. M. Day
6. C. Pennington

Citations in the corpus

• A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease (2019, background): “ADAM-10 regulates the cleavage of N-cadherin to increase apoptosis in human atherosclerotic lesions and promote the risk of vulnerable plaque [134].”
• The ADAM metalloproteinases (2008, background): “Several studies have however linked ADAM-10 to cleavage of the adhesion molecules N-, E- and VE-cadherin (Maretzky et al., 2005a; Reiss et al., 2005; Schulz et al., 2008).”
• ADAM15 regulates endothelial permeability and neutrophil migration via Src/ERK1/2 signalling. (2010, background): “The metalloproteinase domain has a consensus HEXXGXXH sequence capable of degrading matrix(14) and shedding cytokines,(15) growth factor and growth factor receptors,(16,17) and cadherins.(18,19) The disintegrin domain of human ADAM15 contains an RGD sequence that can regulate integrin binding and su”