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Literature summary for 3.4.24.81 extracted from

  • Schulz, B.; Pruessmeyer, J.; Maretzky, T.; Ludwig, A.; Blobel, C.P.; Saftig, P.; Reiss, K.
    ADAM10 regulates endothelial permeability and T-Cell transmigration by proteolysis of vascular endothelial cadherin (2008), Circ. Res., 102, 1192-1201.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
staurosporine ADAM10-mediated proteolysis of VE-cadherin is induced Homo sapiens

Application

Application Comment Organism
molecular biology ADAM10 is regulator of vascular permeability and possesses a function VE-cadherin-dependent endothelial cell functions and leukocyte transendothelial migration Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expressed in HUVEC and COS-7 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information increased ADAM10 expression is functionally associated with an increase in endothelial permeability. ADAM10 activity also contributes to the thrombin-induced decrease of endothelial cell-cell adhesion Homo sapiens
additional information knockdown of ADAM10 in HUVECs as well as in T cells by small interfering RNA impairs T-cell transmigration Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ ADAM10-mediated proteolysis of VE-cadherin is induced by Ca2+ influx Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
VE-cadherin + H2O 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 gamma-secretase cleavage Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
ADAM10
-
Homo sapiens