Literature summary for 3.4.24.81 extracted from

Pabois, A.; Devalliere, J.; Quillard, T.; Coulon, F.; Gerard, N.; Laboisse, C.; Toquet, C.; Charreau, B.
The disintegrin and metalloproteinase ADAM10 mediates a canonical Notch-dependent regulation of IL-6 through Dll4 in human endothelial cells (2015), Biochem. Pharmacol., 91, 510-521 .

Search for more literature for 3.4.24.81

Inhibitors

Inhibitors	Comment	Organism	Structure
GI254023X	specific inhibitor, i.e. (2R,3S)-3-(formyl-hydroxyamino)-2-(3-phenyl-1-propyl) butanoic acid [(1S)-2,2-dimethyl-1 methylcarbamoyl-1-propyl] amide	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O14672	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
arteriole	-	Homo sapiens	-
CD31+ cell	-	Homo sapiens	-
endothelial cell	-	Homo sapiens	-
endothelium	-	Homo sapiens	-
JURKAT cell	-	Homo sapiens	-
additional information	the enzyme is not localized in cardiomyocytes	Homo sapiens	-
vascular endothelial cell	-	Homo sapiens	-

Subunits

Subunits	Comment	Organism
?	x * 105000, SDS-PAGE	Homo sapiens

Synonyms

Synonyms	Comment	Organism
ADAM10	-	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	the enzyme activates Notch signaling through Hes1 and Hey1	Homo sapiens
physiological function	the enzyme mediates a canonical Notch-dependent regulation of IL-6 through Dll4 in human endothelial cells. ADAM10/Dll4 signaling is a major signaling pathway in endothelial cells driving inflammatory events involved in inflammation and immune cell recruitment	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)