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Information on EC 3.4.24.81 - ADAM10 endopeptidase and Organism(s) Homo sapiens and UniProt Accession O14672

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.81 ADAM10 endopeptidase
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This record set is specific for:
Homo sapiens
UNIPROT: O14672 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
endopeptidase of broad specificity
Synonyms
adam10, adam-10, adam 10, a disintegrin and metalloproteinase 10, a disintegrin and metalloprotease 10, kuzbanian, metalloproteinase adam10, metalloproteinase 10, metalloproteinase-disintegrin, a disintegrin and metalloproteinase-10, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
a disintegrin and metalloproteinase 10
-
a disintegrin and metalloprotease 10
-
-
a disintegrin and metalloproteinase 10
-
-
a disintegrin and metalloproteinase-10
-
-
ADAM 10
-
-
ADAM-10
ADAM10
CD23 metalloprotease
-
-
kuzbanian
-
-
Kuzbanian protein
-
-
-
-
mammalian disintegrin-metalloprotease
-
-
-
-
metalloproteinase 10
-
-
metalloproteinase ADAM10
-
-
-
-
metalloproteinase Kuzbanian
-
-
-
-
metalloproteinase MADM
-
-
-
-
metalloproteinase-disintegrin
-
-
myelin-associated disintegrin metalloproteinase
-
-
-
-
notch proteinase
-
-
-
-
transmembrane metzinkin-protease of the a disintegrin and metalloproteinase family-10
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
additional information
-
ADAM10 mediates the epidermal growth factor-induced CD44 cleavage by the small monomeric GTPase Rac1
CAS REGISTRY NUMBER
COMMENTARY hide
193099-09-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alcadein + H2O
?
show the reaction diagram
-
-
-
?
annexin A1 + H2O
?
show the reaction diagram
-
-
-
?
beta-amyloid precursor protein + H2O
sAPP-alpha fragment + C-terminal fragment
show the reaction diagram
Bri2 + H2O
?
show the reaction diagram
-
-
-
?
C4.4A + H2O
?
show the reaction diagram
-
-
-
?
Cad6B + H2O
?
show the reaction diagram
-
-
-
?
CD154 + H2O
?
show the reaction diagram
-
-
-
?
CD84 + H2O
?
show the reaction diagram
signaling lymphocyte activation molecule (SLAM) family receptor CD84
CD84 is cleaved from the surface of human platelets. ADAM10 is the principal sheddase responsible for CD84 cleavage
-
?
cell adhesion molecule 1 + H2O
?
show the reaction diagram
-
-
-
?
cell adhesion molecule CADM1 + H2O
?
show the reaction diagram
type I transmembrane glycoprotein, endopeptidase ADAM10 mediates endogenous CADM1 shedding. The membrane-bound fragment generated by shedding is further cleaved by gammaetase and generates CADM1-intracellular domain
-
-
?
cell surface VEGF receptor Flt + H2O
?
show the reaction diagram
-
release of an N-terminal extracellular fragment which can antagonize the effects of vascular endothelial growth factor, substrate can be cleaved to release an N-terminal extracellular fragment. Overexpression of ADAM10 and ADAM17, EC 3.4.24.86, increase cleavage while knockdown of ADAM10 and ADAM17 reduce N-terminal cleavage
-
?
collagen type XVII + H2O
?
show the reaction diagram
-
-
-
?
coxsackievirus and adenovirus receptor + H2O
?
show the reaction diagram
-
-
-
?
CXCL16 + H2O
?
show the reaction diagram
-
-
-
?
discoidin domain receptor 1 + H2O
?
show the reaction diagram
-
-
-
?
E(Edans)-PLAQAVRSSS[O-(beta-D-Glc-(1->3)-alpha-D-GlcNAc]-K(Dabcyl) + H2O
E(Edans)-PLAQA + VRSSS[O-(beta-D-Glc-(1->3)-alpha-D-GlcNAc]-K(Dabcyl)
show the reaction diagram
-
-
-
ir
E-cadherin + H2O
?
show the reaction diagram
efficient cleavage of the ADAM10 substrate epithelial cadherin (E-cadherin) requires supra-cytotoxic concentrations of alpha-toxin
-
-
?
FAT1 + H2O
?
show the reaction diagram
-
-
-
?
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser(glycosyl)-Ser-Lys(DABCYL) + H2O
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala + Val-Arg-Ser-Ser(glycosyl)-Ser-Lys(DABCYL)
show the reaction diagram
-
-
-
?
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Lys(DABCYL) + H2O
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala + Val-Arg-Ser-Ser-Ser-Lys(DABCYL)
show the reaction diagram
-
-
-
?
gp130 + H2O
?
show the reaction diagram
-
-
-
?
HER2 + H2O
?
show the reaction diagram
-
-
-
?
interleukin 11R + H2O
?
show the reaction diagram
-
-
-
?
interleukin-6 receptor + H2O
sIL-6R fragment + C-terminal fragment
show the reaction diagram
-
-
-
?
interleukin-6 receptor subunit alpha + H2O
?
show the reaction diagram
-
cleavage occurs between residues LPVQ357-DSSV. Substrate shows N-linked glycosylation 7 residues apart from scissile bond
-
?
Klotho + H2O
?
show the reaction diagram
-
-
-
?
L1 adhesion molecule + H2O
?
show the reaction diagram
-
-
-
?
Leda-1 + H2O
?
show the reaction diagram
-
-
-
?
N-cadherin + H2O
?
show the reaction diagram
-
-
-
?
nerveglia antigen 2 + H2O
?
show the reaction diagram
-
-
-
?
neuroligin 1 + H2O
?
show the reaction diagram
-
-
-
?
Notch-1 + H2O
?
show the reaction diagram
-
-
-
?
PMEL17 + H2O
?
show the reaction diagram
-
-
-
?
probetacellulin + H2O
?
show the reaction diagram
-
cleavage occurs between residues CVVA31-DGNS. Substrate shows N-linked glycosylation 3 residues apart from scissile bond
-
?
proheparin-binding EGF-like growth factor + H2O
?
show the reaction diagram
-
cleavage occurs between residues RKVR62-DLQE. Substrate shows O-linked glycosylation 13 residues apart from scissile bond
-
?
protransforming growth factor alpha + H2O
?
show the reaction diagram
-
cleavage occurs between residues AAA39-VVSH. Substrate shows N-linked glycosylation 14 residues apart from scissile bond
-
?
SIRPalpha + H2O
?
show the reaction diagram
-
-
-
?
syndecan + H2O
?
show the reaction diagram
-
-
-
?
syndecan-1 + H2O
?
show the reaction diagram
both ADAM10 and ADAM17 contribute to SDC1 shedding
-
-
?
TACI + H2O
?
show the reaction diagram
-
-
-
?
thyrotropin receptor + H2O
?
show the reaction diagram
-
-
-
?
TREM2 + H2O
?
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl-EVHHQKLVFFAE + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-HGDQMAQKSQST + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-LPQLENVKGTED + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-RAEQQRLKSQDL + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-SPLAQAVRSSSR + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Arg-Dap(dnp)-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
amyloid precursor protein + H2O
?
show the reaction diagram
amyloid precursor-like protein 2 + H2O
soluble amyloid precursor-like protein 2 ectodomain + amyloid precursor-like protein 2 C-terminal fragments
show the reaction diagram
-
ADAM10 cleaves after Arg670
-
-
?
annexin A1 + H2O
?
show the reaction diagram
-
ADAM10 cleaves within the N-terminal domain after Phe7, cleavage occurs on the outer cell surface during secondary but not primary necrosis
-
-
?
beta-amyloid precursor protein
sAPP-alpha fragment + C-terminal fragment
show the reaction diagram
beta-amyloid precursor protein + H2O
sAPP-alpha fragment + C-terminal fragment
show the reaction diagram
-
-
-
-
?
beta-amyloid precursor protein + H2O
sAPP-alpha fragment of beta-amyloid precursor protein + C-terminal fragment of beta-amyloid precursor protein
show the reaction diagram
-
-
-
-
?
biotin-SPLAQAVRSSSRTPS-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
Bri2 protein + H2O
?
show the reaction diagram
-
-
the ADAM10 cleavage liberates the BRICHOS domain of Bri2
-
?
C4.4A + H2O
?
show the reaction diagram
-
the proteomic identification of a novel substrate for ADAM10 and ADAM17 is presented by using SILAC (Stable Isotope Labeling by Amino acids in Cell culture), a proteomic technique based on the differential metabolic labeling of cells in different conditions. This is applied to MCF7 cells derived from an invasive mammary tumor, and the same cells expressing shRNAs that knock down ADAM10 or -17. C4.4A is a member of the Ly-6 family originally identified in a screening designed to select membrane proteins differentially expressed on metastatic pancreatic adenocarcinoma cells
-
-
?
CD23 + H2O
?
show the reaction diagram
-
-
-
-
?
CD46 + H2O
sCD46-ectodomain + ?
show the reaction diagram
-
-
-
-
?
cellular prion protein
N1 fragment + C-terminal fragment
show the reaction diagram
-
constitutive protein cleavage
-
?
CXCL16 + H2O
?
show the reaction diagram
-
-
-
-
?
dabcyl-LAQA(homoPhe)RSC(fluorescein)-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
epidermal growth factor + H2O
?
show the reaction diagram
-
-
-
-
?
epithelial cadherin + H2O
38-kDa C-terminal fragment + ?
show the reaction diagram
-
-
-
-
?
epithelial growth factor receptor
?
show the reaction diagram
-
activation of the receptor leads to cleavage of transmembrane heparin-binding site by ADAM10 in response to infection by Staphylococcus aureus
-
-
?
extracellular domain of Klotho + H2O
130000 Da Klotho fragment + 68000 Da Klotho fragment
show the reaction diagram
-
-
-
-
?
Fas ligand + H2O
soluble Fas ligand ectodomain + ?
show the reaction diagram
-
transmembrane protein
-
-
?
FcalphaR + H2O
?
show the reaction diagram
L1 adhesion molecule
L1-200 fragment + L1-32 fragment + ?
show the reaction diagram
-
ADAM10 cleaves L1
-
?
L1 cell-adhesion molecule + H2O
?
show the reaction diagram
L1-CAM extracellular domain + H2O
?
show the reaction diagram
-
-
-
-
?
neuronal cadherin + H2O
neuronal cadherin C-terminal fragment + ?
show the reaction diagram
-
-
-
-
?
protocadherin + H2O
?
show the reaction diagram
-
ADAM10 cleaves the extracellular domain of protocadherin
-
-
?
RAGE + H2O
?
show the reaction diagram
-
a soluble form of the receptor for advanced glycation endproducts (RAGE) is produced by proteolytic cleavage of the membrane-bound form by ADAM10
-
-
?
TNF-alpha + H2O
?
show the reaction diagram
-
-
-
-
?
VE-cadherin + H2O
?
show the reaction diagram
-
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
-
-
?
additional information
?
-
-
TIMP1 and TIMP-3 (tissue inhibitors of metalloproteinase) interact and inhibit ADAM10
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alcadein + H2O
?
show the reaction diagram
-
-
-
?
annexin A1 + H2O
?
show the reaction diagram
-
-
-
?
beta-amyloid precursor protein + H2O
sAPP-alpha fragment + C-terminal fragment
show the reaction diagram
Bri2 + H2O
?
show the reaction diagram
-
-
-
?
C4.4A + H2O
?
show the reaction diagram
-
-
-
?
Cad6B + H2O
?
show the reaction diagram
-
-
-
?
CD154 + H2O
?
show the reaction diagram
-
-
-
?
cell adhesion molecule 1 + H2O
?
show the reaction diagram
-
-
-
?
collagen type XVII + H2O
?
show the reaction diagram
-
-
-
?
coxsackievirus and adenovirus receptor + H2O
?
show the reaction diagram
-
-
-
?
E-cadherin + H2O
?
show the reaction diagram
efficient cleavage of the ADAM10 substrate epithelial cadherin (E-cadherin) requires supra-cytotoxic concentrations of alpha-toxin
-
-
?
FAT1 + H2O
?
show the reaction diagram
-
-
-
?
gp130 + H2O
?
show the reaction diagram
-
-
-
?
interleukin 11R + H2O
?
show the reaction diagram
-
-
-
?
interleukin-6 receptor + H2O
sIL-6R fragment + C-terminal fragment
show the reaction diagram
-
-
-
?
Klotho + H2O
?
show the reaction diagram
-
-
-
?
L1 adhesion molecule + H2O
?
show the reaction diagram
-
-
-
?
Leda-1 + H2O
?
show the reaction diagram
-
-
-
?
N-cadherin + H2O
?
show the reaction diagram
-
-
-
?
nerveglia antigen 2 + H2O
?
show the reaction diagram
-
-
-
?
neuroligin 1 + H2O
?
show the reaction diagram
-
-
-
?
Notch-1 + H2O
?
show the reaction diagram
-
-
-
?
PMEL17 + H2O
?
show the reaction diagram
-
-
-
?
SIRPalpha + H2O
?
show the reaction diagram
-
-
-
?
TACI + H2O
?
show the reaction diagram
-
-
-
?
TREM2 + H2O
?
show the reaction diagram
-
-
-
?
amyloid precursor protein + H2O
?
show the reaction diagram
annexin A1 + H2O
?
show the reaction diagram
-
ADAM10 cleaves within the N-terminal domain after Phe7, cleavage occurs on the outer cell surface during secondary but not primary necrosis
-
-
?
beta-amyloid precursor protein
sAPP-alpha fragment + C-terminal fragment
show the reaction diagram
beta-amyloid precursor protein + H2O
sAPP-alpha fragment of beta-amyloid precursor protein + C-terminal fragment of beta-amyloid precursor protein
show the reaction diagram
-
-
-
-
?
cellular prion protein
N1 fragment + C-terminal fragment
show the reaction diagram
-
constitutive protein cleavage
-
?
epithelial growth factor receptor
?
show the reaction diagram
-
activation of the receptor leads to cleavage of transmembrane heparin-binding site by ADAM10 in response to infection by Staphylococcus aureus
-
-
?
FcalphaR + H2O
?
show the reaction diagram
-
FcaR (CD89) is the Fc receptor for immunoglobulin A. ADAM10 and ADAM17 are involved in the shedding of FcalphaR
-
-
?
L1 adhesion molecule
L1-200 fragment + L1-32 fragment + ?
show the reaction diagram
-
ADAM10 cleaves L1
-
?
L1 cell-adhesion molecule + H2O
?
show the reaction diagram
-
the ectodomain of L1 cell-adhesion molecule is cleaved at the plasma membrane by ADAM10. Regulated proteolytic processing by ADAM10 and PS/gamma-secretase is essential for the nuclear signalling of L1 in human carcinoma cell lines
-
-
?
additional information
?
-
-
TIMP1 and TIMP-3 (tissue inhibitors of metalloproteinase) interact and inhibit ADAM10
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
activation of the enzyme can be achieved by cellular influx of Ca2+
Ca2+
-
ADAM10-mediated proteolysis of VE-cadherin is induced by Ca2+ influx
Zinc
-
ADAM10 belongs to the subgroup of metzincins within the zinc proteinases family
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(2,4-dioxo-3-phenyl-1,3-thiazolidin-5-yl)-N-(4-ethoxyphenyl)acetamide
-
3-[[1-[(2-(hydroxymethyl)-1-pyrrolidinyl)carbonyl]-2-methylpropyl]carbamoyl]octanohydroxamic acid
actinonin
4-(1H-indol-3-yl)-4-oxobutanoic acid
-
5-[(4-chlorophenyl)methyl]-5-phenylimidazolidine-2,4-dione
-
ADAM10 prodomain
-
-
GI254023X
GW280264X
-
marimastat
-
N-(3-chloro-4-methylphenyl)-2-[2-(3-methoxybenzoyl)hydrazinyl]-2-oxoacetamide
selective, non-competitive inhibitor
nerve growth factor
-
-
Rapamycin
-
((2R,3S)-3-(formyl-hydroxyamino)-2-(3-phenyl-1-propyl)butanoic acid)[(1S)-2,2-dimethyl-1-methylcarbamoyl-1-propyl]amide
-
compound GI254023X, IC50: 5.3
(2S)-N4-hydroxy-N1-[(1S)-1-(1H-indol-3-ylmethyl)-2-(methylamino)-2-oxoethyl]-2-isobutylsuccinamide
-
GM6001
AEBSF
-
0.1 mM
atorvastatin
-
80mg/day
BB3103
-
0.01 mM inhibitory but not completely
-
decanoyl-RVKR-chloromethylketone
-
0.03 mM of this proprotein convertase inhibitor decreases the formation of the ADAM10 mature form
EDTA
-
10 mM
EGTA
-
10 mM
G1254023X
-
specific inhibitor
GI254023
-
0.005 mM
GI254023X
GM6001
GW 280264X
-
ADAM10/17 inhibitor
GW280264
-
0.005 mM
GW280264X
GW280623X
-
inhibits RAGE (receptor for advanced glycation endproducts) cleavage
GW4023
-
-
-
o-phenanthroline
-
inhibit activity 0.1 mM
pepstatin A
-
0.001 mM
TAPI
-
0.01 mM inhibitory but not completely
TAPI-1
TAPI-2
TIMP-1
-
TIMP-2
-
modest inhibitory activity toward CD23 shedding
-
TIMP-3
-
TNFalpha protease inhibitor
-
0.05 mM
-
Wortmannin
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-hydroxytryptamine receptor
-
-
acetyl-L-carnitine
-
bombesin receptor
-
-
cryptotanshinone
-
donezipil
-
epigallocatechin-3-gallate
-
FLZ
synthetic analogue of natural squamosamide
formononentin
-
G-protein-coupled purinergic receptor
-
-
gintonin
-
-
glucagon-like peptide-1 receptor
-
-
ion channel purinergic receptor
-
-
metallothionein III
-
-
nardilysin
-
-
pituitary adenylate cyclase-activating polypeptide receptor
-
-
synapse-associated protein 97
-
-
tetraspanin 10
-
-
tetraspanin 12
-
tetraspanin 14
-
-
tetraspanin 15
-
-
tetraspanin 17
-
-
tetraspanin 27
-
-
tetraspanin 28
-
-
tetraspanin 29
-
-
tetraspanin 33
-
-
tetraspanin 5
-
-
thyrotropin
increases dose dependently thyrotropin receptor ectodomain cleavage
-
5alpha-dihydrotestosterone
-
10 nM, in the presence of 10 or 50 ng/ml insulin-like growth factor, 1.8fold upregulation of the 100-kDa proform and 3 to 4 fold stimulation of the active 60-kDa form
donepezil
-
because donepezil-treated cells show an increase in the metabolic active form of ADAM 10, this suggests that donepezil may cause a direct increase in the level of ADAM 10 in cellular membranes
Epidermal growth factor
-
50 ng/ml, 2fold stimulation of 100-kDa proform and 3fold stimulation of 60-kDa form
Insulin
-
0.001 mM, stimulates the cleavage of the extracellular domain of Klotho
-
insulin-like growth factor I
-
10 ng/ml or 50 ng/ml, in the presence of 10 nM 5alpha-dihydrotestosterone, 1.8fold upregulation of the 100-kDa proform and 3 to 4fold stimulation of the active 60-kDa form
-
interleukin-1alpha
-
2 ng/ml stimulates ADAM-10 level 2.1 fold after 16h treatment
-
ionomycin
-
0.005 mM, strongly increases the generation of epithelial cadherin 38 kDa-C-terminal fragment
phorbol myristate acetate
-
100 nM, induces the expression of the highly processed form of ADAM10
phorbol-12 myristate 13-acetate
-
clearly enhanced epithelial cadherin shedding
S100A7
-
expression of exogenous S100A7, a biomarker protein for alzheimer’s disease known to be involved in immune responses, in primary cortico-hippocampal neuron cultures derived from Tg2576 transgenic mice embryos inhibits the generation of beta-amyloid (Abeta)1-42 and Abeta1-40 peptides, coincidental with a selective promotion of non-amyloidogenic alpha-secretase activity via promotion of ADAM10. A selective expression of human S100A7, in the brain of transgenic mice results in significant promotion of alpha-secretase activity
-
staurosporine
tetraspanin
-
several anti-tetraspanin mAbs (CD9, CD81, CD82) increase epidermal growth factor and/or TNF-alpha secretion through a mechanism dependent on ADAM10. The effect of anti-tetraspanin mAb on TNF-alpha release is rapid, not relayed by intercellular signaling, and depends on an intact MEK/Erk1/2 pathway. It is also associated with a concentration of ADAM10 in tetraspanin-containing patches. A large fraction of ADAM10 associates with several tetraspanins
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0085
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser(glycosyl)-Ser-Lys(DABCYL)
pH 7.5, 22°C
0.012
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Lys(DABCYL)
pH 7.5, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser(glycosyl)-Ser-Lys(DABCYL)
pH 7.5, 22°C
0.28
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Lys(DABCYL)
pH 7.5, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser(glycosyl)-Ser-Lys(DABCYL)
pH 7.5, 22°C
25
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Lys(DABCYL)
pH 7.5, 22°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000005
GI254023X
pH and temperature not specified in the publication
0.000883
N-(3-chloro-4-methylphenyl)-2-[2-(3-methoxybenzoyl)hydrazinyl]-2-oxoacetamide
at pH 7.5 and 25°C
0.0000001
TIMP-1
pH and temperature not specified in the publication
-
0.0000009
TIMP-3
pH and temperature not specified in the publication
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
2-(2,4-dioxo-3-phenyl-1,3-thiazolidin-5-yl)-N-(4-ethoxyphenyl)acetamide
Homo sapiens
IC50 above 0.07 mM, at pH 7.5 and 25°C
0.07
3-[[1-[(2-(hydroxymethyl)-1-pyrrolidinyl)carbonyl]-2-methylpropyl]carbamoyl]octanohydroxamic acid
Homo sapiens
IC50 above 0.07 mM, at pH 7.5 and 25°C
0.07
4-(1H-indol-3-yl)-4-oxobutanoic acid
Homo sapiens
IC50 above 0.07 mM, at pH 7.5 and 25°C
0.032
5-[(4-chlorophenyl)methyl]-5-phenylimidazolidine-2,4-dione
Homo sapiens
at pH 7.5 and 25°C
0.0065
N-(3-chloro-4-methylphenyl)-2-[2-(3-methoxybenzoyl)hydrazinyl]-2-oxoacetamide
Homo sapiens
at pH 7.5 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
both ADAM10 and ADAM17 contribute to SDC1 shedding and IL-8 production by HVECs in response to staphylococcal superantigen toxic shock syndrome toxin TSST-1
Manually annotated by BRENDA team
-
A-172 cell line has potent alpha-secretase activity, higher than HEK-293 cell line
Manually annotated by BRENDA team
-
strain U373 MG
Manually annotated by BRENDA team
-
expression of ADAM 10, 12 and 17 is analyzed by immunohistochemistry in skin tissues obtained from 25 patients with different types of basal cell carcinomas. Immunoreactivity of ADAM 10, 12 and 17 is increased at the peripheral tumor margin compared with central areas of basal cell carcinomas tumor cell nests. Immunoreactivity of ADAM 10 and 12 is increased in the deep margin of invading tumor cell nests in mixed basal cell carcinomas
Manually annotated by BRENDA team
-
intraluminal
Manually annotated by BRENDA team
-
lower levels of ADAM10 in Alzheimer disease
Manually annotated by BRENDA team
-
there is expression of the enzyme
Manually annotated by BRENDA team
-
there is expression of the enzyme
Manually annotated by BRENDA team
-
the expression is increased 2-fold in Alzheimer disease
Manually annotated by BRENDA team
-
HM3 cell line
Manually annotated by BRENDA team
-
the expression is increased 2-fold in Alzheimer disease
Manually annotated by BRENDA team
-
confirmation of ADAM10-TSPAN12 association
Manually annotated by BRENDA team
-
there is expression of the enzyme
Manually annotated by BRENDA team
-
there is expression of the enzyme
Manually annotated by BRENDA team
-
confirmation of ADAM10-TSPAN12 association
Manually annotated by BRENDA team
-
human mesenchymal stem cells interfere with cell–cell adhesion and enhance migration of breast cancer cells by activating ADAM10
Manually annotated by BRENDA team
-
strain SH-SY5Y
Manually annotated by BRENDA team
-
ADAM10 is necessary for epidermal growth factor receptor transactivation
Manually annotated by BRENDA team
-
cell line LNCaP, localized to the secretory cells of prostate glands, with additional basal cell expression in benign glands
Manually annotated by BRENDA team
-
human salivary gland cells are used
Manually annotated by BRENDA team
-
cytoplasmic expression of ADAM 10 is observed in the hair bulb keratinocytes and fibroblasts of dermal papilla in anagen I–III hair follicles. Decreased ADAM 10 expression is observed in the hair matrix keratinocytes as compared to the hair bulb keratinocytes in anagen I–III hair follicles. ADAM 10 immunoreactivity is expressed weakly in the lower portion of outer root sheath of anagen VI hair follicles, and strong ADAM 10 expression is detected in the outer root sheath of catagen and telogen hair follicles
Manually annotated by BRENDA team
-
there is expression of the enzyme
Manually annotated by BRENDA team
-
there is expression of the enzyme
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
most of the activity of the enzyme
Manually annotated by BRENDA team
-
predominant localization of the protein at the perinuclear region and at the cell surface where it appears as punctuated dots evenly distributed at the plasma membrane
-
Manually annotated by BRENDA team
-
exosomal
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
the enzyme activates Notch signaling through Hes1 and Hey1
physiological function
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADA10_HUMAN
748
1
84142
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
SDS-PAGE, proform of ADAM-10
45000
-
highly processed mature form, SDS-PAGE
60000
68000
70000
-
SDS-PAGE, mature form wild-type
85000
98000
-
SDS-PAGE, immature form wild-type
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
the enzyme has four potential N-glycosylation sites (N267, N278, N439 and N551)
glycoprotein
proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q170H
the mutation in the pro-domain region of the ADAM10 gene reduce alpha-secretase activity of the enzyme
R181G
the mutation in the pro-domain region of the ADAM10 gene reduce alpha-secretase activity of the enzyme
DELTA672
-
a truncated soluble construct of ADAM10 lacking the transmembrane and cytosolic domains (truncation after Glu680), although correctly post-translationally processed and catalytically active with respect to a synthetic peptide substrate, is incapable of shedding cell-associated amyloid precursor protein (APP)
E384A
-
the point mutation which compromises the zinc-binding consensus motif, leads to a substantial decrease in amyloid precursor protein-alpha secretion
E385A
-
inactive
N439
-
mutation at the N-glycosylation site N439 increase ADAM10s susceptibility to proteolytical degradation
Q170H
R181G
S441A
-
the mutant displays higher susceptibility to proteolysis
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a C-terminal HA-tagged fusion protein is transfected in human ovarian cancer SKOV3 cells and human embryonic kidney HEK293 cells
-
ADAM10 is expressed as a wild-type protein and as a FLAG-tagged ADAM10 fusion protein in which the tag is inserted immediately C-terminal to the proprotein convertase recognition sequence RKKR. Expression is carried out by stable transfection of a human neuroblastoma SH-SY5Y cell line. Internally tagged ADAM10 fusion protein is easily detected in Western blot analysis. Catalytic activity of wild-type and internally tagged protein is indistinguishable
-
expressed in Escherichia coli
-
expressed in HUVEC and COS-7 cells
-
expressed in Ls174T human colon cancer cells
-
expressed in MEF cells and 293-T cells
-
expression in CHO cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is significantly elevated in nasopharyngeal carcinoma
the enzyme is upregulated at injury sites and in denervated areas of the brain following brain injury
ADAM10 mRNA is lowered in moderate to severe Alzheimer’s disease
-
amount and activity of ADAM10 is increased by application of low doses of statins
-
cultured HL-60 neutrophils exposed to tobacco smoke extract show increased enzyme content, cleavage of the molecule into its active form, and release of microvesicles carrying mature enzyme
-
enzyme levels are higher in sections from patients with anterior disk displacement with and without reduction compared to normal temporomandibular joint disks
-
retinoids induce gene expression of ADAM10. The vitamin A analog acitretin stimulates ADAM10 promoter activity with an EC50 of 0.0015 mM
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
patients with nasopharyngeal carcinoma with high expression of the enzyme have shorter overall survival rates
medicine
molecular biology
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vincent, B.; Paitel, E.; Saftig, P.; Frobert, Y.; Hartmann, D.; De Strooper, B.; Grassi, J.; Lopez-Perez, E.; Checler, F.
The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein
J. Biol. Chem.
276
37743-37746
2001
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Lopez-Perez, E.; Zhang, Y.; Frank, S.J.; Creemers, J.; Seidah, N.; Checler, F.
Constitutive a-secretase cleavage of the b-amyloid precursor protein in the furin-deficient LoVo cell line: involvement of the pro-hormone convertase 7 and the disintegrin metalloprotease ADAM10
J. Neurochem.
76
1532-1539
2001
Homo sapiens
Manually annotated by BRENDA team
Anders, A.; Gilbert, S.; Garten, W.; Postina, R.; Fahrenholz, F.
Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases
FASEB J.
15
1837-1839
2001
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Lemjabbar, H.; Basbaum, C.
Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells
Nat. Med.
8
41-46
2002
Homo sapiens
Manually annotated by BRENDA team
Gutwein, P.; Mechtersheimer, S.; Riedle, S.; Stoeck, A.; Gast, D.; Joumaa, S.; Zentgraf, H.; Fogel, M.; Altevogt, P.
ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles
FASEB J.
17
292-294
2003
Homo sapiens
Manually annotated by BRENDA team
Asai, M.; Hattori, C.; Szabo, B.; Sasagawa, N.; Maruyama, K.; Tanuma, S.I.; Ishiura, S.
Putative function of ADAM9, ADAM10, and ADAM17 as APP alpha-secretase
Biochem. Biophys. Res. Commun.
301
231-235
2003
Homo sapiens
Manually annotated by BRENDA team
Gatta, L.B.; Albertini, A.; Ravid, R.; Finazzi, D.
Levels of beta-secretase BACE and alpha-secretase ADAM10 mRNAs in Alzheimer hippocampus
NeuroReport
13
2031-2033
2002
Homo sapiens
Manually annotated by BRENDA team
Colciaghi, F.; Borroni, B.; Pastorino, L.; Marcello, E.; Zimmermann, M.; Cattabeni, F.; Padovani, A.; Di Luca, M.
alpha-secretase ADAM10 as well as aAPPs is reduced in platelets and CSF of Alzheimer Disease patients
Mol. Med.
8
67-74
2002
Homo sapiens
Manually annotated by BRENDA team
Yan, Y.; Shirakabe, K.; Werb, Z.
The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors
J. Cell Biol.
158
221-226
2002
Chlorocebus aethiops, Homo sapiens
Manually annotated by BRENDA team
Murai, T.; Miyauchi, T.; Yanagida, T.; Sako, Y.
Epidermal growth factor-regulated activation of Rac GTPase enhances CD44 cleavage by metalloproteinase disintegrin ADAM10
Biochem. J.
395
65-71
2006
Homo sapiens
Manually annotated by BRENDA team
McCulloch, D.R.; Akl, P.; Samaratunga, H.; Herington, A.C.; Odorico, D.M.
Expression of the disintegrin metalloprotease, ADAM-10, in prostate cancer and its regulation by dihydrotestosterone, insulin-like growth factor I, and epidermal growth factor in the prostate cancer cell model LNCaP
Clin. Cancer Res.
10
314-323
2004
Homo sapiens
Manually annotated by BRENDA team
Ludwig, A.; Hundhausen, C.; Lambert, M.H.; Broadway, N.; Andrews, R.C.; Bickett, D.M.; Leesnitzer, M.A.; Becherer, J.D.
Metalloproteinase inhibitors for the disintegrin-like metalloproteinases ADAM10 and ADAM17 that differentially block constitutive and phorbol ester-inducible shedding of cell surface molecules
Comb. Chem. High Throughput Screen.
8
161-171
2005
Homo sapiens
Manually annotated by BRENDA team
Allinson, T.M.; Parkin, E.T.; Condon, T.P.; Schwager, S.L.; Sturrock, E.D.; Turner, A.J.; Hooper, N.M.
The role of ADAM10 and ADAM17 in the ectodomain shedding of angiotensin converting enzyme and the amyloid precursor protein
Eur. J. Biochem.
271
2539-2547
2004
Homo sapiens
Manually annotated by BRENDA team
Zimmermann, M.; Gardoni, F.; Marcello, E.; Colciaghi, F.; Borroni, B.; Padovani, A.; Cattabeni, F.; Di Luca, M.
Acetylcholinesterase inhibitors increase ADAM10 activity by promoting its trafficking in neuroblastoma cell lines
J. Neurochem.
90
1489-1499
2004
Homo sapiens
Manually annotated by BRENDA team
Bandyopadhyay, S.; Hartley, D.M.; Cahill, C.M.; Lahiri, D.K.; Chattopadhyay, N.; Rogers, J.T.
Interleukin-1alpha stimulates non-amyloidogenic pathway by alpha-secretase (ADAM-10 and ADAM-17) cleavage of APP in human astrocytic cells involving p38 MAP kinase
J. Neurosci. Res.
84
106-118
2006
Homo sapiens
Manually annotated by BRENDA team
Uemura, K.; Kihara, T.; Kuzuya, A.; Okawa, K.; Nishimoto, T.; Ninomiya, H.; Sugimoto, H.; Kinoshita, A.; Shimohama, S.
Characterization of sequential N-cadherin cleavage by ADAM10 and PS1
Neurosci. Lett.
402
278-283
2006
Homo sapiens
Manually annotated by BRENDA team
Maretzky, T.; Reiss, K.; Ludwig, A.; Buchholz, J.; Scholz, F.; Proksch, E.; de Strooper, B.; Hartmann, D.; Saftig, P.
ADAM10 mediates E-cadherin shedding and regulates epithelial cell-cell adhesion, migration, and beta-catenin translocation
Proc. Natl. Acad. Sci. USA
102
9182-9187
2005
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Schramme, A.; Abdel-Bakky, M.S.; Kaempfer-Kolb, N.; Pfeilschifter, J.; Gutwein, P.
The role of CXCL16 and its processing metalloproteinases ADAM10 and ADAM17 in the proliferation and migration of human mesangial cells
Biochem. Biophys. Res. Commun.
370
311-316
2008
Homo sapiens
Manually annotated by BRENDA team
Ko, S.; Lin, S.; Wong, Y.; Liu, C.; Chang, K.; Liu, T.
Increase of disintegrin and metalloprotease 10 (ADAM10) expression in oral squamous cell carcinoma
Cancer Lett.
245
33-43
2007
Homo sapiens
Manually annotated by BRENDA team
Gavert, N.; Sheffer, M.; Raveh, S.; Spaderna, S.; Shtutman, M.; Brabletz, T.; Barany, F.; Paty, P.; Notterman, D.; Domany, E.; Ben-Zeev, A.
Expression of L1-CAM and ADAM10 in human colon cancer cells induces metastasis
Cancer Res.
67
7703-7712
2007
Homo sapiens
Manually annotated by BRENDA team
Smith, C.; Halvorsen, B.; Otterdal, K.; Waehre, T.; Yndestad, A.; Fevang, B.; Sandberg, W.J.; Breland, U.M.; Froland, S.S.; Oie, E.; Gullestad, L.; Damas, J.K.; Aukrust, P.
High levels and inflammatory effects of soluble CXC ligand 16 (CXCL16) in coronary artery disease: down-regulatory effects of statins
Cardiovasc. Res.
79
195-203
2008
Homo sapiens
Manually annotated by BRENDA team
Schulte, M.; Reiss, K.; Lettau, M.; Maretzky, T.; Ludwig, A.; Hartmann, D.; de Strooper, B.; Janssen, O.; Saftig, P.
ADAM10 regulates FasL cell surface expression and modulates FasL-induced cytotoxicity and activation-induced cell death
Cell Death Differ.
14
1040-1049
2007
Homo sapiens
Manually annotated by BRENDA team
Conrad, D.H.; Ford, J.W.; Sturgill, J.L.; Gibb, D.R.
CD23: an overlooked regulator of allergic disease
Curr. Allergy Asthma Rep.
7
331-337
2007
Homo sapiens
Manually annotated by BRENDA team
Hakulinen, J.; Keski-Oja, J.
ADAM10-mediated release of complement membrane cofactor protein during apoptosis of epithelial cells
J. Biol. Chem.
281
21369-21376
2006
Homo sapiens
Manually annotated by BRENDA team
Lemieux, G.A.; Blumenkron, F.; Yeung, N.; Zhou, P.; Williams, J.; Grammer, A.C.; Petrovich, R.; Lipsky, P.E.; Moss, M.L.; Werb, Z.
The low affinity IgE receptor (CD23) is cleaved by the metalloproteinase ADAM10
J. Biol. Chem.
282
14836-14844
2007
Homo sapiens
Manually annotated by BRENDA team
Martin, L.; Fluhrer, R.; Reiss, K.; Kremmer, E.; Saftig, P.; Haass, C.
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
J. Biol. Chem.
283
1644-1652
2008
Homo sapiens
Manually annotated by BRENDA team
Kaczur, V.; Puskas, L.G.; Nagy, Z.U.; Miled, N.; Rebai, A.; Juhasz, F.; Kupihar, Z.; Zvara, A.; Hackler, L.J.; Farid, N.R.
Cleavage of human thyrotropin receptor by ADAM10 is regulated by thyrotropin
J. Mol. Recognit.
20
392-404
2007
Homo sapiens (O14672), Homo sapiens
Manually annotated by BRENDA team
Dehmel, T.; Janke, A.; Hartung, H.P.; Goebel, H.H.; Wiendl, H.; Kieseier, B.C.
The cell-specific expression of metalloproteinase-disintegrins (ADAMs) in inflammatory myopathies
Neurobiol. Dis.
25
665-674
2007
Homo sapiens
Manually annotated by BRENDA team
Chen, C.D.; Podvin, S.; Gillespie, E.; Leeman, S.E.; Abraham, C.R.
Insulin stimulates the cleavage and release of the extracellular domain of Klotho by ADAM10 and ADAM17
Proc. Natl. Acad. Sci. USA
104
19796-19801
2007
Homo sapiens
Manually annotated by BRENDA team
Rapti, M.; Atkinson, S.J.; Lee, M.H.; Trim, A.; Moss, M.; Murphy, G.
The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition
Biochem. J.
411
433-439
2008
Homo sapiens
Manually annotated by BRENDA team
Escrevente, C.; Morais, V.A.; Keller, S.; Soares, C.M.; Altevogt, P.; Costa, J.
Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme
Biochim. Biophys. Acta
1780
905-913
2008
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Esselens, C.W.; Malapeira, J.; Colome, N.; Moss, M.; Canals, F.; Arribas, J.
Metastasis-associated C4.4A, a GPI-anchored protein cleaved by ADAM10 and ADAM17
Biol. Chem.
389
1075-1084
2008
Homo sapiens
Manually annotated by BRENDA team
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
Circ. Res.
102
1192-1201
2008
Homo sapiens
Manually annotated by BRENDA team
Raucci, A.; Cugusi, S.; Antonelli, A.; Barabino, S.M.; Monti, L.; Bierhaus, A.; Reiss, K.; Saftig, P.; Bianchi, M.E.
A soluble form of the receptor for advanced glycation endproducts (RAGE) is produced by proteolytic cleavage of the membrane-bound form by the sheddase a disintegrin and metalloprotease 10 (ADAM10)
FASEB J.
22
3716-3727
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Freese, C.; Garratt, A.N.; Fahrenholz, F.; Endres, K.
The effects of alpha-secretase ADAM10 on the proteolysis of neuregulin-1
FEBS J.
276
1568-1580
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Oh, S.T.; Schramme, A.; Stark, A.; Tilgen, W.; Gutwein, P.; Reichrath, J.
The disintegrin-metalloproteinases ADAM 10, 12 and 17 are upregulated in invading peripheral tumor cells of basal cell carcinomas
J. Cutan. Pathol.
36
395-401
2009
Homo sapiens
Manually annotated by BRENDA team
Arduise, C.; Abache, T.; Li, L.; Billard, M.; Chabanon, A.; Ludwig, A.; Mauduit, P.; Boucheix, C.; Rubinstein, E.; Le Naour, F.
Tetraspanins regulate ADAM10-mediated cleavage of TNF-alpha and epidermal growth factor
J. Immunol.
181
7002-7013
2008
Homo sapiens
Manually annotated by BRENDA team
Parkin, E.; Harris, B.
A disintegrin and metalloproteinase (ADAM)-mediated ectodomain shedding of ADAM10
J. Neurochem.
108
1464-1479
2009
Homo sapiens
Manually annotated by BRENDA team
Dehmel, T.; Goebel, H.H.; Hartung, H.P.; Lehmann, H.; Wiendl, H.; Kieseier, B.C.
The metalloproteinase-disintegrin ADAM10 is exclusively expressed by type I muscle fibers
Muscle Nerve
38
1049-1051
2008
Homo sapiens
Manually annotated by BRENDA team
Qin, W.; Ho, L.; Wang, J.; Peskind, E.; Pasinetti, G.M.
S100A7, a novel Alzheimers disease biomarker with non-amyloidogenic alpha-secretase activity acts via selective promotion of ADAM-10
PLoS ONE
4
e4183
2009
Homo sapiens
Manually annotated by BRENDA team
Riedle, S.; Kiefel, H.; Gast, D.; Bondong, S.; Wolterink, S.; Gutwein, P.; Altevogt, P.
Nuclear translocation and signalling of L1-CAM in human carcinoma cells requires ADAM10 and presenilin/gamma-secretase activity
Biochem. J.
420
391-402
2009
Homo sapiens
Manually annotated by BRENDA team
Dittmer, A.; Hohlfeld, K.; Luetzkendorf, J.; Mueller, L.P.; Dittmer, J.
Human mesenchymal stem cells induce E-cadherin degradation in breast carcinoma spheroids by activating ADAM10
Cell. Mol. Life Sci.
66
3053-3065
2009
Homo sapiens
Manually annotated by BRENDA team
Oh, S.T.; Cho, B.K.; Schramme, A.; Gutwein, P.; Tilgen, W.; Reichrath, J.
Hair-cycle dependent differential expression of ADAM 10 and ADAM 12: An immunohistochemical analysis in human hair follicles in situ
Dermatoendocrinol.
1
46-53
2009
Homo sapiens
Manually annotated by BRENDA team
Tippmann, F.; Hundt, J.; Schneider, A.; Endres, K.; Fahrenholz, F.
Up-regulation of the alpha-secretase ADAM10 by retinoic acid receptors and acitretin
FASEB J.
23
1643-1654
2009
Homo sapiens
Manually annotated by BRENDA team
Xu, D.; Sharma, C.; Hemler, M.E.
Tetraspanin12 regulates ADAM10-dependent cleavage of amyloid precursor protein
FASEB J.
23
3674-3681
2009
Homo sapiens
Manually annotated by BRENDA team
Endres, K.; Fahrenholz, F.
Upregulation of the alpha-secretase ADAM10--risk or reason for hope?
FEBS J.
277
1585-1596
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Kim, M.; Suh, J.; Romano, D.; Truong, M.H.; Mullin, K.; Hooli, B.; Norton, D.; Tesco, G.; Elliott, K.; Wagner, S.L.; Moir, R.D.; Becker, K.D.; Tanzi, R.E.
Potential late-onset Alzheimers disease-associated mutations in the ADAM10 gene attenuate {alpha}-secretase activity
Hum. Mol. Genet.
18
3987-3996
2009
Homo sapiens
Manually annotated by BRENDA team
Peng, M.; Guo, S.; Yin, N.; Xue, J.; Shen, L.; Zhao, Q.; Zhang, W.
Ectodomain shedding of Fcalpha receptor is mediated by ADAM10 and ADAM17
Immunology
130
83-91
2010
Homo sapiens
Manually annotated by BRENDA team
Ratchford, A.M.; Baker, O.J.; Camden, J.M.; Rikka, S.; Petris, M.J.; Seye, C.I.; Erb, L.; Weisman, G.A.
P2Y2 nucleotide receptors mediate metalloprotease-dependent phosphorylation of epidermal growth factor receptor and ErbB3 in human salivary gland cells
J. Biol. Chem.
285
7545-7555
2010
Homo sapiens
Manually annotated by BRENDA team
Jacobsen, K.T.; Adlerz, L.; Multhaup, G.; Iverfeldt, K.
Insulin-like growth factor-1 (IGF-1)-induced processing of amyloid-beta precursor protein (APP) and APP-like protein 2 is mediated by different metalloproteinases
J. Biol. Chem.
285
10223-10231
2010
Homo sapiens
Manually annotated by BRENDA team
Endres, K.; Fahrenholz, F.
Regulation of alpha-secretase ADAM10 expression and activity
Exp. Brain Res.
2011
1-10
2011
Homo sapiens
-
Manually annotated by BRENDA team
Bouillot, S.; Tillet, E.; Carmona, G.; Prandini, M.H.; Gauchez, A.S.; Hoffmann, P.; Alfaidy, N.; Cand, F.; Huber, P.
Protocadherin-12 cleavage is a regulated process mediated by ADAM10 protein: evidence of shedding up-regulation in pre-eclampsia
J. Biol. Chem.
286
15195-15204
2011
Homo sapiens
Manually annotated by BRENDA team
Blume, K.E.; Soeroes, S.; Keppeler, H.; Stevanovic, S.; Kretschmer, D.; Rautenberg, M.; Wesselborg, S.; Lauber, K.
Cleavage of annexin A1 by ADAM10 during secondary necrosis generates a monocytic find-me signal
J. Immunol.
188
135-145
2012
Homo sapiens
Manually annotated by BRENDA team
Hogl, S.; Kuhn, P.H.; Colombo, A.; Lichtenthaler, S.F.
Determination of the proteolytic cleavage sites of the amyloid precursor-like protein 2 by the proteases ADAM10, BACE1 and gamma-secretase
PLoS ONE
6
e21337
2011
Homo sapiens
Manually annotated by BRENDA team
Nagara, Y.; Hagiyama, M.; Hatano, N.; Futai, E.; Suo, S.; Takaoka, Y.; Murakami, Y.; Ito, A.; Ishiura, S.
Tumor suppressor cell adhesion molecule 1 (CADM1) is cleaved by a disintegrin and metalloprotease 10 (ADAM10) and subsequently cleaved by gamma-secretase complex
Biochem. Biophys. Res. Commun.
417
462-467
2012
Homo sapiens (O14672)
Manually annotated by BRENDA team
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
Biochem. Pharmacol.
91
510-521
2014
Homo sapiens (O14672), Homo sapiens
Manually annotated by BRENDA team
Breshears, L.M.; Schlievert, P.M.; Peterson, M.L.
A disintegrin and metalloproteinase 17 (ADAM17) and epidermal growth factor receptor (EGFR) signaling drive the epithelial response to Staphylococcus aureus toxic shock syndrome toxin-1 (TSST-1)
J. Biol. Chem.
287
32578-32587
2012
Homo sapiens (O14672), Homo sapiens
Manually annotated by BRENDA team
Minond, D.; Cudic, M.; Bionda, N.; Giulianotti, M.; Maida, L.; Houghten, R.; Fields, G.
Discovery of novel inhibitors of a disintegrin and metalloprotease 17 (ADAM17) using glycosylated and non-glycosylated substrates
J. Biol. Chem.
287
36473-36487
2012
Homo sapiens (O14672)
Manually annotated by BRENDA team
Hofmann, S.; Vgtle, T.; Bender, M.; Rose-John, S.; Nieswandt, B.
The SLAM family member CD84 is regulated by ADAM10 and calpain in platelets
J. Thromb. Haemost.
10
2581-2592
2012
Homo sapiens (O14672), Mus musculus (O35598)
Manually annotated by BRENDA team
Shitomi, Y.; Thogersen, I.; Ito, N.; Leitinger, B.; Enghild, J.; Itoh, Y.
ADAM10 controls collagen signaling and cell migration on collagen by shedding the ectodomain of discoidin domain receptor 1 (DDR1)
Mol. Biol. Cell
26
659-673
2015
Homo sapiens (O14672)
Manually annotated by BRENDA team
Raikwar, N.; Liu, K.; Thomas, C.
N-terminal cleavage and release of the ectodomain of Flt1 is mediated via ADAM10 and ADAM 17 and regulated by VEGFR2 and the Flt1 intracellular domain
PLoS ONE
9
e112794
2014
Homo sapiens (O14672)
Manually annotated by BRENDA team
Loreto, C.; Chiarenza, G.P.; Musumeci, G.; Castrogiovanni, P.; Imbesi, R.; Ruggeri, A.; Almeida, L.E.; Leonardi, R.
ADAM10 localization in temporomandibular joint disk with internal derangement an ex vivo immunohistochemical study
Acta Histochem.
118
293-298
2016
Homo sapiens
Manually annotated by BRENDA team
von Hoven, G.; Rivas, A.J.; Neukirch, C.; Klein, S.; Hamm, C.; Qin, Q.; Meyenburg, M.; Fueser, S.; Saftig, P.; Hellmann, N.; Postina, R.; Husmann, M.
Dissecting the role of ADAM10 as a mediator of Staphylococcus aureus alpha-toxin action
Biochem. J.
473
1929-1940
2016
Homo sapiens (O14672), Homo sapiens
Manually annotated by BRENDA team
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
Biochem. Pharmacol.
91
510-521
2015
Homo sapiens (O14672), Homo sapiens
Manually annotated by BRENDA team
Vincent, B.
Regulation of the alpha-secretase ADAM10 at transcriptional, translational and post-translational levels
Brain Res. Bull.
126
154-169
2016
Homo sapiens (O14672)
Manually annotated by BRENDA team
You, B.; Shan, Y.; Shi, S.; Li, X.; You, Y.
Effects of ADAM10 upregulation on progression, migration, and prognosis of nasopharyngeal carcinoma
Cancer Sci.
106
1506-1514
2015
Homo sapiens (O14672), Homo sapiens
Manually annotated by BRENDA team
Endres, K.; Deller, T.
Regulation of alpha-secretase ADAM10 in vitro and in vivo Genetic, epigenetic, and protein-based mechanisms
Front. Mol. Neurosci.
10
56
2017
Homo sapiens (O14672), Homo sapiens
Manually annotated by BRENDA team
Siney, E.J.; Holden, A.; Casselden, E.; Bulstrode, H.; Thomas, G.J.; Willaime-Morawek, S.
Metalloproteinases ADAM10 and ADAM17 mediate migration and differentiation in glioblastoma sphere-forming cells
Mol. Neurobiol.
54
3893-3905
2017
Homo sapiens (O14672), Homo sapiens
Manually annotated by BRENDA team
Madoux, F.; Dreymuller, D.; Pettiloud, J.P.; Santos, R.; Becker-Pauly, C.; Ludwig, A.; Fields, G.B.; Bannister, T.; Spicer, T.P.; Cudic, M.; Scampavia, L.D.; Minond, D.
Discovery of an enzyme and substrate selective inhibitor of ADAM10 using an exosite-binding glycosylated substrate
Sci. Rep.
6
11
2016
Homo sapiens (O14672)
Manually annotated by BRENDA team
Riethmueller, S.; Ehlers, J.C.; Lokau, J.; Duesterhoeft, S.; Knittler, K.; Dombrowsky, G.; Groetzinger, J.; Rabe, B.; Rose-John, S.; Garbers, C.
Cleavage site localization differentially controls interleukin-6 receptor proteolysis by ADAM10 and ADAM17
Sci. Rep.
6
25550
2016
Homo sapiens (O14672)
Manually annotated by BRENDA team
Folkesson, M.; Li, C.; Frebelius, S.; Swedenborg, J.; Wagsaeter, D.; Williams, K.J.; Eriksson, P.; Roy, J.; Liu, M.L.
Proteolytically active ADAM10 and ADAM17 carried on membrane microvesicles in human abdominal aortic aneurysms
Thromb. Haemost.
114
1165-1174
2015
Homo sapiens
Manually annotated by BRENDA team