3.4.24.81: ADAM10 endopeptidase
This is an abbreviated version!
For detailed information about ADAM10 endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.81
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3.4.24.81
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alzheimer
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adam17
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amyloid
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ectodomain
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sheddase
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alpha-secretase
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endothelial
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metalloproteases
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neuroprotective
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plaque
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amyloidogenic
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non-amyloidogenic
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tnf
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sh-sy5y
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synaptic
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secretase
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membrane-anchored
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tetraspanins
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gamma-secretase
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n-cadherin
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presenilins
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notch1
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intramembrane
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abeta
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cxcl16
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prpc
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prion
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amyloid-beta
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prodomains
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psen1
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beta-secretase
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sappalpha
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hb-egf
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beta-site
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trans-signaling
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amphiregulin
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fractalkine
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meprin
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disintegrin-like
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adam17-mediated
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app-cleaving
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betacellulin
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nicastrin
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timp-3
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molecular biology
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anti-amyloidogenic
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medicine
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srage
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notch-dependent
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ad-like
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juxtamembrane
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bace-1
- 3.4.24.81
- alzheimer
- adam17
-
amyloid
- ectodomain
- sheddase
- alpha-secretase
- endothelial
- metalloproteases
-
neuroprotective
- plaque
-
amyloidogenic
-
non-amyloidogenic
- tnf
-
sh-sy5y
- synaptic
-
secretase
-
membrane-anchored
- tetraspanins
- gamma-secretase
- n-cadherin
-
presenilins
- notch1
-
intramembrane
- abeta
- cxcl16
- prpc
- prion
- amyloid-beta
- prodomains
- psen1
- beta-secretase
-
sappalpha
- hb-egf
-
beta-site
-
trans-signaling
- amphiregulin
- fractalkine
- meprin
-
disintegrin-like
-
adam17-mediated
-
app-cleaving
- betacellulin
-
nicastrin
- timp-3
- molecular biology
-
anti-amyloidogenic
- medicine
-
srage
-
notch-dependent
-
ad-like
-
juxtamembrane
- bace-1
Reaction
endopeptidase of broad specificity =
Synonyms
a disintegrin and metalloprotease 10, a disintegrin and metalloproteinase 10, a disintegrin and metalloproteinase-10, a-disintegrin-and-metalloprotease 10, AD10, ADAM 10, ADAM-10, ADAM10, CD156c, CD23 metalloprotease, HsT18717, kuz, kuzbanian, Kuzbanian protein, MADM, 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
ECTree
3.4.24.81 ADAM10 endopeptidaseAdvanced search results
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results (Source Tissue
Source Tissue on EC 3.4.24.81 - ADAM10 endopeptidase
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
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A-172 cell line has potent alpha-secretase activity, higher than HEK-293 cell line
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N-Cadherin cleavage occurs at a higher level in glioblastoma cells than in non-neoplastic astrocytes
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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
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COS7 cell line transfected with ADAM10 produces transactivation of epidermal growth factor receptor
both ADAM10 and ADAM17, EC 3.4.24.86, are present during all stages of spermatogenesis
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
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human mesenchymal stem cells interfere with cellcell adhesion and enhance migration of breast cancer cells by activating ADAM10
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acinar cell during embryogenesis, endocrinic cell and exocrinic cell in adult
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ADAM10 is necessary for epidermal growth factor receptor transactivation
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cell line LNCaP, localized to the secretory cells of prostate glands, with additional basal cell expression in benign glands
both ADAM10 and ADAM17, EC 3.4.24.86, are present during all stages of spermatogenesis
both ADAM10 and ADAM17, EC 3.4.24.86, are present during all stages of spermatogenesis. Protein level and cell surface localization strongly dropp in Dark segments as compared with the rest of the segments
additional information
ADAM10 specifically localizes in the CD31+ endothelial cells in normal human cardiac tissues and in cultured primary arterial endothelial cells
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ADAM17-/-, Ras-Myc-immortalized murine fibroblasts. ADAM10 is a major TNF sheddase in ADAM17-deficient fibroblasts
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U-1242 MG, N-Cadherin cleavage occurs at a higher level in glioblastoma cells than in non-neoplastic astrocytes
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in the adult intestine, ADAM10 is abundantly expressed on the basolateral cell surface of all intestinal epithelial cells
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epidermal hair follicle infundibulum, keratinocytes of the hair infundibulum do not show any difference as compared to keratinocytes of the normal epidermis
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ADAMs9 and 10 are the most prominent collagen XVII sheddases in primary keratinocytes
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LoVo cell line does not express furin protease has both the immature and mature form of the enzyme
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by immunohistochemistry, ADAM10 is shown to stain human muscle fibers exclusively. Neither satellite cells nor capillaries exhibit any positive immunoreactivity. Histochemical staining with ATPase reveals a colocalization of positive ADAM10 immunoreactivity to type I fibers only, whereas the staining pattern for ADAM10 never matches with the presence of type II fibers
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cytoplasmic expression of ADAM 10 is observed in the hair bulb keratinocytes and fibroblasts of dermal papilla in anagen IIII hair follicles. Decreased ADAM 10 expression is observed in the hair matrix keratinocytes as compared to the hair bulb keratinocytes in anagen IIII 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
additional information
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endothelial cells of venules and arterioles do not express ADAM10
