3.4.24.B28: ADAM15
This is an abbreviated version!
For detailed information about ADAM15, go to the full flat file.
Word Map on EC 3.4.24.B28
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3.4.24.B28
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metalloprotease
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ectodomains
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metalloprotease-disintegrins
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rgd-dependent
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metargidin
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medicine
- 3.4.24.B28
- metalloprotease
- ectodomains
-
metalloprotease-disintegrins
-
rgd-dependent
- metargidin
- medicine
Reaction
proteolysis of proteins =
Synonyms
a disintegrin and metalloproteinase 15, ADAM15 endopeptidase, ADAM15 isoforms i1, ADAM15 isoforms i2, ADAM15 isoforms i3, ADAM15 isoforms i4, ADAM15 isoforms i5, ADAM15 isoforms i6
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medicine
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ADAM15 ranks in the top 5% of amplified genes and its mRNA is significantly overexpressed in invasive and metastatic bladder cancer compared to noninvasive disease. In metastatic samples, increased ADAM15 immunoreactivity is associated with increasing cancer stage and exhibits significantly stronger staining. The knockdown of ADAM15 mRNA expression significantly inhibits bladder tumor cell migration and reduces the invasive capacity of bladder tumor cells through MatrigelTM and monolayers of vascular endothelium. The knockdown of ADAM15 in a human xenograft model of bladder cancer inhibits tumor growth by 45% compared to controls
medicine
high expression of ADAM15 is associated with decreased overall survival and disease-free survival in non-small cell lung cancer (NSCLC) patients. shRNA-mediated knockdown of ADAM15 attenuates cell migration and invasion. ADAM15 upregulates MMP9 expression in lung cancer cells via activation of the MEK-ERK pathway. ADAM15 proteolytically cleaves and activates pro-MMP9 in vitro and interacts with MMP9 in vivo. Overexpression of ADAM15 in A-549 cells promotes cell invasion, while knocking down MMP9 attenuates cell invasive ability