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ERVK-6 — PLAU
Text-mined interactions from Literome
List et al., Biochemistry 2000
:
The
pro-uPA converting activity of the mGK-6 enzyme, as well as its ability to cleave a synthetic substrate for glandular kallikrein, was
inhibited by the serine proteinase inhibitor leupeptin but not by other serine
proteinase inhibitors such as aprotinin, antithrombin III, or alpha ( 1 ) -antitrypsin
Inuzuka et al., J Surg Res 2000
(Carcinoma...) :
The following activation mechanism for
proteinase might occur :
uPA coexpressed with MMP-9
activated plasminogen, and plasmin activated proMMP-3, which was secreted depending upon inflammatory infiltration, and then MMP-3 activated proMMP-9, resulting in colorectal cancer progression and metastasis