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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