[HTML][HTML] Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease
SL Lee, RB Dickson, CY Lin - Journal of Biological Chemistry, 2000 - ASBMB
Matriptase is an epithelial-derived, integral membrane serine protease. The enzyme was
initially isolated from human breast cancer cells and has been implicated in breast cancer
invasion and metastasis. In the current study, using active matriptase isolated from human
milk, we demonstrate that matriptase is able to cleave various synthetic substrates with
arginine or lysine as their P1 sites and prefers small side chain amino acids, such as Ala
and Gly, at P2 sites. For the most reactive substrates, N-tert-butoxycarbonyl (Nt-Boc)-γ …
initially isolated from human breast cancer cells and has been implicated in breast cancer
invasion and metastasis. In the current study, using active matriptase isolated from human
milk, we demonstrate that matriptase is able to cleave various synthetic substrates with
arginine or lysine as their P1 sites and prefers small side chain amino acids, such as Ala
and Gly, at P2 sites. For the most reactive substrates, N-tert-butoxycarbonyl (Nt-Boc)-γ …