Protease-mediated human smooth muscle cell proliferation by urokinase requires epidermal growth factor receptor transactivation by triple membrane signaling
作者： Enrico A. Duru , Yuyang Fu , Mark G. Davies
DOI: 10.1016/J.JSS.2014.06.054
关键词:
摘要: Abstract Background Urokinase (uPA) modulates cellular and extracellular matrix responses within the microenvironment of vessel wall has been shown to activate epidermal growth factor receptor (EGFR). This study examines role protease domain uPA during EGFR activation in human vascular smooth muscle cells (VSMC). Methods Human coronary VSMC were cultured in vitro. Assays cell proliferation phosphorylation examined response carboxyterminal fragment (CTF) presence absence plasmin, metalloprotease a disintegrin metalloproteinase (ADAM) inhibitors, heparin-bound (HB-EGF), small interfering RNA ADAMs. Results CTF produced dose-dependent increase DNA synthesis VSMC, which was blocked manner by both plasmin inhibitors inhibitor, AG1478. induced time-dependent phosphorylation, metalloproteinases activity. The urokinase plasminogen activator not required. Inhibition ADAM-10 -12, HB-EGF CTF. CTF-mediated mediated through Gβγ, src, NAD(P)H oxidase. Conclusions In induces uPAR-independent, domain-dependent transactivation plasmin-mediated, ADAM-induced, HB-EGF–dependent process, is intracellular pathways involving Gαi,
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