A new function of calphobindin I (annexin V)
作者： Hiroshi NAKAO , Masanao WATANABE , Masahiro MAKI
DOI: 10.1111/J.1432-1033.1994.TB19067.X
关键词:
摘要: Calphobindin I (CPB-I, annexin V) is an anticoagulant protein purified from human placenta; it a member of the family that binds phospholipids in calcium-dependent manner. In this study, we discovered and examined new function CPB-I: promotion both migration urokinase-type plasminogen activator (uPA) activity normal keratinocytes (NHK). While treatment NHK with 10-μg/ml concentration CPB-I for 24 h or 48 caused approximate 30% increase (compared no treatment), was inhibited when anti-CPB-I monoclonal antibodies (i.e. A46 A180) were added along CPB-I. Moreover, while greater than 10 μg/ml significant secreted uPA, reflected approximately 40% cell migration, uPA by cycloheximide antibodies. This seen 8 after addition Specific binding to had Kd value 95.2 nM (equivalent 3.2 μg/ml), also However, effect on proliferation. Furthermore, enhanced reepithelialization applied locally twice day full-thickness cutaneous wounds made male rats. Our results show that, during injury, helps through synthesis without stimulating their
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