TAILIEUCHUNG - Báo cáo khoa học: Functional hierarchy of plasminogen kringles 1 and 4 in fibrinolysis and plasmin-induced cell detachment and apoptosis

Plasmin(ogen) kringles 1 and 4 are involved in anchorage of plasmin(ogen) to fibrin and cells, an essential step in fibrinolysis and pericellular proteo-lysis. Their contribution to these processes was investigated by selective neutralization of their lysine-binding function. Blocking the kringle 1 lysine-binding site with monoclonal antibody 34D3 fully abolished binding and activation of Glu-plasminogen and prevented both fibrinolysis and plasmin-induced cell detachment-induced apoptosis. | ềFEBS Journal Functional hierarchy of plasminogen kringles 1 and 4 in fibrinolysis and plasmin-induced cell detachment and apoptosis Benoĩt Ho-Tin-Noe1 Gertrudis Rojas2 Roger Vranckx1 H. Roger Lijnen3 and Eduardo Angles-Cano1 1 INSERM U698 Centre Hospitalier Universitaire Bichat-Claude Bernard Paris France 2 Center for Genetic Engineering and Biotechnology Havana Cuba 3 Center for Molecular and Vascular Biology Katholieke Universiteit Leuven Campus Gasthuisberg Leuven Belgium Keywords cell detachment-induced apoptosis extracellular matrix proteolysis fibrinolysis lysine-binding site plasminogen activation Correspondence E. Angles-Cano INSERM U698 CHU Bichat-Claude Bernard 46 rue Henri Huchard F-75877-Cdx Paris 18 France Fax 33 1 40 25 86 10 Tel 33 1 40 25 86 11 E-mail angles@ Received 30 March 2005 revised 5 May 2005 accepted 9 May 2005 doi Plasmin ogen kringles 1 and 4 are involved in anchorage of plasmin ogen to fibrin and cells an essential step in fibrinolysis and pericellular proteolysis. Their contribution to these processes was investigated by selective neutralization of their lysine-binding function. Blocking the kringle 1 lysine-binding site with monoclonal antibody 34D3 fully abolished binding and activation of Glu-plasminogen and prevented both fibrinolysis and plasmin-induced cell detachment-induced apoptosis. In contrast blocking the kringle 4 lysine-binding site with monoclonal antibody did not impair its activation although it partially inhibited plasmin ogen binding fibrinolysis and cell detachment. This remarkable biologically relevant distinctive response was not observed for plasmin or Lys-plasminogen each antibody inhibited their binding and activation of Lys-plasminogen to a limited extent and full inhibition of fibrinolysis required simultaneous neutralization of both kringles. Thus in Lys-plasminogen and plasmin kringles 1 and 4 act as independent and complementary domains both able to .

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