Trypsin induced von Willebrand factor release from human endothelial cells in mediated by PAR-2 activation.
Nystedt and co-workers cloned in 1994 a second protease activatable receptor (PAR-2) that could be activated by trypsin but not by thrombin (1). In this study, we investigated whether trypsin induced stimulation of endothelial cells is linked to PAR-2 activation. We have found by mRNA analysis that endothelial cells of venous and arterial origin express both protease activatable receptors. The functional thrombin receptor and the protease activated receptor-2 (PAR-2) mediate apparently the same effects in human vascular endothelial cells. Both, the activation of the thrombin receptor with thrombin or SFLLRN and the activation of the PAR-2 with trypsin or SLIGRL induced intracellular calcium mobilisation and a subsequent release of von Willebrand factor (vWf) from Weibel-Palade bodies. As a consequence, it can be concluded that endothelial cells have two different receptors mediating the same cellular responses after activation.
Storck
J
J
Institute of Vegetative Physiology, University of Münster, Germany.
Küsters
B
B
Vahland
M
M
Morys-Wortmann
C
C
Zimmermann
E R
ER
D002478:Cells, Cultured; D004730:Endothelium, Vascular / Q000378:metabolism*; D006801:Humans; D044464:Receptor, PAR-2; D011956:Receptors, Cell Surface / Q000378:metabolism*; D015398:Signal Transduction; D014357:Trypsin / Q000494:pharmacology*; D014841:von Willebrand Factor / Q000378:metabolism*
D044464:Receptor, PAR-2; D011956:Receptors, Cell Surface; D014841:von Willebrand Factor; D014357:Trypsin