References of "Oury, Cécile"
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See detailATP Augments von Willebrand Factor-dependent Shear-induced Platelet Aggregation through Ca2+-Calmodulin and Myosin Light Chain Kinase Activation
Oury, Cécile ULg; Sticker, Elsie; Cornelissen, Heidi et al

in Journal of Biological Chemistry (2004)

Shear stress triggers von Willebrand factor (VWF) binding to platelet glycoprotein Ibalpha and subsequent integrin alpha(IIb)beta(3)-dependent platelet aggregation. Concomitantly, nucleotides are released ... [more ▼]

Shear stress triggers von Willebrand factor (VWF) binding to platelet glycoprotein Ibalpha and subsequent integrin alpha(IIb)beta(3)-dependent platelet aggregation. Concomitantly, nucleotides are released from plateletdense granules, and ADP is known to contribute to shear-induced platelet aggregation (SIPA). This study shows that ATP also contributes to SIPA. The ATP-gated P2X(1) ion channel induces MLC-mediated cytoskeletal rearrangements that increases platelet degranulation during VWF-triggered platelet activation. [less ▲]

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See detailFacilitating roles of murine platelet glycoprotein Ib and alphaIIbbeta3 in phosphatidylserine exposure during vWF-collagen-induced thrombus formation.
Kuijpers, Marijke; Schulte, V.; Oury, Cécile ULg et al

in Journal of Physiology (2004)

This work indicates that, under physiological conditions of flow, both adhesive receptors GPIb and alphaIIbbeta3 facilitate GPVI-mediated PS exposure by stabilizing platelet binding to collagen. Hence ... [more ▼]

This work indicates that, under physiological conditions of flow, both adhesive receptors GPIb and alphaIIbbeta3 facilitate GPVI-mediated PS exposure by stabilizing platelet binding to collagen. Hence, these glycoproteins have an assistant procoagulant role in collagen-dependent thrombus formation, which is most prominent at reduced GPVI activity and is independent of the presence of thrombin. [less ▲]

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See detailOverexpression of the platelet P2X1 ion channel in transgenic mice generates a novel prothrombotic phenotype.
Oury, Cécile ULg; Kuijpers, Marijke; Toth-Zsamboki, Emese et al

in Journal of Thrombosis and Haemostasis (2003)

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See detailP2X1-mediated ERK2 activation amplifies the collagen-induced platelet secretion by enhancing myosin light chain kinase activation.
Oury, Cécile ULg; Toth-Zsamboki, Emese; Cornelissen, Heidi et al

in Journal of Biological Chemistry (2003)

This study shows that, at low doses of collagen, glycoprotein VI activation leads to early protein kinase C- and MLC kinase-dependent platelet degranulation. Rapidly released ATP triggers P2X1 -mediated ... [more ▼]

This study shows that, at low doses of collagen, glycoprotein VI activation leads to early protein kinase C- and MLC kinase-dependent platelet degranulation. Rapidly released ATP triggers P2X1 -mediated Ca2+ influx, activating ERK2, in turn amplifying platelet secretion by reinforcing the early MLC kinase phosphorylation. Hence, the P2X1-ERK2-MLC axis contributes to collagen-induced platelet activation by enhancing platelet degranulation. [less ▲]

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See detailThe platelet purinergic receptors
Oury, Cécile ULg; Hoylaerts, Marc

Book published by Leuven University Press (2003)

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See detailGlycoprotein Ib and integrin alphaIIbbeta3 contribute to GPVI-dependent vWF-collagen induced thrombus formation under flow
Kuijpers, Marijke; Oury, Cécile ULg; Schulte, V. et al

in Journal of Thrombosis and Haemostasis [=JTH] (2003)

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See detailP2X1-induced activation of Ca2+ calmodulin leads to myosin light chain and ERK2 phosphorylation in human platelets.
Toth-Zsamboki, Emese; Oury, Cécile ULg; De Vos, Rita et al

in Journal of Thrombosis and Haemostasis [=JTH] (2003)

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See detailOverexpression of the platelet P2X1 ion channel in transgenic mice generates a novel prothrombotic phenotype.
Oury, Cécile ULg; Kuijpers, Marijke; Toth-Zsamboki, Emese et al

in Blood (2003)

This study describes transgenic mice overexpressing the human P2X(1) ion channel in the megakaryocytic cell lineage. Platelets from these mice display increased secretion and aggregation evoked by low ... [more ▼]

This study describes transgenic mice overexpressing the human P2X(1) ion channel in the megakaryocytic cell lineage. Platelets from these mice display increased secretion and aggregation evoked by low doses of collagen, convulxin, or the thromboxane A(2) mimetic U46619. Perfusing whole blood from transgenic mice over collagen fibers at a shear rate of 1000 seconds(-1) resulted in increased P2X(1)-dependent aggregate formation and phosphatidylserine exposure. Platelet hyperreactivity to collagen was correlated with up-regulated extracellular signal-regulated kinase 2 (ERK2) phosphorylation. In a viscometer, shear stress caused potent aggregation of transgenic platelets under conditions in which wild-type platelets did not aggregate. In an in vivo model of thromboembolism consisting of intravenous injection of a low dose of collagen plus epinephrine, transgenic mice died more readily than wild-type mice. Preinjection of U0126 not only fully protected transgenic mice against thrombosis, it also enhanced the survival of wild-type mice injected with a higher collagen dose. Hence, the platelet P2X(1) ion channel plays a role in hemostasis and thrombosis through its participation in collagen-, thromboxane A(2)-, and shear stress-triggered platelet responses. Activation of the ERK2 pathway is instrumental in these processes. [less ▲]

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See detailThe intracellular tyrosine residues of the ATP-gated P2X(1) ion channel are essential for its function.
Oury, Cécile ULg; Toth-Zsamboki, Emese; Watanabe, Hiroyuki et al

in FEBS Letters (2002)

In this study, we mutated the four highly conserved intracellular tyrosine residues of the P2X(1) ion channel were mutated into phenylalanine. Simultaneous electrophysiological and calcium measurements in ... [more ▼]

In this study, we mutated the four highly conserved intracellular tyrosine residues of the P2X(1) ion channel were mutated into phenylalanine. Simultaneous electrophysiological and calcium measurements in transfected human embryonic kidney (HEK 293) cells indicated that Y362F and Y370F mutants were non-functional, despite their proper plasma membrane expression. The Y16F and Y363F mutants retained 2.2% and 26% of the wild-type P2X(1) activity, respectively. However, no tyrosine phosphorylation was detected on Western blots of P2X(1) immunoprecipitates derived either from HEK 293 cell lysates or from human platelets, expressing P2X(1) endogenously. Thus, Y16, Y362, Y363 and Y370 are required for the appropriate three-dimensional structure and function of the intracellular P2X(1) domains. [less ▲]

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See detailCa2+ influx via the platelet P2X1 ion channel contributes to collagen-induced platelet activation.
Hoylaerts, Marc; Oury, Cécile ULg; Toth-Zsamboki, Emese et al

in Haematologica (2002), 87

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See detailP2X1-mediated activation of Ca2+-calmodulin leads to myosin light chain and ERK2 phosphorylation in human platelets.
Toth-Zsamboki, Emese; Oury, Cécile ULg; De Vos, Rita et al

in Haematologica (2002), 87

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See detailIncreased platelet reactivity to collagen in transgenic mice overexpressing the P2X1 ion channel.
Oury, Cécile ULg; Kuijpers, marijke; Toth-Zsamboki, Emese et al

in Haematologica (2002), 87

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See detailEnhanced Platelet Reactivity to Collagen and Shear Stress in Transgenic Mice Overexpressing the Platelet P2X1 Ion Channel
Oury, Cécile ULg; Kuijpers, Marijke; Toth-Zsamboki, Emese et al

in Blood (2002), 100

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See detailDoes the P(2X1del) variant lacking 17 amino acids in its extracellular domain represent a relevant functional ion channel in platelets?
Oury, Cécile ULg; Toth-Zsamboki, Emese; Vermylen, Jos et al

in Blood (2002)

In this letter, we questionned the existence of a ADP responsive P2X1 protein variant in platelets.

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See detailP2X(1)-mediated activation of extracellular signal-regulated kinase 2 contributes to platelet secretion and aggregation induced by collagen.
Oury, Cécile ULg; Toth-Zsamboki, Emese; Vermylen, Jos et al

in Blood (2002)

This study shows that mild platelet stimulation with collagen rapidly releases ATP, which activates the P2X(1)-PKC-ERK2 pathway. This process enhances further degranulation of the collagen-primed granules ... [more ▼]

This study shows that mild platelet stimulation with collagen rapidly releases ATP, which activates the P2X(1)-PKC-ERK2 pathway. This process enhances further degranulation of the collagen-primed granules allowing platelet aggregation to be completed. [less ▲]

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See detailThe P2Y1 receptor antagonist adenosine-2',5'-diphosphate non-selectively antagonizes the platelet P2X1 ion channel.
Oury, Cécile ULg; Toth-Zsamboki, Emese; Tytgat, Jan et al

in Thrombosis and Haemostasis (2001)

This letter indicates a lack of specificity of a platelet P2Y1 receptor antagonist.

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See detailRapid Ca2+ influx via the platelet P2X1 ion channel requires its N- and C-terminal tyrosine phosphorylation.
Oury, Cécile ULg; Toth-Zsamboki, Emese; Nilius, Bernd et al

in Thrombosis and Haemostasis (2001)

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See detailThe P2X1 ion channel in platelets acts as a functional receptor for ATP and is weakly antagonized by ADP.
Oury, Cécile ULg; Toth-Zsamboki, Emese; Thys, Chantal et al

in Thrombosis and Haemostasis (2001)

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See detailThe ATP-gated P2X1 ion channel acts as a positive regulator of platelet responses to collagen.
Oury, Cécile ULg; Toth-Zsamboki, Emese; Thijs, Chantal et al

in Thrombosis and Haemostasis (2001)

This study shows that, during collagen-initiated platelet activation, the early secretion of ATP results in the activation of the P2X1 ion channel, which plays a role as a positive regulator of further ... [more ▼]

This study shows that, during collagen-initiated platelet activation, the early secretion of ATP results in the activation of the P2X1 ion channel, which plays a role as a positive regulator of further platelet responses. [less ▲]

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