References of "Oury, Cécile"
     in
Bookmark and Share    
Full Text
Peer Reviewed
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)

Detailed reference viewed: 8 (2 ULg)
Full Text
Peer Reviewed
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)

Detailed reference viewed: 7 (1 ULg)
Full Text
Peer Reviewed
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 ▲]

Detailed reference viewed: 25 (2 ULg)
Full Text
Peer Reviewed
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 ▲]

Detailed reference viewed: 14 (4 ULg)
Full Text
Peer Reviewed
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

Detailed reference viewed: 11 (1 ULg)
Full Text
Peer Reviewed
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

Detailed reference viewed: 10 (2 ULg)
Full Text
Peer Reviewed
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

Detailed reference viewed: 8 (2 ULg)
Full Text
Peer Reviewed
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

Detailed reference viewed: 14 (4 ULg)
Full Text
Peer Reviewed
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.

Detailed reference viewed: 2 (0 ULg)
Full Text
Peer Reviewed
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 ▲]

Detailed reference viewed: 7 (2 ULg)
Full Text
Peer Reviewed
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.

Detailed reference viewed: 14 (1 ULg)
Peer Reviewed
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)

Detailed reference viewed: 12 (1 ULg)
Peer Reviewed
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)

Detailed reference viewed: 8 (1 ULg)
Full Text
Peer Reviewed
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 ▲]

Detailed reference viewed: 27 (0 ULg)
Full Text
Peer Reviewed
See detailA natural dominant negative P2X1 receptor due to deletion of a single amino acid residue.
Oury, Cécile ULg; Toth-Zsamboki, Emese; Van Geet, Chris et al

in Journal of Biological Chemistry (2000)

We describe a naturally occurring dominant negative P2X1 mutant. This mutant lacks one leucine within a stretch of four leucine residues in its second transmembrane domain (TM2) (amino acids 351-354 ... [more ▼]

We describe a naturally occurring dominant negative P2X1 mutant. This mutant lacks one leucine within a stretch of four leucine residues in its second transmembrane domain (TM2) (amino acids 351-354). Confocal microscopy revealed proper plasma membrane localization of the mutant in stably transfected HEK293 cells. Nevertheless, voltage-clamped HEK293 cells expressing mutated P2X1 channels failed to develop an ATP or ADP-induced current. Furthermore, when co-expressed with the wild type receptor in Xenopus oocytes, the mutated protein exhibited a dose-dependent dominant negative effect on the normal ATP or ADP-induced P2X1 channel activity. These data indicate that deletion of a single apolar amino acid residue at the inner border of the P2X1 TM2 generates a nonfunctional channel. [less ▲]

Detailed reference viewed: 15 (0 ULg)
Peer Reviewed
See detailCongenital deficiency of the phospholipase C coupled P2Y1 receptor leads to a mild bleeding disorder.
Oury, Cécile ULg; Lenaerts, Tim; Peerlinck, Kathelijn et al

in Thrombosis and Haemostasis (1999)

Detailed reference viewed: 20 (1 ULg)
Peer Reviewed
See detailA dominant negative mutation in the P2X1 receptor causes a severe bleeding disorder.
Oury, Cécile ULg; Toth-Zsamboki, Emese; Van Geet, Chris et al

in Blood (1999)

Detailed reference viewed: 7 (0 ULg)
Full Text
Peer Reviewed
See detailTEL is a sequence-specific transcriptional repressor.
Lopez, Rodolphe; Carron, Clémence; Oury, Cécile ULg et al

in Journal of Biological Chemistry (1999)

TEL is a gene frequently involved in specific chromosomal translocations in human leukemia and sarcoma that encodes a member of the ETS family of transcriptional regulators. TEL is unusual among other ETS ... [more ▼]

TEL is a gene frequently involved in specific chromosomal translocations in human leukemia and sarcoma that encodes a member of the ETS family of transcriptional regulators. TEL is unusual among other ETS proteins by its ability to self-associate in vivo, a property that is essential to the oncogenic activation of TEL-derived fusion proteins. We show here that TEL is a sequence-specific transcriptional repressor of ETS-binding site-driven transcription of model and natural promoters. [less ▲]

Detailed reference viewed: 4 (0 ULg)
Full Text
Peer Reviewed
See detailA domain of TEL conserved in a subset of ETS proteins defines a specific oligomerization interface essential to the mitogenic properties of the TEL-PDGFR beta oncoprotein.
Jousset, C.; Carron, C.; Boureux, A. et al

in EMBO Journal (1997)

TEL is a novel member of the ETS family of transcriptional regulators which is frequently involved in human leukemias as the result of specific chromosomal translocations. This study shows that the amino ... [more ▼]

TEL is a novel member of the ETS family of transcriptional regulators which is frequently involved in human leukemias as the result of specific chromosomal translocations. This study shows that the amino-terminal domain conserved in a subset of the ETS proteins has evolved to generate a specialized protein-protein interaction interface which is likely to be an important determinant of their specificity as transcriptional regulators. [less ▲]

Detailed reference viewed: 5 (0 ULg)