References of "Oury, Cécile"
     in
Bookmark and Share    
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: 7 (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: 13 (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: 26 (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: 14 (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)
Full Text
Peer Reviewed
See detailThe TEL gene products: nuclear phosphoproteins with DNA binding properties.
Poirel, H.; Oury, Cécile ULg; Carron, Clémence et al

in Oncogene (1997)

The human TEL gene is involved in several 12p13 chromosomal abnormalities present in various human hematological malignancies, the most frequent being the t(12;21)(p13;q22), specific for childhood acute ... [more ▼]

The human TEL gene is involved in several 12p13 chromosomal abnormalities present in various human hematological malignancies, the most frequent being the t(12;21)(p13;q22), specific for childhood acute lymphoblastic leukemia. The predicted product of TEL harbours an amino acid region similar to the ETS DNA binding domain. We now report the isolation of the murine TEL cDNA and the characterization of the human TEL proteins. Human and murine TEL proteins are particularly homologous within their aminoterminal regions and their ETS domains. TEL proteins are nuclear and display specific DNA binding activity toward classical ETS binding sites. In addition, we show that TEL mRNAs initiate translation at either of the two first inframe ATGs (codon 1 and 43) to encode 50 kDa and 57 kDa TEL proteins. In vivo, each of these primary translational products is modified by multiple phosphorylation events. [less ▲]

Detailed reference viewed: 2 (0 ULg)
Peer Reviewed
See detailA one-nucleotide difference in a cAMP and phorbol ester response element leads to differential regulation of the human chorionic somatomammotropin A and B gene transcription
Oury, Cécile ULg; Alsat, E.; Jacquemin, P. et al

in Journal of Molecular Endocrinology (1997), 18(2), 87-99

Human chorionic somatomammotropin (hCS) is encoded by two highly related genes, hCS-A and hCS-B, located in the hGH/hCS gene locus. Both genes are expressed in the syncytiotrophoblast layer of the ... [more ▼]

Human chorionic somatomammotropin (hCS) is encoded by two highly related genes, hCS-A and hCS-B, located in the hGH/hCS gene locus. Both genes are expressed in the syncytiotrophoblast layer of the placenta and hCS release from trophoblast cells is known to be increased by cAMP and phorbol esters. However, it remains unclear whether this regulation acts at the level of hCS gene expression or secretion and whether both genes are affected. We examined the effects of cAMP and phorbol 12-myristate 13-acetate (PMA) on the transcription of the hCS-A and hCS-B genes. Transient expression experiments revealed a 7 bp cAMP- and PMA-responsive element (CRElhCS-A) spanning nucleotides-1102 to -1096 upstream of the hCS-A gene. In contrast, the homologous sequence upstream of hCS-B (CRElhCS-B), differing from CRElhCS-A by a single substitution, shows little or no response to cAMP. In band-shift assays, the CRElhCS-A oligonucleotide was shown to bind two factors related to CREBP and AP-1, whereas CRElhCS-B only competes for one of these complexes. Finally, Southwestern analysis revealed that the CRElhCS-A element binds two ubiquitous proteins of 100 kDa and 47 kDa respectively, whereas CRElhCS-B interacts only with the 47 kDa protein. Taken together, these results suggest that a 47 kDa protein binding to the CRElhCS-A and CRElhCS-B elements is involved in the PMA response of the hCS-A and hCS-B genes, and a 100 kDa protein plays a crucial role in cAMP regulation of the hCS-A gene. [less ▲]

Detailed reference viewed: 23 (4 ULg)
Peer Reviewed
See detailThe enhancers of the human placental lactogen B, A, and L genes: progressive activation during in vitro trophoblast differentiation and importance of the DF-3 element in determining their respective activities
Jacquemin, P.; Alsat, E.; Oury, Cécile ULg et al

in DNA & Cell Biology (1996), 15(10), 845-54

The hCS-A and hCS-B genes encoding human chorionic somatomammotropin and the related hCS-L gene are very similar in their coding and flanking sequences. For each of these genes, downstream enhancers ... [more ▼]

The hCS-A and hCS-B genes encoding human chorionic somatomammotropin and the related hCS-L gene are very similar in their coding and flanking sequences. For each of these genes, downstream enhancers, varying in strength, have been identified with the help of cytotrophoblast-derived JEG-3 cells, which do not express the hCS genes. Here we study the activity of the hCS enhancers in human syncytiotrophoblast in primary culture, which naturally expresses the hCS genes. We show that the activity of the hCS-B gene enhancer is mediated by two elements, DF-3 and DF-4, whereas the hCS-L and hCS-A gene enhancers display weaker activity due to mutations in their respective DF-3 sites. Replacement of the hCS-B DF-3 site with the homologous hCS-A sequence causes hCS-B enhancer activity to decrease. Primary cytotrophoblasts differentiate in culture to form the syncytiotrophoblast. We show that during this process the production of hCS progressively increases and that concomitantly all three hCS enhancers are progressively activated. A targeted mutation in the 3' part of the DF-4 element abolishes the binding of a protein present only in syncytiotrophoblast extracts and inactivates the DF-4 element. Thus, a direct correlation exists between the appearance of this syncytiotrophoblast-specific protein and hCS enhancer activity. This primary culture model proves useful in studying the regulation of the hCS genes. [less ▲]

Detailed reference viewed: 22 (6 ULg)