5 results on '"Cécile Oury"'
Search Results
2. Platelet Acetyl-CoA Carboxylase Phosphorylation
- Author
-
Shakeel Kautbally, MD, Sophie Lepropre, PhD, Marie-Blanche Onselaer, PhD, Astrid Le Rigoleur, MD, Audrey Ginion, MS, Christophe De Meester de Ravenstein, PhD, Jerome Ambroise, PhD, Karim Z. Boudjeltia, PhD, Marie Octave, MS, Odile Wéra, MS, Alexandre Hego, BSc, Joël Pincemail, PhD, Jean-Paul Cheramy-Bien, Thierry Huby, PhD, Martin Giera, PhD, Bernhard Gerber, MD, PhD, Anne-Catherine Pouleur, MD, PhD, Bruno Guigas, PhD, Jean-Louis Vanoverschelde, MD, PhD, Joelle Kefer, MD, PhD, Luc Bertrand, PhD, Cécile Oury, PhD, Sandrine Horman, PhD, and Christophe Beauloye, MD, PhD
- Subjects
Diseases of the circulatory (Cardiovascular) system ,RC666-701 - Abstract
Summary: Adenosine monophosphate–activated protein kinase (AMPK) acetyl-CoA carboxylase (ACC) signaling is activated in platelets by atherogenic lipids, particularly by oxidized low-density lipoproteins, through a CD36-dependent pathway. More interestingly, increased platelet AMPK–induced ACC phosphorylation is associated with the severity of coronary artery calcification as well as acute coronary events in coronary artery disease patients. Therefore, AMPK–induced ACC phosphorylation is a potential marker for risk stratification in suspected coronary artery disease patients. The inhibition of ACC resulting from its phosphorylation impacts platelet lipid content by down-regulating triglycerides, which in turn may affect platelet function. Key Words: AMPK, acetyl-CoA carboxylase, coronary artery disease, lipidomics, platelet
- Published
- 2019
- Full Text
- View/download PDF
3. Soluble GPVI is elevated in injured patients: shedding is mediated by fibrin activation of GPVI
- Author
-
Samantha J. Montague, Céline Delierneux, Christelle Lecut, Nathalie Layios, Robert J. Dinsdale, Christine S.-M. Lee, Natalie S. Poulter, Robert K. Andrews, Peter Hampson, Christopher M. Wearn, Nathalie Maes, Jonathan Bishop, Amy Bamford, Chris Gardiner, Woei Ming Lee, Tariq Iqbal, Naiem Moiemen, Steve P. Watson, Cécile Oury, Paul Harrison, and Elizabeth E. Gardiner
- Subjects
Specialties of internal medicine ,RC581-951 - Abstract
Abstract: Soluble glycoprotein VI (sGPVI) is shed from the platelet surface and is a marker of platelet activation in thrombotic conditions. We assessed sGPVI levels together with patient and clinical parameters in acute and chronic inflammatory conditions, including patients with thermal injury and inflammatory bowel disease and patients admitted to the intensive care unit (ICU) for elective cardiac surgery, trauma, acute brain injury, or prolonged ventilation. Plasma sGPVI was measured by enzyme-linked immunosorbent assay and was elevated on day 14 after thermal injury, and was higher in patients who developed sepsis. sGPVI levels were associated with sepsis, and the value for predicting sepsis was increased in combination with platelet count and Abbreviated Burn Severity Index. sGPVI levels positively correlated with levels of D-dimer (a fibrin degradation product) in ICU patients and patients with thermal injury. sGPVI levels in ICU patients at admission were significantly associated with 28- and 90-day mortality independent of platelet count. sGPVI levels in patients with thermal injury were associated with 28-day mortality at days 1, 14, and 21 when adjusting for platelet count. In both cohorts, sGPVI associations with mortality were stronger than D-dimer levels. Mechanistically, release of GPVI was triggered by exposure of platelets to polymerized fibrin, but not by engagement of G protein-coupled receptors by thrombin, adenosine 5′-diphosphate, or thromboxane mimetics. Enhanced fibrin production in these patients may therefore contribute to the observed elevated sGPVI levels. sGPVI is an important platelet-specific marker for platelet activation that predicts sepsis progression and mortality in injured patients.
- Published
- 2018
- Full Text
- View/download PDF
4. Purinergic control of inflammation and thrombosis: Role of P2X1 receptors
- Author
-
Cécile Oury, Christelle Lecut, Alexandre Hego, Odile Wéra, and Céline Delierneux
- Subjects
Thrombosis ,Inflammation ,P2X receptor ,Biotechnology ,TP248.13-248.65 - Abstract
Inflammation shifts the hemostatic mechanisms in favor of thrombosis. Upon tissue damage or infection, a sudden increase of extracellular ATP occurs, that might contribute to the crosstalk between inflammation and thrombosis. On platelets, P2X1 receptors act to amplify platelet activation and aggregation induced by other platelet agonists. These receptors critically contribute to thrombus stability in small arteries. Besides platelets, studies by our group indicate that these receptors are expressed by neutrophils. They promote neutrophil chemotaxis, both in vitro and in vivo. In a laser-induced injury mouse model of thrombosis, it appears that neutrophils are required to initiate thrombus formation and coagulation activation on inflamed arteriolar endothelia. In this model, by using P2X1−/− mice, we recently showed that P2X1 receptors, expressed on platelets and neutrophils, play a key role in thrombus growth and fibrin generation. Intriguingly, in a model of endotoxemia, P2X1−/− mice exhibited aggravated oxidative tissue damage, along with exacerbated thrombocytopenia and increased activation of coagulation, which translated into higher susceptibility to septic shock. Thus, besides its ability to recruit neutrophils and platelets on inflamed endothelia, the P2X1 receptor also contributes to limit the activation of circulating neutrophils under systemic inflammatory conditions. Taken together, these data suggest that P2X1 receptors are involved in the interplay between platelets, neutrophils and thrombosis. We propose that activation of these receptors by ATP on neutrophils and platelets represents a new mechanism that regulates thrombo-inflammation.
- Published
- 2015
- Full Text
- View/download PDF
5. Platelet Acetyl-CoA Carboxylase Phosphorylation
- Author
-
Audrey Ginion, Luc Bertrand, Christophe de Meester de Ravenstein, Jean-Louis Vanoverschelde, Anne-Catherine Pouleur, Odile Wéra, Jérôme Ambroise, Bruno Guigas, Christophe Beauloye, M. Octave, Jean Paul Cheramy-Bien, Cécile Oury, Bernhard Gerber, Astrid Le Rigoleur, Marie-Blanche Onselaer, Karim K.Z. Boudjeltia, Joël Pincemail, Alexandre Hego, S. Kautbally, Thierry Huby, Martin Giera, Joelle Kefer, Sandrine Horman, and S. Lepropre
- Subjects
0301 basic medicine ,medicine.medical_specialty ,lcsh:Diseases of the circulatory (Cardiovascular) system ,business.industry ,Acetyl-CoA carboxylase ,AMPK ,030204 cardiovascular system & hematology ,medicine.disease ,Adenosine ,Pyruvate carboxylase ,Coronary artery disease ,03 medical and health sciences ,030104 developmental biology ,0302 clinical medicine ,Endocrinology ,lcsh:RC666-701 ,Internal medicine ,Medicine ,Phosphorylation ,Platelet ,Cardiology and Cardiovascular Medicine ,Protein kinase A ,business ,medicine.drug - Abstract
Summary: Adenosine monophosphate–activated protein kinase (AMPK) acetyl-CoA carboxylase (ACC) signaling is activated in platelets by atherogenic lipids, particularly by oxidized low-density lipoproteins, through a CD36-dependent pathway. More interestingly, increased platelet AMPK–induced ACC phosphorylation is associated with the severity of coronary artery calcification as well as acute coronary events in coronary artery disease patients. Therefore, AMPK–induced ACC phosphorylation is a potential marker for risk stratification in suspected coronary artery disease patients. The inhibition of ACC resulting from its phosphorylation impacts platelet lipid content by down-regulating triglycerides, which in turn may affect platelet function. Key Words: AMPK, acetyl-CoA carboxylase, coronary artery disease, lipidomics, platelet
- Published
- 2019
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.