Antoine Pilon
Pasteur Institute
Network
Latest external collaboration on country level. Dive into details by clicking on the dots.
Publication
Featured researches published by Antoine Pilon.
Arteriosclerosis, Thrombosis, and Vascular Biology | 2000
Antoine Pilon; Olivier Briand; Sophie Lestavel; Corinne Copin; Zouher Majd; Jean-Charles Fruchart; Graciela Castro; Véronique Clavey
Apolipoproteins of high density lipoprotein (HDL) and especially apolipoprotein (apo)AI and apoAII have been demonstrated as binding directly to the class B type I scavenger receptor (SR-BI), the HDL receptor that mediates selective cholesteryl ester uptake. However, the functional relevance of the binding capacity of each apolipoprotein is still unknown. The human adrenal cell line, NCI-H295R, spontaneously expresses a high level of SR-BI, the major apoAI binding protein in these cells. As previously described for murine SR-BI, free apoAI, palmitoyl-oleoyl-phosphatidylcholine (POPC)-AI, and HDL are good ligands for human SR-BI. In vitro displacement of apoAI by apoAII in HDLs or in Lp AI purified from HDL by immunoaffinity enhances their ability to compete with POPC-AI to bind to SR-BI and also enhances their direct binding capacity. The next step was to determine whether the higher affinity of apoAII for SR-BI correlated with the specific uptake of cholesteryl esters from these HDLs. Free apoAII and, to a lesser extent, free apoAI that were added to the cell medium during uptake experiments inhibited the specific uptake of [(3)H]cholesteryl esters from HDL, indicating that binding sites on cells were the same as cholesteryl ester uptake sites. In direct experiments, the uptake of [(3)H]cholesteryl esters from apoAII-enriched HDL was highly reduced compared with the uptake from native HDL. These results demonstrate that in the human adrenal cell line expressing SR-BI as the major HDL binding protein, efficient apoAII binding has an inhibitory effect on the delivery of cholesteryl esters to cells.
Diabetes | 2007
Maria del Carmen Carmona; Katie Louche; Bruno Lefebvre; Antoine Pilon; Nathalie Hennuyer; Véronique Audinot-Bouchez; Catherine Fievet; Gérard Torpier; Pierre Formstecher; Pierre Renard; Philippe Lefebvre; Catherine Dacquet; Bart Staels; Louis Casteilla; Luc Pénicaud
OBJECTIVE—Rosiglitazone displays powerful antidiabetes benefits but is associated with increased body weight and adipogenesis. Keeping in mind the concept of selective peroxisome proliferator–activated receptor (PPAR)γ modulator, the aim of this study was to characterize the properties of a new PPARγ ligand, S 26948, with special attention in body-weight gain. RESEARCH DESIGN AND METHODS—We used transient transfection and binding assays to characterized the binding characteristics of S 26948 and GST pull-down experiments to investigate its pattern of coactivator recruitment compared with rosiglitazone. We also assessed its adipogenic capacity in vitro using the 3T3-F442A cell line and its in vivo effects in ob/ob mice (for antidiabetes and antiobesity properties), as well as the homozygous human apolipoprotein E2 knockin mice (E2-KI) (for antiatherogenic capacity). RESULTS—S 26948 displayed pharmacological features of a high selective ligand for PPARγ with low potency in promoting adipocyte differentiation. It also displayed a different coactivator recruitment profile compared with rosiglitazone, being unable to recruit DRIP205 or PPARγ coactivator-1α. In vivo experiments showed that S 26948 was as efficient in ameliorating glucose and lipid homeostasis as rosiglitazone, but it did not increase body and white adipose tissue weights and improved lipid oxidation in liver. In addition, S 26948 represented one of the few molecules of the PPARγ ligand class able to decrease atherosclerotic lesions. CONCLUSIONS—These findings establish S 26948 as a selective PPARγ ligand with distinctive coactivator recruitment and gene expression profile, reduced adipogenic effect, and improved biological responses in vivo.
Archive | 2002
Antoine Pilon; Hélène Duez; Jean-Charles Fruchart; Bart Staels
Peroxisome proliferator-activated receptors (PPARs) are a subfamily of nuclear receptors comprising 3 isotypes, PPARα, β/δ, and γ, which control a variety of cellular functions such as lipid and lipoprotein metabolism, fatty acid oxidation, glucose metabolism, adipogenesis, and cellular differentiation. Moreover, emerging data suggest that, besides their role in regulating metabolic risk factors for cardiovascular diseases, PPARs are involved in the control of vascular inflammation and thrombogenicity related to atherosclerosis. This review will focus on recent developments on the role of PPARα and γ in this field.
Journal of Biological Chemistry | 2004
Philippe Gervois; Robert Kleemann; Antoine Pilon; Frédéric Percevault; Wolfgang Koenig; Bart Staels; Teake Kooistra
FEBS Journal | 1999
Geneviève Martin; Antoine Pilon; Caroline Albert; Michel Valle; Dean W. Hum; Jean-Charles Fruchart; Jamila Najib; Véronique Clavey; Bart Staels
Journal of Biological Chemistry | 2002
Stéphanie Bultel-Brienne; Sophie Lestavel; Antoine Pilon; Isabelle Laffont; Anne Tailleux; Jean-Charles Fruchart; Gérard Siest; Véronique Clavey
Biochemical Pharmacology | 2001
Didier Junquero; Antoine Pilon; Elizabeth Carilla-Durand; Jean-Francois Patoiseau; Jean-Pierre Tarayre; Gérard Torpier; Bart Staels; Jean-Charles Fruchart; Francis C. Colpaert; Véronique Clavey; André Delhon
Atherosclerosis | 1999
A. Delhon; D. Junquero; Antoine Pilon; E. Carilla-Durand; J.-F. Patoiseau; J.-P. Tarayre; Véronique Clavey; Bart Staels; Jean-Charles Fruchart; F.C. Colpaert
Atherosclerosis | 1999
Véronique Clavey; Antoine Pilon; M. Bouly; Olivier Briand; Sophie Lestavel; Corinne Copin; Jean-Charles Fruchart
Atherosclerosis | 1999
Sophie Lestavel; Olivier Briand; Antoine Pilon; Corinne Copin; Jean-Charles Fruchart; J.C. Fruchart; Gérard Torpier; Véronique Clavey