Jacques Chanard
Centre national de la recherche scientifique
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Publication
Featured researches published by Jacques Chanard.
American Journal of Human Genetics | 2005
Qing Ling Duan; Borzoo Nikpoor; Marie-Pierre Dubé; Giuseppe Molinaro; Inge A. Meijer; Patrick A. Dion; Daniel Rochefort; Judith Saint-Onge; Leah Flury; Nancy J. Brown; James V. Gainer; Jean L. Rouleau; Angelo Agostoni; Massimo Cugno; Pierre Simon; Pierre Clavel; Jacky Potier; Bassem Wehbe; Seddik Benarbia; Julien MarcAurele; Jacques Chanard; Tatiana Foroud; Albert Adam; Guy A. Rouleau
Angiotensin I-converting enzyme inhibitors (ACEi), which are used to treat common cardiovascular diseases, are associated with a potentially life-threatening adverse reaction known as angioedema (AE-ACEi). We have previously documented a significant association between AE-ACEi and low plasma aminopeptidase P (APP) activity. With eight large pedigrees, we hereby demonstrate that this quantitative trait is partially regulated by genetic factors. We tested APP activity using a variance-component QTL analysis of a 10-cM genomewide microsatellite scan enriched with seven markers over two candidate regions. We found significant linkage (LOD = 3.75) to a locus that includes the XPNPEP2 candidate gene encoding membrane-bound APP. Mutation screening of this QTL identified a large coding deletion segregating in one pedigree and an upstream single-nucleotide polymorphism (C-2399A SNP), which segregates in the remaining seven pedigrees. Measured genotype analysis strongly suggests that the linkage signal for APP activity at this locus is accounted for predominantly by the SNP association. In a separate case-control study (20 cases and 60 controls), we found significant association of this SNP to ACEi-induced AE (P=.0364). In conclusion, our findings provide supporting evidence that the C-2399A variant in XPNPEP2 is associated with reduced APP activity and a higher incidence of AE-ACEi.
Biochemical Journal | 2008
Fatouma Touré; J.M. Zahm; Roselyne Garnotel; Elise Lambert; Noël Bonnet; Ann Marie Schmidt; Fabien Vitry; Jacques Chanard; Philippe Gillery; Philippe Rieu
AGEs (advanced glycation end-products) accumulate in collagen molecules during uraemia and diabetes, two diseases associated with high susceptibility to bacterial infection. Because neutrophils bind to collagen during their locomotion in extravascular tissue towards the infected area we investigated whether glycoxidation of collagen (AGE-collagen) alters neutrophil migration. Type I collagen extracted from rat tail tendons was used for in vitro glycoxidation (AGE-collagen). Neutrophils were obtained from peripheral blood of healthy adult volunteers and were used for the in vitro study of adhesion and migration on AGE- or control collagen. Glycoxidation of collagen increased adhesion of neutrophils to collagen surfaces. Neutrophil adhesion to AGE-collagen was inhibited by a rabbit anti-RAGE (receptor for AGEs) antibody and by PI3K (phosphoinositide 3-kinase) inhibitors. No effect was observed with ERK (extracellular-signal-regulated kinase) or p38 MAPK (mitogen-activated protein kinase) inhibitors. AGE-collagen was able to: (i) induce PI3K activation in neutrophils, and (ii) inhibit chemotaxis and chemokinesis of chemoattractant-stimulated neutrophils. Finally, we found that blocking RAGE with anti-RAGE antibodies or inhibiting PI3K with PI3K inhibitors restored fMLP (N-formylmethionyl-leucyl-phenylalanine)-induced neutrophil migration on AGE-collagen. These results show that RAGE and PI3K modulate adhesion and migration rate of neutrophils on AGE-collagen. Modulation of adhesiveness may account for the change in neutrophil migration rate on AGE-collagen. As neutrophils rely on their ability to move to perform their function as the first line of defence against bacterial invasion, glycoxidation of collagen may participate in the suppression of normal host defence in patients with diabetes and uraemia.
Nephrologie & Therapeutique | 2010
Jacques Chanard; Michel Thomas; Philippe Rieu
The molecular process that occurs at the interface between blood and a haemodialysis membrane determines the host response. The resulting reactions define the degree of membrane biocompatibility. These reactions are triggered by plasma protein adsorption onto the membrane and blood cell stress. Over the past decade, atomic force microscopy (AFM) has provided mechanistic insights into the molecular level of interactions that occur at the biomaterial surface. AFM provides tridimentional images produced by both changes in applied shear nanoforces and dynamic imaging through the molecular analysis of attraction and repulsion forces. The aim of the present brief review is to shortly present the technique of AFM and its emerging applications in haemodialysis, comparing hydrophilic and hydrophobic structures. Dialysis membrane roughness and protein adsorption mapping can be quantitatively estimated, since AFM resolution power is in the range of a nanometer. It is suggested that estimation of roughness and force mapping determining structure/function relationship should be proposed for the best understanding of membrane biocompatibility.
Nephrology Dialysis Transplantation | 2003
Jacques Chanard; Sylvie Lavaud; Christine Randoux; Philippe Rieu
Biomaterials | 2008
Anik Désormeaux; Marie Eve Moreau; Yves Lepage; Jacques Chanard; Albert Adam
Nephrology Dialysis Transplantation | 1990
P. Bindi; Sylvie Lavaud; B. Bernieh; Olivier Toupance; Jacques Chanard
Nephrology Dialysis Transplantation | 1997
C Hanrotel; Sylvie Lavaud; Olivier Toupance; P Lebon; Jacques Chanard
Nephrology Dialysis Transplantation | 1989
Jacques Chanard; Olivier Toupance; Sylvie Lavaud; Frederic Jaisser; Philippe Gillery
Nephrologie & Therapeutique | 2008
Jacques Chanard
Nephrologie & Therapeutique | 2010
Jacques Chanard; Michel Thomas; Philippe Rieu