References of "Grandfils, Christian"
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See detailDPSC colonization of functionalized 3D textiles
Ortiz, Marine; Rosales-Ibáñez, R; Pozos-Guillén, A. et al

in Journal of Biomedical Materials Research, Part B : Applied Biomaterials (in press)

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See detailTailored made degradable synthetic polymers for 3D (bio)printing
Grandfils, Christian ULg

Conference (2016, January 26)

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See detailComparison of commercial membranes tailored as 3D in vitro cell models
Romano, Ilaria ULg; Tilkin, Rémi ULg; Hubaux, Roland et al

Poster (2016)

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See detailSynthesis of hydrophilic CuInS2/ZnS quantum dots with different polymeric shells and study of their cytotoxicity and hemocompatibility
Speranskaya, Elena Sergeevna; Sevrin, Chantal ULg; De Saeger, Sarah et al

in ACS Applied Materials and Interfaces (2016)

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See detailIn vitro and in vivo evaluation of drug-eluting microspheres designed for transarterial chemoembolization therapy
Wang, Y.; Molin, D.; Sevrin, Chantal ULg et al

in International Journal of Pharmaceutics (2016), 503

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See detailStudy of cell growth on/in modified polymer matrices as scaffolds for tissue engineering
Markvicheva, E.; Drozdova, M.; Demina, T. et al

Poster (2016)

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See detailPolylactide-based microspheres prepared using solid-state copolymerized chitosan and D,L-lactide
Demina, Tatiana; Akopova, T.A.; Vladimirov, L.V. et al

in Materials Science and Engineering: A (2016), C59

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See detailHighly Luminescent Aqueous Ag2S Quantum Dots as New Generation Quantum Dots
Yağcı Acar, Havva Funda; Hocaoğlu, I.; Demir, F. et al

in Proceediing of the meeting (2015, March 09)

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See detailPolymeric synthetic antidote
Grandfils, Christian ULg; Sevrin, Chantal ULg; Flebus, Luca ULg

Patent (2015)

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See detailProduction of extracellular polysaccharide by Enterobacter A47 using cheese whey as the sole carbon source
Antunes, S.; Alves, V.D.; Grandfils, Christian ULg et al

in Proceeding of the meeting (2015, January 19)

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See detailCharacterization of the chitin-glucan complex extracted from Komagataella pastoris cell wall
Farinha, I.; Duarte, P.; Pimentel et al

in Proceeding of the meeting (2015, January 19)

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See detailLow molecular weight poly (2-dimethylamino ethylmethacrylate) polymers with controlled positioned fluorescent labeling: Synthesis, characterization and in vitro interaction with human endothelial cells.
Flebus, Luca ULg; Lombart, François ULg; Sevrin, Chantal et al

in International journal of pharmaceutics (2015), 478(1), 278-287

Poly (2-dimethylamino ethylmethacrylate) (PDMAEMA) is an attractive non-degradable polymer studied as nonviral vector for gene delivery but it can be also adopted for delivery of other biopharmaceutical ... [more ▼]

Poly (2-dimethylamino ethylmethacrylate) (PDMAEMA) is an attractive non-degradable polymer studied as nonviral vector for gene delivery but it can be also adopted for delivery of other biopharmaceutical drugs. As a parenteral carrier, the PDMAEMA free form (FF) might interact with tissues and cells. Few data are available on its selective internalization and efflux from cells, while the majority of studies published have followed the distribution of DNA complexed with PDMAEMA. In order to address polycation safety, the first aim was to synthesize by atom transfer radical polymerisation (ATRP) fluorescent labeled PDMAEMA of low molecular weight (Mw) (below 15kDa), controlling the position and density of fluorescein. The second goal was to analyze the possible difference in uptake and subcellular distribution of this labeled FF polycation between human umbilical vein endothelial cells (HUVEC) and hCMEC/D3 cells. These two cell lines have been chosen in order to detect selectivity towards the blood-brain barrier (BBB). In both cases, polycation was detected along the plasma membrane followed by progressive migration to the peri-nuclear region, where it overlapped with lysosomal structures. The analysis by fluorescence-activated cell sorting (FACS) of the PDMAEMA uptake by hCMEC/D3 cells showed a significant (p<0.05) inhibition (40%) in presence of 2-dexoxy-d-glucose inhibitor, a result supporting an energy-dependence mechanism(s). Cytotoxicity study showed that low Mw PDMAEMA (10kDa) lead to a minor cytotoxicity compared to the higher ones. As main conclusion this study highlights the similitude in cell trafficking of FF PDMAEMA and data previously reported for PDMAEMA/DNA complexes. [less ▲]

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See detailCyto/hemocompatible magnetic hybrid nanoparticles (Ag2SFe3O4) with luminesceence in the near-infrared region as promising theranostic materials
Hocaoglu, I.; Asik, A.; Ulusoy, U. et al

in Colloids and Surfaces B : Biointerfaces (2015), 133

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See detailDeficiency in mouse hyaluronidase 2: a new mechanism of chronic thrombotic microangiopathy.
Onclinx, Cecile; Dogne, Sophie; Jadin, Laurence et al

in Haematologica (2015)

Hyaluronan is a major component of the extracellular matrix and glycocalyx. Its main somatic degrading enzymes are the hyaluronidases 1 and 2, none of which is active in the bloodstream. We generated ... [more ▼]

Hyaluronan is a major component of the extracellular matrix and glycocalyx. Its main somatic degrading enzymes are the hyaluronidases 1 and 2, none of which is active in the bloodstream. We generated hyaluronidase 2 deficient mice. They suffer from mild chronic anemia and thrombocytopenia, in parallel with a 10-fold increase in plasma hyaluronan concentration. The current study explores the mechanism of these hematological anomalies. The decreased erythrocyte and platelet counts were assigned to peripheral consumption. The erythrocyte half-life was reduced from 25 to 8 days without signs of premature aging. Hyaluronidase 2 deficient platelets were functional. Major intrinsic defects in erythrocyte membrane or stability, as well as detrimental effects of high hyaluronan levels on erythrocytes, were ruled out in vitro. Normal erythrocytes transfused into hyaluronidase 2 deficient mice were quickly destroyed but neither splenectomy nor anti-C5 administration prevented from chronic hemolysis. Schistocytes were present in hyaluronidase 2 deficient smears at a level of 1 to 6%, while virtually absent in control mice. Hyaluronidase 2 deficient mice had increased markers of endothelial damage and microvascular fibrin deposition, without renal failure, accumulation of ultra-large multimers of von Willebrand factor, deficiency of A Disintegrin And Metalloproteinase with ThromboSpondin type 1 motifs, member 13 (ADAMTS13), or hypertension. There was no sign of structural damage in hepatic or splenic sinusoids, or in any other microvessels. We conclude that hyaluronidase 2 deficiency induces chronic thrombotic microangiopathy with hemolytic anemia in mice. The link between this uncommon condition and hyaluronidase 2 remains to be explored in man. [less ▲]

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See detailMICROCARRIERS LOADED WITH BIOACTIVE MOLECULES FOR TISSUE ENGINEERING
Markvicheva, Elena; Drozdova, Maria; Zlobina, M. et al

in Bioencapsulation Innovations, Newsletter (2015), November

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See detailIn vitro study of the specific interaction between poly (2-dimethylamino ethylmethacrylate) based polymers with platelets and red blood cells.
Flebus, Luca ULg; Lombart, François ULg; Martinez-Jothar, L et al

in International Journal of Pharmaceutics (2015), 492

Poly(2-dimethylamino)ethyl methacrylate (PDMAEMA) is an attractive polycation frequently proposed as a non-viral vector for gene therapy. As expected for other cationic carriers, intravenous ... [more ▼]

Poly(2-dimethylamino)ethyl methacrylate (PDMAEMA) is an attractive polycation frequently proposed as a non-viral vector for gene therapy. As expected for other cationic carriers, intravenous administration of PDMAEMA can result in its ionic complexation with various negatively charged domains found within the blood. To gain more insight into this polycation hemoreactivity, we followed the binding kinetics of a free form (FF) of fluorescein labelled PDMAEMA (below 15 kDa) in normal human blood using flow cytometry. This in vitro study highlighted that platelets display higher affinity for this polycation compared to red blood cells (RBCs), with an adsorption isotherm characteristics of a specific saturable binding site. PDMAEMA (1-20μg/mL) exerted a concentration dependent proaggregant effect with a biphasic aggregation of washed platelets. Activation of platelets was also noticed in whole blood with the expression of P-selectin and fibrinogen on platelet surface. Although additional studies would be needed in order to elucidate the mechanism of PDMAEMA mediated activation of platelets, our manuscript provides important information on the hemoreactivity of FF PDMAEMA. [less ▲]

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