Le laboratoire « Matière et Systèmes Complexes » (MSC) est une unité mixte de recherche du CNRS et de l’université (UMR 7057). Le laboratoire est installé depuis 2007 sur le nouveau campus de l’Université Paris Diderot, Paris Rive Gauche, dans le bâtiment Condorcet. Il est réparti sur plusieurs étages. La direction et le secrétariat se trouvent au 6e étage. Le directeur actuel en est Laurent Limat, secondé par la directrice adjointe Florence Gazeau.
Le laboratoire MSC a pour sujet d’étude la matière et les systèmes complexes sous toutes leurs formes. Il peut s’agir de fluides montrant des phénomènes complexes non-linéaires (facettages de jets ou de tourbillons, structures et propriétés complexes de mousses, phénomènes de mouillage, propagation de vagues et de tsunamis) ou bien, par exemple, de systèmes proches de la géophysique et de l’environnement (systèmes granulaires tels que les dunes, phénomènes d’érosion, morphogenèse des plantes et même des villes, nage collective d’algues ou de bactéries…). Les études théoriques et expérimentales conduisent à des applications comme par exemple les éoliennes flexibles de haut rendement, l’optimisation de méthodes d’enduisage, le contôle de propriétés de surface ou la récupération de la biomasse (ingénierie verte)...
Le laboratoire étudie également le couplage entre la physique et la biologie des systèmes vivants, avec une approche multi-échelle. Les recherches effectuées vont d’échelles moléculaires ou supra-moléculaires (assemblages des protéines, chromatine, cytosquelette etc.) jusqu’à l’échelle de l’organisme entier (méduses, poulets, vers etc.) en passant par des études plus fondamentales sur des cellules uniques sur lesquelles sont exercées des forces quantifiées, permettant de comprendre les propriétés biophysiques de la matière vivante. Ces études aboutissent à de possibles applications en ingénierie tissulaire ou régénération des tissus avec des transferts dans le domaine médical.
Le laboratoire est structuré en cinq équipes :
Cependant les activités de ces équipes se recoupent souvent dans des projets communs aux frontières entre les comportements physiques et/ou biologiques (exemple : comportement de mousses marines, mesures de forces dans des tissus reconstitués, etc.)
Date: 4 Mar 2020 - 17:47
Desc: Focal adhesion kinase (FAK) regulates key biological processes downstream of G protein-coupled receptors (GPCRs) in normal and cancer cells, but the modes of kinase activation by these receptors remain unclear. We report that after GPCR stimulation, FAK activation is controlled by a sequence of events depending on the scaffolding proteins β-arrestins and G proteins. Depletion of β-arrestins results in a marked increase in FAK autophosphorylation and focal adhesion number. We demonstrate that β-arrestins interact directly with FAK and inhibit its autophosphorylation in resting cells. Both FAK-β-arrestin interaction and FAK inhibition require the FERM domain of FAK. Following the stimulation of the angiotensin receptor AT1AR and subsequent translocation of the FAK-β-arrestin complex to the plasma membrane, β-arrestin interaction with the adaptor AP-2 releases inactive FAK from the inhibitory complex, allowing its activation by receptor-stimulated G proteins and activation of downstream FAK effectors. Release and activation of FAK in response to angiotensin are prevented by an AP-2-binding deficient β-arrestin and by a specific inhibitor of β-arrestin/AP-2 interaction; this inhibitor also prevents FAK activation in response to vasopressin. This previously unrecognized mechanism of FAK regulation involving a dual role of β-arrestins, which inhibit FAK in resting cells while driving its activation at the plasma membrane by GPCR-stimulated G proteins, opens new potential therapeutic perspectives in cancers with up-regulated FAK.
Date: 23 Ago 2019 - 15:39
Desc: Tissue-engineered scaffolds are made of biocompatible polymers with various structures, allowing cell seeding, growth, and differentiation. Noninvasive imaging methods are needed to study tissue-engineered constructs before and after implantation. Here, we show that high-resolution magnetic resonance imaging (MRI) performed on a clinical 1.5-T device is a reliable technique to assess three-dimensional structures of porous scaffolds and to validate cell-seeding procedures. A high-temperature superconducting detection coil was used to achieve a resolution of 30Â30Â30 mm 3 when imaging the scaffolds. Three types of structures with tuneable architectures were prepared from naturally derived polysaccharides and evaluated as scaffolds for mesenchymal stem cell (MSC) culture. To monitor cell seeding, MSCs were magnetically labeled using simple incubation with anionic citrate-coated iron-oxide nanoparticles for 30 min. Iron uptake was quantified using single-cell magnetophoresis, and cell proliferation was checked for 7 days after labeling. Three-dimensional (3D) microstructures of scaffolds were assessed using MRI, revealing lamellar or globular porous organization according to the scaffold preparation process. MSCs with different iron load (5, 12 and 31 pg of iron per cell) were seeded on scaffolds at low density (132 cells=mm 3) and detected on 3D gradient-echo MR images according to phase distortions and areas of intensely low signal, whose size increased with cell iron load and echo time. Overall signal loss in the scaffold correlated with the number of seeded cells and their iron load. Different organizations of cells were observed depending on the scaffold architecture. After subcutaneous implantation in mice, scaffolds seeded with labeled cells could be distinguished in vivo from scaffold with nonlabeled cells by observation of signal and phase heterogeneities and by measuring the global signal loss. High-resolution 1.5-T MRI combined with efficient intracellular contrast agents shows promise for noninvasive 3D visualization of tissue-engineered constructs before and after in vivo implantation.
Date: 11 Mar 2019 - 15:14
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Date: 11 Mar 2019 - 15:05
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Date: 21 Oct 2019 - 19:48
Desc: Endothelial integrity relies on a mechanical crosstalk between intercellular and cell-matrix interactions. This crosstalk is compromised in hemorrhagic vascular lesions of patients carrying loss-of-function mutations in cerebral cavernous malformation (CCM) genes. RhoA/ROCK-dependent cytoskeletal remodeling is central to the disease, as it causes unbalanced cell adhesion towards increased cell-extracellular matrix adhesions and destabilized cell-cell junctions. This study reveals that CCM proteins directly orchestrate ROCK1 and ROCK2 complementary roles on the mechanics of the endothelium. CCM proteins act as a scaffold, promoting ROCK2 interactions with VE-cadherin and limiting ROCK1 kinase activity. Loss of CCM1 (also known as KRIT1) produces excessive ROCK1-dependent actin stress fibers and destabilizes intercellular junctions. Silencing of ROCK1 but not ROCK2 restores the adhesive and mechanical homeostasis of CCM1 and CCM2-depleted endothelial monolayers, and rescues the cardiovascular defects of ccm1 mutant zebrafish embryos. Conversely, knocking down Rock2 but not Rock1 in wild-type zebrafish embryos generates defects reminiscent of the ccm1 mutant phenotypes. Our study uncovers the role of the CCM1-CCM2 complex in controlling ROCK1 and ROCK2 to preserve endothelial integrity and drive heart morphogenesis. Moreover, it solely identifies the ROCK1 isoform as a potential therapeutic target for the CCM disease.
Université Paris Diderot - Paris 7
U.F.R. Physique
Bâtiment Condorcet
10, rue Alice Domon et Léonie Duquet
75205 PARIS CEDEX 13