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5 results on '"Boston Children's Hospital-Harvard Medical School [Boston] (HMS)"'

1. Comb-like dextran copolymers: A versatile strategy to coat highly porous MOF nanoparticles with a PEG shell

Author

Borja Moreira-Alvarez, Daniel M. Foulkes, Xue Li, Juan M. Casas-Solvas, Mario Menendez-Miranda, Antonio Vargas-Berenguel, Catherine Ladavière, Giovanna Cutrone, Ruxandra Gref, Jorge Ruiz Encinar, Ahmet Aykaç, Jingwen Qiu, Didier Desmaële, Department of Surgery/Urology, Boston Children's Hospital-Harvard Medical School [Boston] (HMS), Institut des Sciences Moléculaires d'Orsay (ISMO), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Ingénierie des Matériaux Polymères (IMP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Jean Monnet [Saint-Étienne] (UJM)-Centre National de la Recherche Scientifique (CNRS), Institut Galien Paris-Sud (IGPS), University of Almeria, Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), University of Oviedo, Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Jean Monnet [Saint-Étienne] (UJM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut Galien Paris-Saclay (IGPS), and Institut de Chimie du CNRS (INC)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)

Subjects
Polymers and Plastics, Nanoparticle, 02 engineering and technology, 010402 general chemistry, 01 natural sciences, chemistry.chemical_compound, metal organic frameworks, nanomedecine, PEG ratio, Materials Chemistry, ComputingMilieux_MISCELLANEOUS, [CHIM.ORGA]Chemical Sciences/Organic chemistry, Chemistry, nanoparticle, Organic Chemistry, technology, industry, and agriculture, polymer coating, [SDV.SP]Life Sciences [q-bio]/Pharmaceutical sciences, 021001 nanoscience & nanotechnology, 0104 chemical sciences, Dextran, [CHIM.POLY]Chemical Sciences/Polymers, Chemical engineering, dextran, Drug delivery, drug delivery, Click chemistry, Surface modification, 0210 nano-technology, Drug carrier, Ethylene glycol
Abstract

International audience; Nanoparticles made of metal-organic frameworks (nanoMOFs) are becoming of increasing interest as drug carriers. However, engineered coatings such as poly(ethylene glycol) (PEG) based ones are required to prevent nanoMOFs recognition and clearance by the innate immune system, a prerequisite for biomedical applications. This still presents an important challenge due to the highly porous structure and degradability of nanoMOFs. We provide here a proof of concept that the surface of iron-based nanoMOFs can be functionalized in a rapid, organic solvent-free and non-covalent manner using a novel family of comb-like copolymers made of dextran (DEX) grafted with both PEG and alendronate (ALN) moieties, which are iron complexing groups to anchor to the nanoMOFs surface. We describe the synthesis of DEX-ALN-PEG copolymers by click chemistry, with control of both the amount of PEG and ALN moieties. Stable DEX-ALN-PEG coatings substantially decreased their in-ternalization by macrophages in vitro, providing new perspectives for biomedical applications.

Published
2019
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2. Biocompatibility of filomicelles prepared from poly(ethylene glycol)-polylactide diblock copolymers as potential drug carrier

Author

Xin Shen, Suming Li, Xue Liu, Feng Su, Peng Yun, Rongye Li, Chenglong Li, Department of Surgery/Urology, Boston Children's Hospital-Harvard Medical School [Boston] (HMS), College of Chemical Engineering, Qingdao University of Science and Technology, Institut Européen des membranes (IEM), Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM), and Harvard Medical School [Boston] (HMS)-Boston Children's Hospital

Subjects
Materials science, Biocompatibility, Polyesters, Biomedical Engineering, Biophysics, Bioengineering, 02 engineering and technology, 010402 general chemistry, 01 natural sciences, Hemolysis, Cell Line, Polyethylene Glycols, Biomaterials, chemistry.chemical_compound, In vivo, PEG ratio, Materials Testing, Copolymer, Organic chemistry, Animals, Humans, [CHIM]Chemical Sciences, Blood Coagulation, Micelles, Zebrafish, ComputingMilieux_MISCELLANEOUS, Drug Carriers, technology, industry, and agriculture, Serum Albumin, Bovine, 021001 nanoscience & nanotechnology, 0104 chemical sciences, Chemical engineering, Polymerization, chemistry, Cytokines, Cattle, Adsorption, 0210 nano-technology, Drug carrier, Ethylene glycol, Protein adsorption
Abstract

A series of poly(ethylene glycol)-polylactide (PEG-PLA) diblock copolymers were synthesized by ring-opening polymerization of l-lactide using monomethoxy PEG as macroinitiator and zinc lactate as catalyst. Filomicelles were prepared from the resulting copolymers by co-solvent evaporation method. The biocompatibility of the various filomicelles was evaluated with the aim of assessing their potential as drug carriers. Various aspects of biocompatibility were considered, including agar diffusion test, MTT assay, release of cytokines, hemolytic test, dynamic clotting time, protein adsorption in vitro, and zebrafish embryonic compatibility in vivo. The results revealed that the filomicelles present good cytocompatibility and hemocompatibility in vitro. Moreover, the cumulative effects of filomicelles throughout embryos deveploping stages have no toxicity in vivo. It is thus concluded that filomicelles prepared from PEG-PLA copolymers with outstanding biocompatibility are promising as potential drug car...

Published
2017
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3. Choroid-Plexus-Derived Otx2 Homeoprotein Constrains Adult Cortical Plasticity

Author

Henry H.C. Lee, Ariel A. Di Nardo, Alain Joliot, Lorenzo Tibaldi, Julien Spatazza, Takao K. Hensch, Alain Prochiantz, Laboratoire de Biologie Cellulaire et Moléculaire du Contrôle de la Prolifération (LBCMCP), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), F.M. Kirby Neurobiology Center [Boston, MA, USA] (Harvard Medical School), Boston Children's Hospital-Harvard Medical School [Boston] (HMS), Centre interdisciplinaire de recherche en biologie (CIRB), Labex MemoLife, École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Collège de France (CdF (institution))-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Molecular and Cellular Biology [Cambridge, MA, USA] (Center for Brain Science), Harvard University [Cambridge], Chaire Processus morphogénétiques, Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Labex MemoLife, Harvard Medical School [Boston] (HMS)-Boston Children's Hospital, École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Collège de France - Chaire Processus morphogénétiques, Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Labex MemoLife, Di Nardo, Ariel, Collège de France (CdF (institution))-Université Paris sciences et lettres (2020-....) (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Center for Interdisciplinary Research in Biology (CIRB)

Subjects
genetic structures, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Regulator, Biology, Plasticity, GABAergic neuron, Article, General Biochemistry, Genetics and Molecular Biology, Mice, 03 medical and health sciences, 0302 clinical medicine, Neuroplasticity, medicine, Animals, Humans, lcsh:QH301-705.5, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, Neuronal Plasticity, Otx Transcription Factors, [SDV.NEU.NB] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Anatomy, eye diseases, Early life, Mice, Inbred C57BL, Visual cortex, medicine.anatomical_structure, lcsh:Biology (General), Choroid Plexus, Forebrain, Choroid plexus, Neuroscience, 030217 neurology & neurosurgery
Abstract

International audience; Brain plasticity is often restricted to critical periods in early life. Here, we show that a key regulator of this process in the visual cortex, Otx2 homeoprotein, is synthesized and secreted globally from the choroid plexus. Consequently, Otx2 is maintained in selected GABA cells unexpectedly throughout the mature forebrain. Genetic disruption of choroid-expressed Otx2 impacts these distant circuits and in the primary visual cortex reopens binocular plasticity to restore vision in amblyopic mice. The potential to regulate adult cortical plasticity through the choroid plexus underscores the importance of this structure in brain physiology and offers therapeutic approaches to recovery from a broad range of neurodevelopmental disorders.

Published
2013
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4. Translational implications of endothelial cell dysfunction in association with chronic allograft rejection

Author

Kevin P. Daly, Daniel Irimia, Leo Boneschansker, David M. Briscoe, Hironao Nakayama, Fadi Fakhouri, Johannes Wedel, Sarah Bruneau, Transplant Research Program [Boston, MA, USA], Boston Children's Hospital, Division of Nephrology [Boston, MA, USA] (Department of Medicine), Department of Pediatrics [Boston, MA, USA], Harvard Medical School [Boston] (HMS), Centre de Recherche en Transplantation et Immunologie (U1064 Inserm - CRTI), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN), Vascular Biology Program [Boston, MA, USA] (Department of Surgery and Pathology), Boston Children's Hospital-Harvard Medical School [Boston] (HMS), Department of Surgery [Boston, MA, USA] (BioMEMS Resource Center), Harvard Medical School [Boston] (HMS)-Massachusetts General Hospital [Boston]-Shriners Hospitals for Children [Boston], NIH Grants R01AI046756, R01AI92305 and R21AI114223, a Pfizer ARTS grant. NIH grant T32DK007726 and T32AI007529. AST Fellowship grant and a grant from the Fondation pour la Recherche Médicale ARF20140129163, the German Research Foundation (DFG)., Le Bihan, Sylvie, and Harvard Medical School [Boston] (HMS)-Boston Children's Hospital

Subjects
0301 basic medicine, Nephrology, medicine.medical_specialty, Time Factors, Angiogenesis, Endothelial cells, Cell, Kidney, Article, Translational Research, Biomedical, 03 medical and health sciences, chemistry.chemical_compound, Risk Factors, Internal medicine, microRNA, medicine, Animals, Humans, mTOR-mediated signaling, miRNA, [SDV.MHEP] Life Sciences [q-bio]/Human health and pathology, business.industry, Mechanism (biology), Graft survival, Allografts, Kidney Transplantation, Vascular endothelial growth factor, Endothelial stem cell, MicroRNAs, Treatment Outcome, 030104 developmental biology, medicine.anatomical_structure, Cellular Microenvironment, Gene Expression Regulation, chemistry, Allograft rejection, Chronic Disease, Microvessels, Pediatrics, Perinatology and Child Health, Immunology, Graft rejection, Cancer research, Preventative therapeutics, business, Biomarkers, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
Abstract

Advances in therapeutics have dramatically improved short-term graft survival, but the incidence of chronic rejection has not changed in the past 20 years. New insights into mechanism are sorely needed at this time and it is hoped that the development of predictive biomarkers will pave the way for the emergence of preventative therapeutics. In this review, we discuss a paradigm suggesting that sequential changes within graft endothelial cells (EC) lead to an intragraft microenvironment that favors the development of chronic rejection. Key initial events include EC injury, activation and uncontrolled leukocyte-induced angiogenesis. We propose that all of these early changes in the microvasculature lead to abnormal blood flow patterns, local tissue hypoxia, and an associated overexpression of HIF-1α-inducible genes, including vascular endothelial growth factor. We also discuss how cell intrinsic regulators of mTOR-mediated signaling within EC are of critical importance in microvascular stability and may thus have a role in the inhibition of chronic rejection. Finally, we discuss recent findings indicating that miRNAs may regulate EC stability, and we review their potential as novel non-invasive biomarkers of allograft rejection. Overall, this review provides insights into molecular events, genes, and signals that promote chronic rejection and their potential as biomarkers that serve to support the future development of interruption therapeutics.

Published
2016
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5. MTM1 mutation associated with X-linked myotubular myopathy in Labrador Retrievers

Author

G. Diane Shelton, Susan M. Taylor, Alan H. Beggs, Johann Böhm, Katie M. Minor, Laurent Tiret, Marie Maurer, Andrew P. Mizisin, Ling T. Guo, Elizabeth C R Snead, Jocelyn Laporte, James R. Mickelson, M. Kozlowski, Martin K. Childers, Christophe Hitte, Anna Buj-Bello, Manton Center for Orphan Disease Research, Harvard Medical School [Boston] (HMS)-Boston Children's Hospital, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Western College of Veterinary Medicine, University of Saskatchewan [Saskatoon] (U of S), Génétique Moléculaire et Cellulaire (UGMC), École nationale vétérinaire d'Alfort (ENVA)-Institut National de la Recherche Agronomique (INRA), School of Veterinary Medicine, University of Minnesota [Twin Cities] (UMN), University of Minnesota System-University of Minnesota System, Wake Forest University, Institut de Génétique et Développement de Rennes (IGDR), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS), Department of Pathology [San Diego], University of California [San Diego] (UC San Diego), University of California-University of California, Généthon, University of Minnesota [Twin Cities], Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-IFR140-Centre National de la Recherche Scientifique (CNRS), Genethon, Boston Children's Hospital-Harvard Medical School [Boston] (HMS), De Villemeur, Hervé, École nationale vétérinaire - Alfort (ENVA)-Institut National de la Recherche Agronomique (INRA), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS), Department of Pathology [Univ California San Diego] (UC San Diego), School of Medicine [Univ California San Diego] (UC San Diego), University of California (UC)-University of California (UC)-University of California [San Diego] (UC San Diego), and University of California (UC)-University of California (UC)

Subjects
Male, Pathology, Myotubularin, necklace fibers, canine myopathy, [SDV.GEN] Life Sciences [q-bio]/Genetics, Exon, Mice, 0302 clinical medicine, congenital myopathy, Chlorocebus aethiops, Missense mutation, Dog Diseases, Fluorescent Antibody Technique, Indirect, Genetics, Mice, Knockout, 0303 health sciences, Multidisciplinary, Genetic Diseases, X-Linked, SDV:GEN, Biological Sciences, myotubularin, animal model, Protein Tyrosine Phosphatases, Non-Receptor, X-linked myotubular myopathy, Muscle atrophy, Pedigree, COS Cells, Female, medicine.symptom, Myopathies, Structural, Congenital, medicine.medical_specialty, Genotype, Green Fluorescent Proteins, Molecular Sequence Data, Biology, 03 medical and health sciences, Dogs, Genetic model, medicine, Animals, Humans, Amino Acid Sequence, Centronuclear myopathy, Muscle, Skeletal, 030304 developmental biology, [SDV.GEN]Life Sciences [q-bio]/Genetics, Base Sequence, Sequence Homology, Amino Acid, medicine.disease, Congenital myopathy, Microscopy, Electron, Haplotypes, Mutation, 030217 neurology & neurosurgery
Abstract

Mutations in the MTM1 gene encoding myotubularin cause X-linked myotubular myopathy (XLMTM), a well-defined subtype of human centronuclear myopathy. Seven male Labrador Retrievers, age 14–26 wk, were clinically evaluated for generalized weakness and muscle atrophy. Muscle biopsies showed variability in fiber size, centrally placed nuclei resembling fetal myotubes, and subsarcolemmal ringed and central dense areas highlighted with mitochondrial specific reactions. Ultrastructural studies confirmed the centrally located nuclei, abnormal perinuclear structure, and mitochondrial accumulations. Wild-type triads were infrequent, with most exhibiting an abnormal orientation of T tubules. MTM1 gene sequencing revealed a unique exon 7 variant in all seven affected males, causing a nonconservative missense change, p.N155K, which haplotype data suggest derives from a recent founder in the local population. Analysis of a worldwide panel of 237 unaffected Labrador Retrievers and 59 additional control dogs from 25 other breeds failed to identify this variant, supporting it as the pathogenic mutation. Myotubularin protein levels and localization were abnormal in muscles from affected dogs, and expression of GFP-MTM1 p.N155K in COS-1 cells showed that the mutant protein was sequestered in proteasomes, where it was presumably misfolded and prematurely degraded. These data demonstrate that XLMTM in Labrador Retrievers is a faithful genetic model of the human condition.

Published
2010
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