Search results for "extracellular matrix ()"

showing 10 items of 101 documents

Usher syndrome and Leber congenital amaurosis are molecularly linked via a novel isoform of the centrosomal ninein-like protein.

2009

Contains fulltext : 80984.pdf (Publisher’s version ) (Closed access) Usher syndrome (USH) and Leber congenital amaurosis (LCA) are autosomal recessive disorders resulting in syndromic and non-syndromic forms of blindness. In order to gain insight into the pathogenic mechanisms underlying retinal degeneration, we searched for interacting proteins of USH2A isoform B (USH2A(isoB)) and the LCA5-encoded protein lebercilin. We identified a novel isoform of the centrosomal ninein-like protein, hereby named Nlp isoform B (Nlp(isoB)), as a common interactor. Although we identified the capacity of this protein to bind calcium with one of its three EF-hand domains, the interacton with USH2A(isoB) did …

Gene isoformRetinal degenerationCandidate geneGenetics and epigenetic pathways of disease [NCMLS 6]Usher syndromeMolecular Sequence DataOptic Atrophy Hereditary LeberBiologyIn Vitro TechniquesNeuroinformatics [DCN 3]CiliopathiesRetinaCell LineMiceCiliogenesisTwo-Hybrid System TechniquesGeneticsmedicineotorhinolaryngologic diseasesAnimalsHumansProtein IsoformsPhotoreceptor CellsAmino Acid SequenceNuclear proteinRats WistarEye ProteinsMolecular BiologyGenetics (clinical)GeneticsExtracellular Matrix ProteinsCiliumNuclear ProteinsGeneral MedicineArticlesmedicine.diseaseRatsMice Inbred C57BLMicrotubule-Associated ProteinsSequence AlignmentUsher SyndromesFunctional Neurogenomics [DCN 2]Protein BindingHuman Molecular Genetics
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Allelic age of the USH2A c.2299delG mutation

2010

24 p., figuras y bibliografía

Gene isoformUsher syndromePopulationc.2299delGSingle-nucleotide polymorphismBiologyPolymorphism Single NucleotideArticleLinkage DisequilibriumWhite PeopleExonUSH2Aotorhinolaryngologic diseasesGeneticsmedicineHaplotypeHumansAlleleeducationGeneAllelesPhylogenyGenetics (clinical)GeneticsExtracellular Matrix Proteinseducation.field_of_studyHaplotypemedicine.diseaseHaplotypesMutationDatingUsher Syndromes
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Expression profiling of human fetal growth plate cartilage by EST sequencing.

2005

The differentiation of mesenchymal stem cells into hypertrophic chondrocytes is an integral and multistep process important in pattern formation, endochondral ossification, and postnatal growth of the skeleton. In recent years, novel genes involved in these processes have been identified, but still only little is known about the large-scale gene expression profile during skeletal development. We initiated an expressed sequence tag (EST) project aiming at the identification of genes and pathways involved in this complex process. Candidate genes are expected to be of value for diagnosis and treatment of monogenic and multigenic heritable disorders of the skeleton. Here, we describe the sequen…

GeneticsExpressed Sequence TagsCandidate geneExpressed sequence tagExtracellular Matrix ProteinscDNA libraryIn silicoGene Expression ProfilingGene Expression Regulation DevelopmentalBiologyGene expression profilingFetusGene expressionHumansProteoglycansGrowth PlateMolecular BiologyEndochondral ossificationGeneMatrix biology : journal of the International Society for Matrix Biology
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Genetic analysis of 2299delG and C759F mutations (USH2A) in patients with visual and/or auditory impairments

2004

The most common mutation in the USH2A gene (Usherin), 2299delG, causes both typical Usher (USH) syndrome type II and atypical USH syndrome, two autosomal recessive disorders, characterised by moderate to severe sensorineural hearing loss and retinitis pigmentosa (RP). Furthermore, the C759F mutation in the USH2A gene has been described in 4.5% of patients with nonsyndromic recessive RP. We have investigated the presence of the 2299delG and/or the C759F mutations in 191 unrelated Spanish patients with different syndromic and nonsyndromic retinal diseases, or with nonsyndromic hearing impairment. The 2299delG mutation was observed in patients with clinical signs of USHII or of atypical USH sy…

GenotypeHearing Loss SensorineuralEye diseaseDNA Mutational AnalysisMutation MissenseGenetic analysisGene FrequencyGenotypeRetinitis pigmentosaotorhinolaryngologic diseasesGeneticsmedicineHumansAlleleAllelesPolymorphism Single-Stranded ConformationalGenetics (clinical)Sequence DeletionGeneticsExtracellular Matrix Proteinsbusiness.industryDNAmedicine.diseasePhenotypePhenotypeSpainMutation (genetic algorithm)Sensorineural hearing lossbusinessRetinitis PigmentosaEuropean Journal of Human Genetics
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Role of the Netrin-like Domain of Procollagen C-Proteinase Enhancer-1 in the Control of Metalloproteinase Activity

2010

The netrin-like (NTR) domain is a feature of several extracellular proteins, most notably the N-terminal domain of tissue inhibitors of metalloproteinases (TIMPs), where it functions as a strong inhibitor of matrix metalloproteinases and some other members of the metzincin superfamily. The presence of a C-terminal NTR domain in procollagen C-proteinase enhancers (PCPEs), proteins that stimulate the activity of astacin-like tolloid proteinases, raises the possibility that this might also have inhibitory activity. Here we show that both long and short forms of the PCPE-1 NTR domain, the latter beginning at the N-terminal cysteine known to be critical for TIMP activity, show no inhibition, at …

Glycobiology and Extracellular MatricesMatrix metalloproteinaseBiochemistryBONE MORPHOGENETIC PROTEIN-1AdamalysinFIBRILLAR PROCOLLAGENSTolloid ProteinaseExtracellular Matrix Proteins0303 health sciencesADAMTSFRIZZLED-RELATED PROTEINS030302 biochemistry & molecular biologyTissue Inhibitor of Metalloproteinases11 Medical And Health SciencesALPHA-CONVERTING-ENZYMEI PROCOLLAGENADAM ProteinsExtracellular MatrixPLASMINOGEN ACTIVATIONBiochemistryCollagen03 Chemical SciencesLife Sciences & BiomedicineProcollagenBiochemistry & Molecular BiologyTERMINAL DOMAINTolloid-Like MetalloproteinasesADAMTSBiologyBone morphogenetic protein 1Cell Line03 medical and health sciencesDisintegrinHumansHUMAN TISSUE INHIBITORMatrix MetalloproteinaseMolecular BiologyGlycoproteins030304 developmental biologyThrombospondinScience & TechnologyHeparinADAMCell Biology06 Biological SciencesMATRIX-METALLOPROTEINASESProtein Structure TertiaryADAM ProteinsProcollagen peptidaseSULFATED GLYCOSAMINOGLYCANSEnzymologybiology.proteinJournal of Biological Chemistry
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The shell-forming proteome of Lottia gigantea reveals both deep conservations and lineage-specific novelties

2013

19 pages; International audience; Proteins that are occluded within the molluscan shell, the so-called shell matrix proteins (SMPs), are an assemblage of biomolecules attractive to study for several reasons. They increase the fracture resistance of the shell by several orders of magnitude, determine the polymorph of CaCO(3) deposited, and regulate crystal nucleation, growth initiation and termination. In addition, they are thought to control the shell microstructures. Understanding how these proteins have evolved is also likely to provide deep insight into events that supported the diversification and expansion of metazoan life during the Cambrian radiation 543 million years ago. Here, we p…

Glycoside Hydrolasesmedicine.medical_treatmentproteomeGastropodaMolecular Sequence DataBiologyBiochemistrymollusc shell matrix proteinsTranscriptomeCyclophilins03 medical and health sciencesPaleontologyLineage specificAnimal ShellsSequence Analysis ProteinTandem Mass Spectrometry[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]evolutionmedicineAnimalsAmino Acid Sequence14. Life underwaterMantle (mollusc)[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyCarbonic Anhydrases030304 developmental biologyExtracellular Matrix Proteins0303 health sciencesProteaseEpidermal Growth FactorSequence Homology Amino AcidLimpet030302 biochemistry & molecular biologyCell Biologybiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsbiomineralizationPeptide FragmentsProtein Structure TertiaryPeroxidasesEvolutionary biology[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]ProteomeLottia giganteaElectrophoresis Polyacrylamide GelmantleBiomineralization
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Synthesis of undulin by rat liver fat-storing cells: Comparison with fibronectin and tenascin

1992

Abstract Fat-storing cells (FSCs) are known to synthesize various components of the hepatic extracellular matrix and thereby play an important role during liver fibrogenesis. The aim of our study was to investigate the synthesis of undulin, a recently described connective tissue protein belonging to the fibronectin—tenascin superfamily of glycoproteins, by fat-storing cells in primary culture. SDS-PAGE analysis of immunoprecipitates from cell layer lysates or media pulse-labeled with radioactive methionine revealed undulin-specific bands A (270 kDa), B1 (190 kDa), and B2 (180 kDa) after reduction. A single undulin-specific transcript was detected at about 7 kb. Undulin synthesized by cell-f…

GlycosylationCell Adhesion Molecules NeuronalMolecular Sequence DataTenascinConnective tissueExtracellular matrixchemistry.chemical_compoundBiosynthesisAdipocytemedicineAnimalsRNA MessengerRats WistarConnective Tissue CellsGlycoproteinschemistry.chemical_classificationExtracellular Matrix ProteinsBase SequencebiologyTunicamycinTenascinCell BiologyTunicamycinFibronectinsRatsCell biologyFibronectinKineticsmedicine.anatomical_structureLiverBiochemistrychemistryConnective TissueProtein Biosynthesisbiology.proteinFemaleCollagenOligonucleotide ProbesGlycoproteinProtein Processing Post-TranslationalExperimental Cell Research
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Binding of extracellular matrix proteins to Aspergillus fumigatus conidia

1996

As detected by confocal immunofluorescence microscopy, binding of fibronectin and laminin appeared to be associated with the protrusions present on the outer cell wall layer of resting Aspergillus fumigatus conidia. Flow cytometry confirmed that binding of laminin to conidia was dose dependent and saturable. Laminin binding was virtually eliminated in trypsin-treated organisms, thus suggesting the protein nature of the binding site. Conidia were also able to specifically adhere to laminin immobilized on microtiter plates. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting (immunoblotting) with laminin and antilaminin antibody of whole conidial homogenates allowed…

ImmunologyMicrobiologyAspergillus fumigatusLamininCell AdhesionBinding siteCell adhesionLaminin bindingGel electrophoresischemistry.chemical_classificationExtracellular Matrix ProteinsMicroscopy ConfocalbiologyAspergillus fumigatusFlow Cytometrybiology.organism_classificationMolecular biologyFibronectinInfectious DiseasesBiochemistrychemistrybiology.proteinParasitologyGlycoproteinProtein BindingResearch ArticleInfection and Immunity
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Perlecan Maintains microvessel integrity in vivo and modulates their formation in vitro

2012

Perlecan is a heparan sulfate proteoglycan assembled into the vascular basement membranes (BMs) during vasculogenesis. In the present study we have investigated vessel formation in mice, teratomas and embryoid bodies (EBs) in the absence of perlecan. We found that perlecan was dispensable for blood vessel formation and maturation until embryonic day (E) 12.5. At later stages of development 40% of mutant embryos showed dilated microvessels in brain and skin, which ruptured and led to severe bleedings. Surprisingly, teratomas derived from perlecan-null ES cells showed efficient contribution of perlecan-deficient endothelial cells to an apparently normal tumor vasculature. However, in perlecan…

IntegrinsAnatomy and PhysiologyGlycobiologylcsh:MedicineCardiovascularurologic and male genital diseasesCardiovascular SystemBiochemistryBiotecnologiaBasement MembraneMicePregnancyMolecular Cell BiologyMorphogenesisHistochemistrylcsh:ScienceSkinMice KnockoutPeripheral Vascular DiseasesExtracellular Matrix ProteinsNeovascularization PathologicTeratomaProteïnes de membranaBrainCell DifferentiationExtracellular MatrixConnective TissueCytochemistryMedicineFemaleFibroblast Growth Factor 2ProteoglycansResearch Articleendocrine systemMice 129 StrainCèl·lulesNeovascularization PhysiologicCell MigrationGrowth FactorsCell AdhesionAnimalsBirth DefectsBiologyExtracellular Matrix AdhesionsEmbryoid BodiesEmbryonic Stem Cellslcsh:RfungiProteinsExtracellular Matrix CompositionMice Inbred C57BLcarbohydrates (lipids)Cancer and OncologyMicrovesselsCardiovascular Anatomylcsh:QHeparan Sulfate ProteoglycansDevelopmental Biology
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Intramuscular Extracellular Matrix: Complex Environment of Muscle Cells

2002

KOVANEN, V. Intramuscular extracellular matrix: Complex environment of muscle cells. Exerc. Sport Sci. Rev., Vol. 30, No. 1, pp 20–25, 2002. Different collagen types among other extracellular matrix molecules, remodeling of the extracellular matrix with the aid of matrix metalloproteinases, and inte

IntegrinsChemistryFibrillar CollagensPhysical Therapy Sports Therapy and RehabilitationNon-Fibrillar CollagensExtracellular matrix moleculesMatrix metalloproteinaseBasement MembraneMatrix MetalloproteinasesExtracellular MatrixCell biologyExtracellular matrixHumansMyocyteOrthopedics and Sports MedicineMuscle SkeletalExercise and Sport Sciences Reviews
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