Search results for "extracellular matrix ()"

showing 10 items of 101 documents

Impairing Otp homeodomain function in oral ectoderm cells affects skeletogenesis in sea urchin embryos

2003

AbstractIn the sea urchin embryo skeletogenesis is the result of a complex series of molecular and cellular events that coordinate the morphogenetic process. Past and recent evidence strongly indicate that skeletal initiation and growth are strictly dependent on signals emanating from the oral ectodermal wall. As previously suggested, Orthopedia (Otp), a homeodomain-containing transcription factor specifically expressed in a small subset of oral ectoderm cells, might be implicated in this signalling pathway. In this study, we utilize three different strategies to address the issue of whether Otp is an upstream regulator of sketelogenesis. We describe the effects of microinjection of Otp mor…

Transcriptional Activationanimal structuresMorpholinoOrthopedia homeoboxMolecular Sequence DataEctodermNerve Tissue ProteinsBiologyFusion geneEctodermmedicineSkeletogenesisAnimalsAmino Acid SequenceSea urchin embryoTranscription factorMolecular BiologyMessenger RNAExtracellular Matrix ProteinsBone DevelopmentEmbryoCell BiologyMolecular biologyHedgehog signaling pathwayMorpholino oligonucleotidesCytoskeletal Proteinsmedicine.anatomical_structureProtein BiosynthesisSea Urchinsembryonic structuresHomeoboxDevelopmental BiologyDevelopmental Biology
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MMP-10/stromelysin-2 promotes invasion of head and neck cancer.

2011

BackgroundPeriostin, IFN-induced transmembrane protein 1 (IFITM1) and Wingless-type MMTV integration site family, member 5B (Wnt-5b) were previously identified as the invasion promoted genes of head and neck squamous cell carcinoma (HNSCC) by comparing the gene expression profiles between parent and a highly invasive clone. We have previously reported that Periostin and IFITM1 promoted the invasion of HNSCC cells. Here we demonstrated that Wnt-5b overexpression promoted the invasion of HNSCC cells. Moreover, stromelysin-2 (matrix metalloproteinase-10; MMP-10) was identified as a common up-regulated gene among Periostin, IFITM1 and Wnt-5b overexpressing HNSCC cells by using microarray data s…

Tumor PhysiologyClone (cell biology)p38 Mitogen-Activated Protein KinasesMetastasisMetastasisMolecular Cell BiologyBasic Cancer ResearchNeoplasm MetastasisRegulation of gene expressionGene knockdownMultidisciplinaryHead and Neck cancerQRTransfectionHead and Neck TumorsExtracellular MatrixUp-RegulationGene Expression Regulation NeoplasticOncologyHead and Neck NeoplasmsGene Knockdown TechniquesCarcinoma Squamous CellMedicineResearch ArticleScience490Oral MedicineBiologyPeriostinHead and Neck Squamous Cell CarcinomaMatrix Metalloproteinase 10stomatognathic systemSettore MED/28 - Malattie OdontostomatologicheCell Line TumormedicineCancer Detection and Diagnosisotorhinolaryngologic diseasesHumansNeoplasm Invasiveness490BiologyExtracellular Matrix AdhesionsProtein Kinase InhibitorsneoplasmsMicroarray analysis techniquesCancers and Neoplasmsmedicine.diseaseMolecular biologyHead and neck squamous-cell carcinomaAntigens DifferentiationWnt Proteinsstomatognathic diseasesCancer researchCell Adhesion MoleculesPLoS ONE
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Reconstruction of Peritoneal-like Structure in Three-Dimensional Collagen Gel Matrix Culture

1997

The peritoneum is a serous membrane consisting of different kinds of cells and extracellular matrix components (ECM). The aim of the present study was to develop a three-dimensional (3D) in vitro culture system for possible investigation of pathological conditions of the peritoneum. Human omental mesothelial cells (MC) and endothelial cells from the umbilical vein (EC) were cultivated either on (MC) or in (EC) a preformed type I collagen matrix. In 3D culture mesothelial cells showed their phenotypical in vivo characteristics and the synthesis of a new basal membrane (BM). Endothelial cells developed vessel-like structures, produce a BM and express E-selectin after TNF-alpha stimulation. Th…

Umbilical VeinsCell Culture TechniquesBiologyMatrix (biology)EpitheliumUmbilical veinExtracellular matrixPeritoneummedicineHumansEndotheliumExtracellular Matrix ProteinsSerous membraneEpithelial CellsCell BiologyCell biologyEndothelial stem cellMicroscopy Electronmedicine.anatomical_structureAdipose TissueImmunologyKeratinsCollagenPeritoneumGelsOmentumMesothelial CellType I collagenExperimental Cell Research
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Deep conservation of bivalve nacre proteins highlighted by shell matrix proteomics of the Unionoida Elliptio complanata and Villosa lienosa.

2016

The formation of the molluscan shell nacre is regulated to a large extent by a matrix of extracellular macromolecules that are secreted by the shell-forming tissue, the mantle. This so-called ‘calcifying matrix’ is a complex mixture of proteins, glycoproteins and polysaccharides that is assembled and occluded within the mineral phase during the calcification process. Better molecular-level characterization of the substances that regulate nacre formation is still required. Notable advances in expressed tag sequencing of freshwater mussels, such as Elliptio complanata and Villosa lienosa , provide a pre-requisite to further characterize bivalve nacre proteins by a proteomic approach. In this…

Unionidae0301 basic medicineUnionoida[ SDV.BA.ZI ] Life Sciences [q-bio]/Animal biology/Invertebrate ZoologyVillosa lienosaBiomedical EngineeringBiophysicsLife Sciences–Earth Science interfaceBioengineeringBiologyProteomicsBiochemistrybivalveEvolution MolecularBiomaterials03 medical and health sciencesPaleontologyCalcification PhysiologicproteomicsAnimal Shells[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]shell nacreShell matrixAnimalscalcium carbonate14. Life underwaterNacreMantle (mollusc)chemistry.chemical_classificationExtracellular Matrix ProteinsElliptiobiology.organism_classificationbiomineralization[SDV.BA.ZI]Life Sciences [q-bio]/Animal biology/Invertebrate Zoology030104 developmental biologyBiochemistrychemistry[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]organic matrix proteinsGlycoproteinBiotechnologyBiomineralization
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The multiple facets of Cajal-Retzius neurons.

2021

ABSTRACTCajal-Retzius neurons (CRs) are among the first-born neurons in the developing cortex of reptiles, birds and mammals, including humans. The peculiarity of CRs lies in the fact they are initially embedded into the immature neuronal network before being almost completely eliminated by cell death at the end of cortical development. CRs are best known for controlling the migration of glutamatergic neurons and the formation of cortical layers through the secretion of the glycoprotein reelin. However, they have been shown to play numerous additional key roles at many steps of cortical development, spanning from patterning and sizing functional areas to synaptogenesis. The use of genetic l…

[SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/NeurobiologyCell Adhesion Molecules NeuronalNeurogenesisSynaptogenesisHippocampusNerve Tissue Proteins[SDV.BC.IC] Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB]BiologyDevelopmentMolecular heterogeneityHippocampusCajal-Retzius neurons03 medical and health sciencesGlutamatergicMolecular profiling0302 clinical medicineCortex (anatomy)[SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB]Biological neural networkmedicineotorhinolaryngologic diseasesAnimalsHumansReelinMolecular Biology030304 developmental biologyCerebral CortexNeurons0303 health sciencesExtracellular Matrix ProteinsCell DeathSerine Endopeptidases[SDV.NEU.NB] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology[SDV.BDD.EO] Life Sciences [q-bio]/Development Biology/Embryology and OrganogenesisReelin Proteinmedicine.anatomical_structure[SDV.BDD.EO]Life Sciences [q-bio]/Development Biology/Embryology and Organogenesisbiology.proteinCortexIdentification (biology)TranscriptomeNeuroscience030217 neurology & neurosurgerySingle-cell transcriptomicsDevelopmental BiologyDevelopment (Cambridge, England)
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Procollagen C-proteinase Enhancer Stimulates Procollagen Processing by Binding to the C-propeptide Region Only*

2011

Background: Procollagen C-proteinase enhancer-1 (PCPE-1) is an extracellular glycoprotein that increases activity of certain zinc metalloproteinases involved in tissue development and repair. Results: PCPE-1 binds uniquely to the C-propeptide region of the procollagen molecule. Conclusion: PCPE-1 enhances proteolysis by binding solely to the procollagen C-propeptides. Significance: These data may lead to future applications in the development of antifibrotic therapies.

animal structuresGlycosylationBiologyBiochemistryBone morphogenetic protein 1Protein Structure SecondaryBone Morphogenetic Protein 103 medical and health scienceschemistry.chemical_compoundMetalloprotease0302 clinical medicineHumansBinding siteEnhancerMolecular Biology030304 developmental biologyCell Line TransformedGlycoproteinschemistry.chemical_classification0303 health sciencesMetalloproteinaseExtracellular Matrix ProteinsBinding Sitesintegumentary systemCell BiologyEnzymatic ProcessingFibrosisExtracellular MatrixProcollagen peptidaseCollagen Type IIIchemistryBiochemistry030220 oncology & carcinogenesisembryonic structuresEnzymologyCollagenGlycoproteinProtein Processing Post-TranslationalTriple helixThe Journal of Biological Chemistry
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Tenascin gene expression in rat liver and in rat liver cells. In vivo and in vitro studies.

1991

Tenascin is a major glycoprotein constituent of the extracellular matrix with a strong affinity to fibronectin; its distribution is believed to be temporarily and spatially limited. Tenascin gene expression is increased during wound healing processes. As repair mechanisms in chronic liver diseases resemble wound healing we studied tenascin gene expression in rat liver and in isolated rat liver cells. In normal rat liver a tenascin specific antiserum stains sinusoidal cells with fiber-like prolongations, which at the same time are desmin-positive (ITO-cells). In the CCl4-acutely-damaged liver a strong tenascin staining is detected in cells located among the mononuclear cells of the inflammat…

endocrine systemPathologymedicine.medical_specialtyanimal structuresKupffer CellsCell Adhesion Molecules NeuronalTenascinConnective tissueFluorescent Antibody TechniqueGene ExpressionLiver Cirrhosis Experimentaldigestive systemDesminmedicineAnimalsEndotheliumCarbon TetrachlorideCells CulturedExtracellular Matrix ProteinsbiologyTenascin CMuscle SmoothRats Inbred StrainsTenascinFibroblastsmusculoskeletal systemMolecular biologyRatsFibronectinEndothelial stem cellmedicine.anatomical_structureLiverCell cultureembryonic structuresbiology.proteinHepatic stellate cellWound healingVirchows Archiv. B, Cell pathology including molecular pathology
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A luminal glycoprotein drives dose-dependent diameter expansion of the Drosophila melanogaster hindgut tube

2012

An important step in epithelial organ development is size maturation of the organ lumen to attain correct dimensions. Here we show that the regulated expression of Tenectin (Tnc) is critical to shape the Drosophila melanogaster hindgut tube. Tnc is a secreted protein that fills the embryonic hindgut lumen during tube diameter expansion. Inside the lumen, Tnc contributes to detectable O-Glycans and forms a dense striated matrix. Loss of tnc causes a narrow hindgut tube, while Tnc over-expression drives tube dilation in a dose-dependent manner. Cellular analyses show that luminal accumulation of Tnc causes an increase in inner and outer tube diameter, and cell flattening within the tube wall,…

glycoproteinCancer ResearchhindgutOrganogenesis[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritiontenectinHydrostatic pressureExtracellular matrixlumenMolecular Cell BiologyMorphogenesisDrosophila Proteinslumen;hindgut;tenectin;epithelial tube;glycoproteinGenetics (clinical)Animal biologyExtracellular Matrix ProteinsDrosophila MelanogasterGene Expression Regulation DevelopmentalHindgutAnimal ModelsAnatomymusculoskeletal systemExtracellular MatrixCell biologymedicine.anatomical_structureAlimentation et NutritionResearch Articleepithelial tubelcsh:QH426-470MorphogenesisLumen (anatomy)BiologyModel OrganismsGenetic MutationBiologie animaleGeneticsmedicineAnimalsFood and NutritionBiologyMolecular BiologyEcology Evolution Behavior and SystematicsGlycoproteinsEmbryonic stem cellExtracellular Matrix CompositionEpitheliumGastrointestinal Tractlcsh:GeneticsMutagenesisEctopic expressionGene Function[SDV.AEN]Life Sciences [q-bio]/Food and NutritionOrganism DevelopmentDevelopmental Biology
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Microarray-based mutation analysis of 183 Spanish families with Usher syndrome.

2010

PURPOSE. The purpose of this study was to test the ability of the genotyping microarray for Usher syndrome (USH) to identify the mutations responsible for the disease in a cohort of 183 patients with USH. METHODS. DNA from 183 patients with Usher syndrome from the Spanish population was analyzed using a genotyping microarray containing 429 previously identified disease-associated variants in eight USH genes. Mutations detected by the array were confirmed by direct sequencing. Haplotype analysis was also performed in families carrying common Spanish mutations. RESULTS. The genotyping microarray identified 43 different variants, divided into 32 disease causative and 11 probably non-pathologic…

medicine.medical_specialtyGenotypeMicroarrayUsher syndromeDNA Mutational AnalysisCadherin Related ProteinsCell Cycle ProteinsNerve Tissue ProteinsMyosinsBiologymedicine.disease_causePolymerase Chain ReactionReceptors G-Protein-CoupledMolecular geneticsGenotypemedicineotorhinolaryngologic diseasesHumansGenotypingAllelesAdaptor Proteins Signal TransducingOligonucleotide Array Sequence AnalysisGeneticsExtracellular Matrix ProteinsMutationGene Expression ProfilingHaplotypeMembrane ProteinsCadherinsmedicine.diseaseGene expression profilingCytoskeletal ProteinsSpainMyosin VIIaMutationUsher Syndromes
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Developmental expression of human cartilage matrix protein.

1994

Cartilage matrix protein (CMP) is a non-collagenous component of cartilage with a yet unknown function. In this study we used in situ hybridization to investigate the temporal and sptial distribution of CMP transcripts during human embryonic and early fetal development, and compared it to the pattern of expression observed for collagen types I, II, X, and decorin. The distribution of CMP and collagen type II transcripts followed a similar pattern in the embryonic bone anlage, the fetal growth plate, and the developing vertebral column. Expression was highest in the upper hypertrophic and lower proliferative zone, whereas calcified cartilage was negative throughout the different stages of bo…

medicine.medical_specialtyTranscription GeneticDecorinBiologyMatrix (biology)Cartilage Oligomeric Matrix ProteinKidneyChondrocyteBone and BonesExtracellular matrixEmbryonic and Fetal DevelopmentInternal medicinemedicinePerichondriumHumansMatrilin ProteinsRNA MessengerIn Situ HybridizationGlycoproteinsSkinExtracellular Matrix ProteinsCartilageCell DifferentiationDNAChondrogenesisSpineCell biologycarbohydrates (lipids)Collagen type I alpha 1Endocrinologymedicine.anatomical_structureCartilagePhenotypeJointsProteoglycansCollagenDecorinDevelopmental BiologyDevelopmental dynamics : an official publication of the American Association of Anatomists
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