Search results for "matrix proteins"

showing 10 items of 125 documents

Reelin and CXCL12 regulate distinct migratory behaviors during the development of the dopaminergic system.

2014

The proper functioning of the dopaminergic system requires the coordinated formation of projections extending from dopaminergic neurons in the substantia nigra (SN), ventral tegmental area (VTA) and retrorubral field to a wide array of forebrain targets including the striatum, nucleus accumbens and prefrontal cortex. The mechanisms controlling the assembly of these distinct dopaminergic cell clusters are not well understood. Here, we have investigated in detail the migratory behavior of dopaminergic neurons giving rise to either the SN or the medial VTA using genetic inducible fate mapping, ultramicroscopy, time-lapse imaging, slice culture and analysis of mouse mutants. We demonstrate that…

Receptors CXCR4Cell Adhesion Molecules NeuronalDopamineEmbryonic DevelopmentSubstantia nigraNerve Tissue ProteinsStriatumBiologyNucleus accumbensLigandsModels BiologicalTime-Lapse ImagingMiceCell MovementDopaminergic CellmedicineAnimalsCell LineageReelinMolecular BiologyMice KnockoutExtracellular Matrix ProteinsDopaminergic NeuronsDopaminergicSerine EndopeptidasesVentral Tegmental AreaAnatomyChemokine CXCL12Ventral tegmental areaSubstantia NigraReelin Proteinmedicine.anatomical_structurenervous systemForebrainbiology.proteinNeuroscienceDevelopmental BiologySignal TransductionDevelopment (Cambridge, England)
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Scaffold protein harmonin (USH1C) provides molecular links between Usher syndrome type 1 and type 2.

2005

Contains fulltext : 48386.pdf (Publisher’s version ) (Closed access) Usher syndrome (USH) is the most frequent cause of combined deaf-blindness in man. USH is clinically and genetically heterogeneous with at least 11 chromosomal loci assigned to the three USH types (USH1A-G, USH2A-C, USH3A). Although the different USH types exhibit almost the same phenotype in human, the identified USH genes encode for proteins which belong to very different protein classes and families. We and others recently reported that the scaffold protein harmonin (USH1C-gene product) integrates all identified USH1 molecules in a USH1-protein network. Here, we investigated the relationship between the USH2 molecules a…

Scaffold proteinGenetics and epigenetic pathways of disease [NCMLS 6]Usher syndromeStereocilia (inner ear)Cell Cycle ProteinsBiologyInteractomeReceptors G-Protein-CoupledMiceotorhinolaryngologic diseasesGeneticsmedicineAnimalsNeurosensory disorders [UMCN 3.3]Photoreceptor CellsRats WistarMolecular BiologyGeneGenetics (clinical)Renal disorder [IGMD 9]GeneticsExtracellular Matrix ProteinsStereociliumBinding SitesHair Cells Auditory InnerSodium-Bicarbonate SymportersUsher Syndrome Type 1General Medicinemedicine.diseasePhenotypeRatsMice Inbred C57BLCytoskeletal ProteinsCarrier ProteinsUsher Syndromes
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A novel Usher protein network at the periciliary reloading point between molecular transport machineries in vertebrate photoreceptor cells.

2008

Contains fulltext : 69178.pdf (Publisher’s version ) (Closed access) The human Usher syndrome (USH) is the most frequent cause of combined deaf-blindness. USH is genetically heterogeneous with at least 12 chromosomal loci assigned to three clinical types, USH1-3. Although these USH types exhibit similar phenotypes in human, the corresponding gene products belong to very different protein classes and families. The scaffold protein harmonin (USH1C) was shown to integrate all identified USH1 and USH2 molecules into protein networks. Here, we analyzed a protein network organized in the absence of harmonin by the scaffold proteins SANS (USH1G) and whirlin (USH2D). Immunoelectron microscopic anal…

Scaffold proteinGenetics and epigenetic pathways of disease [NCMLS 6]XenopusCell Cycle ProteinsNerve Tissue ProteinsBiologyIn Vitro TechniquesNeuroinformatics [DCN 3]TransfectionModels BiologicalReceptors G-Protein-CoupledMiceChlorocebus aethiopsProtein Interaction MappingGeneticsPerception and Action [DCN 1]otorhinolaryngologic diseasesAnimalsHumansNeurosensory disorders [UMCN 3.3]Cell Cycle ProteinMicroscopy ImmunoelectronMolecular BiologyIntegral membrane proteinGenetics (clinical)Adaptor Proteins Signal TransducingRenal disorder [IGMD 9]GeneticsMice KnockoutExtracellular Matrix ProteinsCiliumSignal transducing adaptor proteinMembrane ProteinsGeneral MedicineTransmembrane proteinCell biologyMice Inbred C57BLCytoskeletal ProteinsEctodomainGenetic defects of metabolism [UMCN 5.1]COS CellsNIH 3T3 CellsCervical collarUsher SyndromesFunctional Neurogenomics [DCN 2]Photoreceptor Cells VertebrateSubcellular FractionsImmunity infection and tissue repair [NCMLS 1]
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The Tegument Protein pp65 of Human Cytomegalovirus Acts as an Optional Scaffold Protein That Optimizes Protein Uploading into Viral Particles

2014

ABSTRACT The mechanisms that lead to the tegumentation of herpesviral particles are only poorly defined. The phosphoprotein 65 (pp65) is the most abundant constituent of the virion tegument of human cytomegalovirus (HCMV). It is, however, nonessential for virion formation. This seeming discrepancy has not met with a satisfactory explanation regarding the role of pp65 in HCMV particle morphogenesis. Here, we addressed the question of how the overall tegument composition of the HCMV virion depended on pp65 and how the lack of pp65 influenced the packaging of particular tegument proteins. To investigate this, we analyzed the proteomes of pp65-positive (pp65pos) and pp65-negative (pp65neg) viri…

Scaffold proteinHuman cytomegalovirusProteomevirusesImmunologyMorphogenesisCytomegalovirusBiologyMicrobiologyMass SpectrometryViral Matrix ProteinsVirologymedicineHumansGeneViral matrix proteinVirus AssemblyStructure and AssemblyVirionvirus diseasesViral tegumentbiochemical phenomena metabolism and nutritionPhosphoproteinsmedicine.diseaseVirologyCell biologysurgical procedures operativeInsect SciencePhosphoproteinProteomeGene DeletionJournal of Virology
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Molecular basis of human Usher syndrome: deciphering the meshes of the Usher protein network provides insights into the pathomechanisms of the Usher …

2006

Usher syndrome (USH) is the most frequent cause of combined deaf-blindness in man. It is clinically and genetically heterogeneous and at least 12 chromosomal loci are assigned to three clinical USH types, namely USH1A-G, USH2A-C, USH3A (Davenport, S.L.H., Omenn, G.S., 1977. The heterogeneity of Usher syndrome. Vth Int. Conf. Birth Defects, Montreal; Petit, C., 2001. Usher syndrome: from genetics to pathogenesis. Annu. Rev. Genomics Hum. Genet. 2, 271-297). Mutations in USH type 1 genes cause the most severe form of USH. In USH1 patients, congenital deafness is combined with a pre-pubertal onset of retinitis pigmentosa (RP) and severe vestibular dysfunctions. Those with USH2 have moderate to…

Scaffold proteinModels MolecularUsher syndromePDZ domainProtocadherinCadherin Related ProteinsCell Cycle ProteinsNerve Tissue ProteinsBiologyDeafnessMyosinsCellular and Molecular NeuroscienceRetinitis pigmentosaotorhinolaryngologic diseasesmedicineAnimalsHumansAdaptor Proteins Signal TransducingGeneticsExtracellular Matrix ProteinsModels GeneticCadherinRetinal DegenerationSignal transducing adaptor proteinDyneinsMembrane Proteinsmedicine.diseaseCadherinsSensory SystemsOphthalmologyCytoskeletal ProteinsDisease Models AnimalMembrane proteinMyosin VIIaMutationMicrotubule ProteinsVestibule LabyrinthUsher SyndromesExperimental eye research
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MPP1 links the Usher protein network and the Crumbs protein complex in the retina.

2007

Contains fulltext : 53571.pdf (Publisher’s version ) (Closed access) The highly ordered distribution of neurons is an essential feature of a functional mammalian retina. Disruptions in the apico-basal polarity complexes at the outer limiting membrane (OLM) of the retina are associated with retinal patterning defects in vertebrates. We have analyzed the binding repertoire of MPP5/Pals1, a key member of the apico-basal Crumbs polarity complex, that has functionally conserved counterparts in zebrafish (nagie oko) and Drosophila (Stardust). We show that MPP5 interacts with its MAGUK family member MPP1/p55 at the OLM. Mechanistically, this interaction involves heterodimerization of both MAGUK mo…

Scaffold proteinanimal structuresGenetics and epigenetic pathways of disease [NCMLS 6]BioinformaticsPDZ domainMolecular Sequence DataMice TransgenicNerve Tissue ProteinsNeuroinformatics [DCN 3]Models BiologicalRetinaMiceTwo-Hybrid System TechniquesCell polarityPerception and Action [DCN 1]GeneticsNeurosensory disorders [UMCN 3.3]Basal bodyAnimalsHumansAmino Acid SequenceRats WistarEye ProteinsMolecular BiologyZebrafishGenetics (clinical)ActinRenal disorder [IGMD 9]GeneticsExtracellular Matrix ProteinsBinding SitesbiologyModels GeneticCell MembraneMembrane ProteinsGeneral MedicineBlood Proteinsbiology.organism_classificationEmbryo MammalianCell biologyProtein Structure TertiaryRatsGenetic defects of metabolism [UMCN 5.1]Eye disordersense organsCellular energy metabolism [UMCN 5.3]Nucleoside-Phosphate KinaseFunctional Neurogenomics [DCN 2]Neural developmentHuman Molecular Genetics
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The colocalizations of pulp neural stem cells markers with dentin matrix protein-1, dentin sialoprotein and dentin phosphoprotein in human denticle (…

2021

Abstract Background The primary dentin, secondary dentin, and reactive tertiary dentin are formed by terminal differentiated odontoblasts, whereas atubular reparative tertiary dentin is formed by odontoblast-like cells. Odontoblast-like cells differentiate from pulpal stem cells, which express the neural stem cell markers nestin, S100β, Sox10, and P0. The denticle (pulp stone) is an unique mineralized extracellular matrix that frequently occurs in association with the neurovascular structures in the dental pulp. However, to date, the cellular origin of denticles in human dental pulp is unclear. In addition, the non-collagenous extracellular dentin matrix proteins dentin matrix protein 1 (DM…

SialoglycoproteinsMatrix (biology)Neural Stem Cellsstomatognathic systemDentinmedicineHumansDental PulpExtracellular Matrix ProteinsOdontoblastsChemistryCell DifferentiationGeneral MedicinePhosphoproteinsDentin phosphoproteinDMP1Cell biologystomatognathic diseasesmedicine.anatomical_structureDentinal TubuleOdontoblastDentinDental Pulp CalcificationPulp (tooth)AnatomyDentin sialoproteinDevelopmental BiologyAnnals of Anatomy - Anatomischer Anzeiger
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Characterization of a putative extracellular matrix protein from the beetle Tenebrio molitor: hormonal regulation during metamorphosis.

2004

0949-944X (Print) Journal Article Research Support, Non-U.S. Gov't; We used differential display to isolate epidermis cDNAs corresponding to juvenile-hormone analog-regulated mRNA from the beetle Tenebrio molitor. One of them encodes a putative extracellular matrix (ECM) protein, named Tenebrin. Indeed, the deduced protein sequence contains ECM typical features like the presence of a signal peptide, internal repeats, a RGD tripeptide sequence motif known to bind integrins and von Willebrand factor type c domains involved in protein-protein interactions. Northern blot analysis reveals a single transcript of about 11 kb with an expression pattern correlated to 20-hydroxyecdysone fluctuations …

Signal peptideIntegrinMolecular Sequence DataCycloheximideBiologyExtracellular matrixchemistry.chemical_compoundExtracellular Matrix Proteins/*genetics/metabolismGeneticsAnimalsDevelopmentalHormones/physiologyNorthern blotAmino Acid SequenceTenebrioTenebrio/*geneticsDifferential displayMessenger RNAExtracellular Matrix ProteinsMetamorphosisMetamorphosis BiologicalGene Expression Regulation DevelopmentalBiological/*physiologyHormoneschemistryBiochemistryGene Expression RegulationJuvenile hormonebiology.proteinDevelopmental BiologyDevelopment genes and evolution
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Mutation of a critical tryptophan to lysine in avidin or streptavidin may explain why sea urchin fibropellin adopts an avidin-like domain

1999

Sea urchin fibropellins are epidermal growth factor homologues that harbor a C-terminal domain, similar in sequence to hen egg-white avidin and bacterial streptavidin. The fibropellin sequence was used as a conceptual template for mutation of designated conserved tryptophan residues in the biotin-binding sites of the tetrameric proteins, avidin and streptavidin. Three different mutations of avidin, Trp-110-Lys, Trp-70-Arg and the double mutant, were expressed in a baculovirus-infected insect cell system. A mutant of streptavidin, Trp-120-Lys, was similarly expressed. The homologous tryptophan to lysine (W--K) mutations of avidin and streptavidin were both capable of binding biotin and bioti…

StreptavidinBiotin bindingTime FactorsFunctional dimerLysineMutantBiophysicsBiotinEnzyme-Linked Immunosorbent AssayBiologyBiochemistrychemistry.chemical_compoundBiotinTetramerStructural BiologyGeneticsAnimalsMolecular BiologyExtracellular Matrix ProteinsBinding SitesEpidermal Growth FactorLysineAvidin-biotin technologyTemperatureTryptophanCell BiologyAvidinRecombinant ProteinsKineticsReversiblechemistryBiochemistryBiotinylationSea UrchinsMutationbiology.proteinRecombinant avidin and streptavidinStreptavidinBiotin-bindingAvidinChromatography LiquidProtein BindingFEBS Letters
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Poly(γ-Glutamic Acid) as an Exogenous Promoter of Chondrogenic Differentiation of Human Mesenchymal Stem/Stromal Cells

2015

Cartilage damage and/or aging effects can cause constant pain, which limits the patient's quality of life. Although different strategies have been proposed to enhance the limited regenerative capacity of cartilage tissue, the full production of native and functional cartilaginous extracellular matrix (ECM) has not yet been achieved. Poly(γ-glutamic acid) (γ-PGA), a naturally occurring polyamino acid, biodegradable into glutamate residues, has been explored for tissue regeneration. In this work, γ-PGA's ability to support the production of cartilaginous ECM by human bone marrow mesenchymal stem/stromal cells (MSCs) and nasal chondrocytes (NCs) was investigated. MSC and NC pellets were cultur…

Stromal cellBiomedical EngineeringType II collagenCell Culture TechniquesBioengineeringBiochemistryBiomaterialsExtracellular matrixTransforming Growth Factor beta1ChondrocytesNasal CartilagesmedicineHumansAggrecansAggrecanCells CulturedGlycosaminoglycansExtracellular Matrix ProteinsChemistryCartilageMesenchymal stem cellMesenchymal Stem CellsSOX9 Transcription FactorOriginal ArticlesChondrogenesisMolecular biologyCulture Mediamedicine.anatomical_structureBiochemistryPolyglutamic AcidCulture Media ConditionedCalciumCollagenStromal CellsChondrogenesisType I collagen
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