Search results for "collagen type IV"

showing 10 items of 21 documents

Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly

2018

15 páginas, 6 figuras, 1 tabla.

0301 basic medicineGoodpasture’s diseaseAddenda and ErrataRandom hexamerBiochemistryEpitopelaw.invention03 medical and health sciencesAlport's syndrome0302 clinical medicineGoodpasture's diseaselawMissense mutationGeneral Materials ScienceAlport’s syndromeStructural motifNetwork assemblyCrystallographyGoodpasture's diseaseChemistry(IV)NC1 hexamersStructural proteinCollagen type IVGeneral ChemistryCondensed Matter PhysicsResearch PapersFolding (chemistry)030104 developmental biologyQD901-999BiophysicsRecombinant DNA030217 neurology & neurosurgeryAlport syndrome
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Stem Cell-Derived, microRNA-Carrying Extracellular Vesicles: A Novel Approach to Interfering with Mesangial Cell Collagen Production in a Hyperglycae…

2016

Extracellular vesicles (EVs) that are derived from stem cells are proving to be promising therapeutic options. We herein investigate the therapeutic potential of EVs that have been derived from different stem cell sources, bone-marrow (MSC) and human liver (HLSC), on mesangial cells (MCs) exposed to hyperglycaemia. By expressing a dominant negative STAT5 construct (ΔNSTAT5) in HG-cultured MCs, we have demonstrated that miR-21 expression is under the control of STAT5, which translates into Transforming Growth Factor beta (TGFβ) expression and collagen production. A number of approaches have been used to show that both MSC- and HLSC-derived EVs protect MCs from HG-induced damage via the trans…

0301 basic medicineMolecular biologyCellGene Expressionlcsh:MedicineBiochemistry0302 clinical medicineAnimal CellsChronic Kidney DiseaseMedicine and Health SciencesSTAT5 Transcription FactorRNA Processing Post-Transcriptionallcsh:ScienceSTAT5Energy-Producing OrganellesCells CulturedMultidisciplinarybiologyMesangial cellStem CellsVector ConstructionCell biologyMitochondriaEnzymesmedicine.anatomical_structureBiochemistryNephrology030220 oncology & carcinogenesisMesangial CellsCollagenStem cellCellular TypesCellular Structures and OrganellesOxidoreductasesLuciferaseResearch ArticleCollagen Type IVBioenergeticsDNA constructionModels Biological03 medical and health sciencesExtracellular VesiclesmicroRNAmedicineGene Expression and Vector TechniquesGeneticsHumansVesiclesCell ProliferationMolecular Biology Assays and Analysis TechniquesCell growthMesenchymal stem celllcsh:RBiology and Life SciencesProteinsMesenchymal Stem CellsTransforming growth factor betaCell BiologyResearch and analysis methodsMicroRNAs030104 developmental biologyMolecular biology techniquesGlucoseHyperglycemiabiology.proteinEnzymologylcsh:QCollagensPLoS ONE
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Pharmacological Suppression of CNS Scarring by Deferoxamine Reduces Lesion Volume and Increases Regeneration in an In Vitro Model for Astroglial-Fibr…

2015

Lesion-induced scarring is a major impediment for regeneration of injured axons in the central nervous system (CNS). The collagen-rich glial-fibrous scar contains numerous axon growth inhibitory factors forming a regeneration-barrier for axons. We demonstrated previously that the combination of the iron chelator 2,2'-bipyridine-5,5'-decarboxylic acid (BPY-DCA) and 8-Br-cyclic AMP (cAMP) inhibits scar formation and collagen deposition, leading to enhanced axon regeneration and partial functional recovery after spinal cord injury. While BPY-DCA is not a clinical drug, the clinically approved iron chelator deferoxamine mesylate (DFO) may be a suitable alternative for anti-scarring treatment (A…

Central Nervous SystemCollagen Type IVmedicine.medical_specialtyNeuriteCentral nervous systemlcsh:MedicineBiologyPharmacologyDeferoxamineIn Vitro TechniquesIron Chelating AgentsCicatrixIn vivoTransforming Growth Factor betamedicineCyclic AMPNeuritesAnimalsHumansRNA MessengerAxonRats Wistarlcsh:ScienceSpinal cord injurySpinal Cord InjuriesMultidisciplinaryDeferoxamine mesylatelcsh:RFibroblastsSpinal cordmedicine.diseaseAxonsSurgeryNerve RegenerationRatsDeferoxamineDisease Models Animalmedicine.anatomical_structureAstrocyteslcsh:QFemalemedicine.drugResearch ArticlePloS one
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Material-driven fibronectin assembly rescues matrix defects due to mutations in collagen IV in fibroblasts

2020

Basement membranes (BMs) are specialised extracellular matrices that provide structural support to tissues as well as influence cell behaviour and signalling. Mutations in COL4A1/COL4A2, a major BM component, cause a familial form of eye, kidney and cerebrovascular disease, including stroke, while common variants in these genes are a risk factor for intracerebral haemorrhage in the general population. These phenotypes are associated with matrix defects, due to mutant protein incorporation in the BM and/or its absence by endoplasmic reticulum (ER) retention. However, the effects of these mutations on matrix stiffness, the contribution of the matrix to the disease mechanism(s) and its effects…

Collagen Type IVCell signalingPopulationIntegrinBiophysicsBioengineering02 engineering and technologyMatrix (biology)medicine.disease_causeBasement MembraneArticleBiomaterialsExtracellular matrix03 medical and health sciences0302 clinical medicineLamininmedicineExtracellularHumanseducationCell adhesion030304 developmental biologyeducation.field_of_study0303 health sciencesMutationbiologyChemistryEndoplasmic reticulumFibroblasts021001 nanoscience & nanotechnologyPhenotypeExtracellular MatrixFibronectinsCell biologyFibronectinMechanics of MaterialsMutationCeramics and Compositesbiology.protein0210 nano-technology030217 neurology & neurosurgeryBiomaterials
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Different adhesins for type IV collagen on Candida albicans: identification of a lectin-like adhesin recognizing the 7S(IV) domain

2001

Adherence of the opportunistic pathogen Candida albicans to basement membrane (BM) proteins is considered a crucial step in the development of candidiasis. In this study the interactions of C. albicans yeast cells with the three main domains of type IV collagen, a major BM glycoprotein, were analysed. C. albicans adhered to the three immobilized domains by different mechanisms. Adhesion to the N-terminal cross-linking domain (7S) required the presence of divalent cations, whereas interaction with the central collagenous domain (CC) was cation-independent. Recognition of the C-terminal non-collagenous domain (NC1) was partially cation-dependent. Binding inhibition assays with the correspondi…

Collagen Type IVGlycosylationImmunoblottingOligosaccharidesBiologyMicrobiologyBasement MembraneType IV collagenOligosaccharide bindingCationsLectinsCandida albicansCell AdhesionAnimalsCandida albicanschemistry.chemical_classificationExtracellular Matrix ProteinsLectinOligosaccharidebiology.organism_classificationCorpus albicansBacterial adhesinchemistryBiochemistrybiology.proteinCattleGlycoproteinMicrobiology
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Genome-Wide Association Study of Diabetic Kidney Disease Highlights Biology Involved in Glomerular Basement Membrane Collagen

2019

BACKGROUND: Although diabetic kidney disease demonstrates both familial clustering and single nucleotide polymorphism heritability, the specific genetic factors influencing risk remain largely unknown.METHODS: To identify genetic variants predisposing to diabetic kidney disease, we performed genome-wide association study (GWAS) analyses. Through collaboration with the Diabetes Nephropathy Collaborative Research Initiative, we assembled a large collection of type 1 diabetes cohorts with harmonized diabetic kidney disease phenotypes. We used a spectrum of ten diabetic kidney disease definitions based on albuminuria and renal function.RESULTS: Our GWAS meta-analysis included association result…

Collagen Type IVMale0301 basic medicineEXPRESSIONNEPHROPATHY030232 urology & nephrologyPROTEINGenome-wide association studyRECEPTOR TYROSINE KINASESBiologySUSCEPTIBILITYBioinformaticsurologic and male genital diseasesAutoantigensNephropathyEnd stage renal diseaseCohort StudiesDiabetic nephropathy03 medical and health sciences0302 clinical medicineSDG 3 - Good Health and Well-beingDiabetes mellitusGlomerular Basement MembranemedicineHumansDiabetic NephropathiesAlport syndromeLetter to the EditorCOMPLICATIONSNITRIC-OXIDEMUTATIONS1184 Genetics developmental biology physiologyGeneral Medicinemedicine.diseaseGENE3. Good healthDiabetes Mellitus Type 1030104 developmental biologyNephrology3121 General medicine internal medicine and other clinical medicineMutationAlbuminuria/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingFemale3111 Biomedicinemedicine.symptomCOLLECTIN 11 CL-11Genome-Wide Association StudyKidney disease
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Novel form of X-linked nonsyndromic hearing loss with cochlear malformation caused by a mutation in the type IV collagen gene COL4A6

2013

Hereditary hearing loss is the most common human sensorineural disorder. Genetic causes are highly heterogeneous, with mutations detected in >40 genes associated with nonsyndromic hearing loss, to date. Whereas autosomal recessive and autosomal dominant inheritance is prevalent, X-linked forms of nonsyndromic hearing impairment are extremely rare. Here, we present a Hungarian three-generation family with X-linked nonsyndromic congenital hearing loss and the underlying genetic defect. Next-generation sequencing and subsequent segregation analysis detected a missense mutation (c.1771G>A, p.Gly591Ser) in the type IV collagen gene COL4A6 in all affected family members. Bioinformatic analysis an…

Collagen Type IVMaleHearing lossDNA Mutational AnalysisMolecular Sequence DataMutation MissenseGene ExpressionDeafnessBiologyCongenital hearing lossmedicine.disease_causeArticleType IV collagenotorhinolaryngologic diseasesGeneticsmedicineAnimalsHumansMissense mutationGenetic Predisposition to DiseaseAmino Acid SequenceAlport syndromeGeneCells CulturedGenetic Association StudiesZebrafishGenetics (clinical)GeneticsMutationGenetic Diseases X-LinkedMiddle Agedmedicine.diseaseCochleaPedigreeMice Inbred C57BLChild PreschoolFemaleRNA Splice SitesOtic vesiclemedicine.symptomEuropean Journal of Human Genetics
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Precise mapping of the Goodpasture epitope(s) using phage display, site-directed mutagenesis, and surface plasmon resonance.

2013

Goodpasture disease is an autoimmune disorder mediated by circulating autoantibodies against the noncollagenous-1 (NC1) domain of the alpha 3 chain of type IV collagen (alpha 3(IV)NC1). The structure of Goodpasture epitope(s) has been previously mapped into two main binding regions (E-A and E-B) of the alpha 3(IV)NC1 domain using a residue mutation approach on the highly related alpha 1(IV)NC1 domain. Here we combined phage display and surface plasmon resonance technology to more precisely localize the pathogenic binding sites. Peptides mimicking the Goodpasture epitope(s) were used to identify residues involved in autoantibody binding and found involvement of eight residues previously unre…

Collagen Type IVMalePhage displayautoantibodiesMutantMutagenesis (molecular biology technique)Enzyme-Linked Immunosorbent Assaycollagen type IVAutoantigensEpitopeType IV collagenHumansBinding siteSite-directed mutagenesisAutoantibodiesepitopeChemistryAutoantibodyGoodpasture diseaseMiddle AgedSurface Plasmon ResonanceMolecular biologyNephrologyMutagenesis Site-DirectedBinding Sites Antibodyphage displayCell Surface Display Techniquessurface plasmon resonanceEpitope MappingKidney international
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Vitamin A deficiency disturbs collagen IV and laminin composition and decreases matrix metalloproteinase concentrations in rat lung. Partial reversib…

2011

Vitamin A is essential for lung development and pulmonary cell differentiation. Its deficiency leads to altered lung structure and function and to basement membrane architecture and composition disturbances. Previously, we showed that lack of retinoids thickens the alveolar basement membrane and increases collagen IV, which are reversed by retinoic acid, the main biologically active vitamin A form. This study analyzed how vitamin A deficiency affects the subunit composition of collagen IV and laminin of lung basement membranes and pulmonary matrix metalloproteinase content, plus the recovering effect of all-trans-retinoic acid. Male weanling pups were fed a retinol-adequate/-deficient diet …

Collagen Type IVMaleVitaminmedicine.medical_specialtyEndocrinology Diabetes and MetabolismClinical BiochemistryRetinoic acidGene ExpressionTretinoinMatrix metalloproteinaseBiochemistryBasement Membranechemistry.chemical_compoundLamininInternal medicineGene expressionmedicineAnimalsRats WistarVitamin ALungMolecular BiologyBasement membraneNutrition and DieteticsLungbiologyVitamin A DeficiencyTissue Inhibitor of Metalloproteinasesmedicine.diseaseMatrix MetalloproteinasesRatsVitamin A deficiencymedicine.anatomical_structureEndocrinologyBiochemistrychemistrybiology.proteinFemaleLamininThe Journal of Nutritional Biochemistry
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Characterization of a Novel Type of Serine/Threonine Kinase That Specifically Phosphorylates the Human Goodpasture Antigen

1999

Goodpasture disease is an autoimmune disorder that occurs naturally only in humans. Also exclusive to humans is the phosphorylation process that targets the unique N-terminal region of the Goodpasture antigen. Here we report the molecular cloning of GPBP (Goodpasture antigen-binding protein), a previously unknown 624-residue polypeptide. Although the predicted sequence does not meet the conventional structural requirements for a protein kinase, its recombinant counterpart specifically binds to and phosphorylates the exclusive N-terminal region of the human Goodpasture antigen in vitro. This novel kinase is widely expressed in human tissues but shows preferential expression in the histologic…

Collagen Type IVMolecular Sequence DataSaccharomyces cerevisiaeProtein Serine-Threonine KinasesMolecular cloningBiologymedicine.disease_causeAutoantigensBiochemistryCell LineAutoimmunitymedicineHumansAmino Acid SequenceCloning MolecularPhosphorylationMolecular BiologyPeptide sequenceCeramide Transfer ProteinSerine/threonine-specific protein kinaseBase SequenceSequence Homology Amino AcidKinaseCell BiologyCeramide transportImmunohistochemistryCell biologyBiochemistryProtein BiosynthesisPhosphorylationCollagenJournal of Biological Chemistry
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