2024
The Increased Burden of Rare Variants in Four Matrix Metalloproteinase-Related Genes in Childhood Glaucoma Suggests a Complex Genetic Inheritance of the Disease
Tevar A, Aroca-Aguilar J, Bonet-Fernández J, Atienzar-Aroca R, Campos-Mollo E, Méndez-Hernández C, Morales-Fernández L, Palmer I, Coca-Prados M, Martinez-de-la-Casa J, Garcia-Feijoo J, Escribano J. The Increased Burden of Rare Variants in Four Matrix Metalloproteinase-Related Genes in Childhood Glaucoma Suggests a Complex Genetic Inheritance of the Disease. International Journal Of Molecular Sciences 2024, 25: 5757. PMID: 38891949, PMCID: PMC11171635, DOI: 10.3390/ijms25115757.Peer-Reviewed Original ResearchChildhood glaucomaGene variantsIncreased burden of rare variantsChildhood glaucoma patientsEarly-onset glaucomaIrreversible optic neuropathyAnterior eye chamberRare variantsPartial loss-of-function effectsLoss-of-function effectProportion of rare variantsBurden of rare variantsComplex genetic inheritanceGlaucoma patientsGlaucoma typePrimary glaucomaOptic neuropathyMutational burdenAnterior segmentEndoplasmic reticulum stressEye chamberT cellsHEK 293T cellsGlaucomaNext-generation sequencing
2011
Interaction of Recombinant Myocilin with the Matricellular Protein SPARC: Functional Implications
Aroca-Aguilar JD, Sánchez-Sánchez F, Ghosh S, Fernández-Navarro A, Coca-Prados M, Escribano J. Interaction of Recombinant Myocilin with the Matricellular Protein SPARC: Functional Implications. Investigative Ophthalmology & Visual Science 2011, 52: 179-189. PMID: 20926826, PMCID: PMC3053273, DOI: 10.1167/iovs.09-4866.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBlotting, WesternCalcium-Binding ProteinsCell LineChromatography, High Pressure LiquidCytoskeletal ProteinsExtracellular Matrix ProteinsEye ProteinsGene Expression ProfilingGlycoproteinsHumansKidneyMicroscopy, FluorescenceMolecular Sequence DataOsteonectinPolymerase Chain ReactionProtein BindingRecombinant Fusion ProteinsRecombinant ProteinsTwo-Hybrid System TechniquesConceptsHEK 293T cellsSolid-phase binding assaysInteraction of myocilinRecombinant proteinsRecombinant myocilinMatricellular proteinEC domainTerminal olfactomedin domainTwo-hybrid analysisTwo-hybrid systemProtein-protein interactionsFull-length myocilinC-terminal domainN-terminal domainC-terminal regionCalcium binding domainsBinding assaysOlfactomedin domainC-terminal fragmentBinding domainsLinker regionUnknown functionExtracellular glycoproteinIntracellular interactionsSPARC family
2008
Heterozygous expression of myocilin glaucoma mutants increases secretion of the mutant forms and reduces extracellular processed myocilin.
Aroca-Aguilar JD, Sánchez-Sánchez F, Martínez-Redondo F, Coca-Prados M, Escribano J. Heterozygous expression of myocilin glaucoma mutants increases secretion of the mutant forms and reduces extracellular processed myocilin. Molecular Vision 2008, 14: 2097-108. PMID: 19023451, PMCID: PMC2585175.Peer-Reviewed Original ResearchConceptsWild-type myocilinWild-type proteinMyocilin mutantsMutant myocilinMutant formsProteolytic processingMissense mutant formsHEK 293T cellsMyocilin geneMutant proteinsSecretory pathwayUnidentified functionExtracellular proteinsMutantsEndoproteolytic processingRecombinant mutantsMyocilin secretionCellular fractionsHeterozygous expressionMyocilinProteinUnknown mechanismExtracellular amountSDS-PAGEHeterozygous state