2009
Functional Role of Proteolytic Processing of Recombinant Myocilin in Self-Aggregation
Aroca-Aguilar JD, Martínez-Redondo F, Sánchez-Sánchez F, Coca-Prados M, Escribano J. Functional Role of Proteolytic Processing of Recombinant Myocilin in Self-Aggregation. Investigative Ophthalmology & Visual Science 2009, 51: 72-78. PMID: 19696176, PMCID: PMC2869055, DOI: 10.1167/iovs.09-4118.Peer-Reviewed Original Research
2007
Characterization of the Intracellular Proteolytic Cleavage of Myocilin and Identification of Calpain II as a Myocilin-processing Protease*
Sánchez-Sánchez F, Martínez-Redondo F, Aroca-Aguilar JD, Coca-Prados M, Escribano J. Characterization of the Intracellular Proteolytic Cleavage of Myocilin and Identification of Calpain II as a Myocilin-processing Protease*. Journal Of Biological Chemistry 2007, 282: 27810-27824. PMID: 17650508, DOI: 10.1074/jbc.m609608200.Peer-Reviewed Original ResearchConceptsExtracellular calciumCalpain IICalcium-activated proteaseIntraocular pressureT cellsIntracellular proteolytic cleavageCalpain inhibitorsCalcium uptakeProteolytic cleavageCalpain inhibitor IVOlfactomedin-like domainCalpain IInhibitor IVMyocilinEndoplasmic reticulumIntracellular processingLumenRNA interference knockdownCalciumProteolytic processingCellsCulture mediumGlaucomaSubcellular fractionationEndoproteolytic processing
2005
Myocilin Mutations Causing Glaucoma Inhibit the Intracellular Endoproteolytic Cleavage of Myocilin between Amino Acids Arg226 and Ile227 *
Aroca-Aguilar JD, Sánchez-Sánchez F, Ghosh S, Coca-Prados M, Escribano J. Myocilin Mutations Causing Glaucoma Inhibit the Intracellular Endoproteolytic Cleavage of Myocilin between Amino Acids Arg226 and Ile227 *. Journal Of Biological Chemistry 2005, 280: 21043-21051. PMID: 15795224, DOI: 10.1074/jbc.m501340200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsArginineBlotting, WesternBrefeldin ACattleCell LineComputational BiologyCOS CellsCulture MediaCytoskeletal ProteinsExtracellular Matrix ProteinsEye ProteinsGlaucomaGlycoproteinsGreen Fluorescent ProteinsHumansIsoleucineLeucineMicroscopy, FluorescenceMolecular Sequence DataMutationPeptidesPhenotypeProtein Structure, TertiarySpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTransfectionConceptsMyocilin mutationPathogenesis of glaucomaCause of blindnessSevere glaucoma phenotypeHuman aqueous humorAqueous humorOcular tissuesGlaucoma phenotypeNonocular tissuesWestern immunoblot analysisGlaucomaPathogenic mutationsOlfactomedin-like domainEndoproteolytic processingWild-type myocilinCell linesImmunoblot analysisMyocilinEndoproteolytic cleavageLeucine zipper-like domainMutant myocilinNormal roleHuman organsInhibitionTissue
2004
The bovine iris–ciliary epithelium expresses components of rod phototransduction
Ghosh S, Salvador-Silva M, Coca-Prados M. The bovine iris–ciliary epithelium expresses components of rod phototransduction. Neuroscience Letters 2004, 370: 7-12. PMID: 15489008, DOI: 10.1016/j.neulet.2004.07.026.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornArrestinBlotting, NorthernBlotting, WesternCattleCiliary BodyEpitheliumEye ProteinsGene ExpressionG-Protein-Coupled Receptor Kinase 1IrisLight Signal TransductionNeuronsPromoter Regions, GeneticProtein KinasesRetinal Rod Photoreceptor CellsReverse Transcriptase Polymerase Chain ReactionRhodopsinRNA, MessengerTransfectionConceptsCiliary epitheliumIris cellsBasal activityCommon embryonic originOcular ciliary epitheliumNeural retinaWestern blotRT-PCR amplificationRetinaEpitheliumSignificant stimulationBovine irisEmbryonic originStimulationBlotRod phototransductionTransient transfectionNorthern blotRhodopsin kinasePromoter activityDistal promoter elementLow levelsIrisReporter constructsLower vertebratesIdentification of Target Genes Regulated by FOXC1 Using Nickel Agarose–Based Chromatin Enrichment
Tamimi Y, Lines M, Coca-Prados M, Walter MA. Identification of Target Genes Regulated by FOXC1 Using Nickel Agarose–Based Chromatin Enrichment. Investigative Ophthalmology & Visual Science 2004, 45: 3904-3913. PMID: 15505035, DOI: 10.1167/iovs.04-0628.Peer-Reviewed Original ResearchConceptsChromatin enrichmentIsolation of chromatinChromatin immunoprecipitation assaysTight electrostatic interactionUncharacterized genesChromatin complexesFOXC1 proteinNickel agaroseImmunoprecipitation assaysPoor quality sequencesTarget genesAntibody availabilityCellular eventsCell cycleHistidine residuesGenesFOXC1Biochemical analysisClonesPCR amplificationChromatinIndependent assaysOcular developmentProteinEpithelium cells
1989
Receptor-mediated phosphoinositide hydrolysis in human ocular ciliary epithelial cells.
Wax M, Coca-Prados M. Receptor-mediated phosphoinositide hydrolysis in human ocular ciliary epithelial cells. Investigative Ophthalmology & Visual Science 1989, 30: 1675-9. PMID: 2545648.Peer-Reviewed Original ResearchConceptsPI hydrolysisReceptor-mediated phosphoinositide hydrolysisEpithelial cellsSelective muscarinic antagonistsInositol phosphatesAccumulation of inositolHydrolysis of phosphoinositidesOcular ciliary epitheliumAFDX-116M3 subtypeMuscarinic antagonistMuscarinic receptorsPutative neurotransmittersEC50 valuesPharmacologic characteristicsCiliary epithelial cellsPeripheral tissuesSpecific antagonistPI breakdownPhosphoinositide hydrolysisArginine vasopressinNonpigmented layerOcular ciliary epithelial cellsCiliary epitheliumMicroCi/