2020
Role of GUCA1C in Primary Congenital Glaucoma and in the Retina: Functional Evaluation in Zebrafish
Morales-Cámara S, Alexandre-Moreno S, Bonet-Fernández J, Atienzar-Aroca R, Aroca-Aguilar J, Ferre-Fernández J, Méndez C, Morales L, Fernández-Sánchez L, Cuenca N, Coca-Prados M, Martínez-de-la-Casa J, Garcia-Feijoo J, Escribano J. Role of GUCA1C in Primary Congenital Glaucoma and in the Retina: Functional Evaluation in Zebrafish. Genes 2020, 11: 550. PMID: 32422965, PMCID: PMC7288452, DOI: 10.3390/genes11050550.Peer-Reviewed Original ResearchMeSH KeywordsAdultAmino Acid SequenceAnimalsApoptosisBase SequenceCRISPR-Cas SystemsFemaleGene EditingGene Knockout TechniquesGlaucomaGliosisGuanylate Cyclase-Activating ProteinsHigh-Throughput Nucleotide SequencingHumansMaleMiddle AgedPedigreeRetinaReverse Transcriptase Polymerase Chain ReactionSequence AlignmentSequence Homology, Amino AcidZebrafishZebrafish ProteinsConceptsPrimary congenital glaucomaCongenital glaucomaRetinal ganglion cell layerRetinal ganglion cell apoptosisCiliary epitheliumGlial fibrillary acidic proteinWhole-exome sequencing analysisGanglion cell layerGanglion cell apoptosisHuman ocular ciliary epitheliumFibrillary acidic proteinOcular anterior segmentIntraocular pressure regulationOcular ciliary epitheliumNon-pigmented ciliary epitheliumAutosomal recessive fashionOptical neuropathyOcular effectsRetinal damageMüller cellsAnterior segmentPressure regulationAcidic proteinKnockout animalsGuanylate cyclaseCPAMD8 loss-of-function underlies non-dominant congenital glaucoma with variable anterior segment dysgenesis and abnormal extracellular matrix
Bonet-Fernández J, Aroca-Aguilar J, Corton M, Ramírez A, Alexandre-Moreno S, García-Antón M, Salazar J, Ferre-Fernández J, Atienzar-Aroca R, Villaverde C, Iancu I, Tamayo A, Méndez-Hernández C, Morales-Fernández L, Rojas B, Ayuso C, Coca-Prados M, Martinez-de-la-Casa J, García-Feijoo J, Escribano J. CPAMD8 loss-of-function underlies non-dominant congenital glaucoma with variable anterior segment dysgenesis and abnormal extracellular matrix. Human Genetics 2020, 139: 1209-1231. PMID: 32274568, DOI: 10.1007/s00439-020-02164-0.Peer-Reviewed Original ResearchMeSH KeywordsAdultAlpha-MacroglobulinsAnimalsAnterior ChamberCase-Control StudiesComplement C3CRISPR-Cas SystemsEmbryo, NonmammalianExtracellular MatrixEye AbnormalitiesFemaleGene EditingGene ExpressionGenes, RecessiveGlaucomaHigh-Throughput Nucleotide SequencingHumansLoss of Function MutationMaleMiddle AgedPedigreeTrabecular MeshworkTrabeculectomyTrypsin Inhibitor, Kazal PancreaticZebrafishConceptsZebrafish embryosAnterior segment dysgenesisExtracellular matrixPrimary congenital glaucomaNext-generation DNA sequencingGross developmental abnormalitiesFunction pathogenic mechanismQuantitative reverse transcription PCRAbnormal extracellular matrixCongenital glaucomaCRISPR/Mesenchyme-like cellsTrabecular meshwork cellsReverse transcription-PCRUnknown functionExtracellular matrix disorganizationDNA sequencingGenesGenetic alterationsEmbryosMeshwork cellsDevelopmental abnormalitiesTranscription-PCRAnterior chamber angleDisease Role
2018
Identification of myocilin as a blood plasma protein and analysis of its role in leukocyte adhesion to endothelial cell monolayers
Aroca-Aguilar JD, Fernández-Navarro A, Ontañón J, Coca-Prados M, Escribano J. Identification of myocilin as a blood plasma protein and analysis of its role in leukocyte adhesion to endothelial cell monolayers. PLOS ONE 2018, 13: e0209364. PMID: 30557320, PMCID: PMC6296516, DOI: 10.1371/journal.pone.0209364.Peer-Reviewed Original ResearchMeSH KeywordsAdultAgedAged, 80 and overBlood ProteinsBlotting, WesternCell AdhesionCytoskeletal ProteinsEye ProteinsFemaleGlycoproteinsHealthy VolunteersHEK293 CellsHuman Umbilical Vein Endothelial CellsHumansLeukocytesLiverMaleMiddle AgedProteolysisReal-Time Polymerase Chain ReactionRNA, MessengerThymus GlandConceptsPresence of myocilinEndothelial cell monolayersWestern immunoblotNon-ocular tissuesCell monolayersLymphoid organsLymphoid tissueT lymphocytesLeukocyte adhesionMatricellular proteinPlasma proteinsHuman myocilinLeukocytesMyocilinSerum proteinsPutative roleQuantitative PCRBlood plasmaLiverBiological activityAnti-adhesive proteinImmunoblotVivo proteolytic processingNew biological propertiesTissueThe Zinc-Metallothionein Redox System Reduces Oxidative Stress in Retinal Pigment Epithelial Cells
Rodríguez-Menéndez S, García M, Fernández B, Álvarez L, Fernández-Vega-Cueto A, Coca-Prados M, Pereiro R, González-Iglesias H. The Zinc-Metallothionein Redox System Reduces Oxidative Stress in Retinal Pigment Epithelial Cells. Nutrients 2018, 10: 1874. PMID: 30513827, PMCID: PMC6315569, DOI: 10.3390/nu10121874.Peer-Reviewed Original ResearchConceptsRetinal pigment epitheliumOxidative stressRetinal pigment epithelial cellsOxidative damagePre-treated cellsInduces oxidative stressPigment epithelial cellsNon-treated cellsReactive oxygen intermediatesΜM of zincPigment epitheliumRPE cellsZn-MTProtective mechanismEpithelial cellsFree radical generatorMT levelsAAPH treatmentOxygen intermediates
2013
Comparative proteomic study in serum of patients with primary open-angle glaucoma and pseudoexfoliation glaucoma
González-Iglesias H, Álvarez L, García M, Escribano J, Rodríguez-Calvo PP, Fernández-Vega L, Coca-Prados M. Comparative proteomic study in serum of patients with primary open-angle glaucoma and pseudoexfoliation glaucoma. Journal Of Proteomics 2013, 98: 65-78. PMID: 24355480, DOI: 10.1016/j.jprot.2013.12.006.Peer-Reviewed Original ResearchConceptsPrimary open-angle glaucomaOpen-angle glaucomaPseudoexfoliation glaucomaGlaucoma patientsInflammatory-related processesSera of patientsForms of glaucomaLarge population studiesPanel of candidatesAge-related blindnessSerum proteinsFunctional pathway analysisClinical manifestationsDietary agentsInflammatory processGlaucoma biomarkersHealthy controlsEarly diagnosisGlaucomaPatientsMajor causeSerumPopulation studiesTwo-dimensional fluorescent difference gel electrophoresisGenetic linkage studies
2002
Adult-Onset Primary Open-Angle Glaucoma Caused by Mutations in Optineurin
Rezaie T, Child A, Hitchings R, Brice G, Miller L, Coca-Prados M, Héon E, Krupin T, Ritch R, Kreutzer D, Crick RP, Sarfarazi M. Adult-Onset Primary Open-Angle Glaucoma Caused by Mutations in Optineurin. Science 2002, 295: 1077-1079. PMID: 11834836, DOI: 10.1126/science.1066901.Peer-Reviewed Original ResearchMeSH KeywordsAdultAlternative SplicingAmino Acid SequenceBrainCell Cycle ProteinsChromosome MappingChromosomes, Human, Pair 10Ciliary BodyExonsEye ProteinsFemaleGlaucoma, Open-AngleGolgi ApparatusHeterozygoteHumansIntraocular PressureMaleMembrane Transport ProteinsMiddle AgedMutationMutation, MissenseNerve Tissue ProteinsOcular HypertensionPedigreePolymorphism, Single-Stranded ConformationalRetinaTrabecular MeshworkTranscription Factor TFIIIAZinc FingersConceptsPrimary open-angle glaucomaHereditary primary open-angle glaucomaNormal intraocular pressureOpen-angle glaucomaAdult-onset primary open-angle glaucomaNeuroprotective roleIntraocular pressureAngle glaucomaTumor necrosisLeading causeTrabecular meshworkOPTN geneCiliary epitheliumCausative genesGlaucomaChromosome 10p14OptineurinSequence alterationsNecrosisRetinaIndividualsBrainEpithelium
2000
Expression of the TIGR gene in the iris, ciliary body, and trabecular meshwork of the human eye.
Huang W, Jaroszewski J, Ortego J, Escribano J, Coca-Prados M. Expression of the TIGR gene in the iris, ciliary body, and trabecular meshwork of the human eye. Ophthalmic Genetics 2000, 21: 155-69. PMID: 11035548, DOI: 10.1076/1381-6810(200009)21:3;1-z;ft155.Peer-Reviewed Original ResearchConceptsTIGR proteinTranscription/translation systemCanine pancreatic microsomal membranesPancreatic microsomal membranesSitu hybridization experimentsTissue-specific mannerTIGR genePattern of expressionCarboxy-terminus regionMajor protein bandsHybridization experimentsTerminus regionFusion proteinGlycosylation activityMolecular massProteinPNGase FDeglycosylation treatmentProtein bandsMicrosomal membranesTranslation systemO-glycosidaseJuvenile-onset primary open-angle glaucomaGenes
1999
A3 adenosine receptors regulate Cl−channels of nonpigmented ciliary epithelial cells
Mitchell C, Peterson-Yantorno K, Carré D, McGlinn A, Coca-Prados M, Stone R, Civan M. A3 adenosine receptors regulate Cl−channels of nonpigmented ciliary epithelial cells. American Journal Of Physiology 1999, 276: c659-c666. PMID: 10069993, DOI: 10.1152/ajpcell.1999.276.3.c659.Peer-Reviewed Original ResearchConceptsAgonist N6HCE cellsIB-MECAA3 receptorsAdenosine receptorsCiliary processesA2A agonist CGS 21680Rabbit ciliary processesCiliary epitheliumA1-selective agonist N6Specific adenosine receptorsAgonist CGS 21680NPE cellsCl- channelsNonpigmented ciliary epithelial cellsA3 adenosine receptorHuman NPE cellsCGS 21680Ciliary epithelial cellsReceptor subtypesIntracellular Ca2MicroM adenosineRabbit ciliary epitheliumRT-PCREpithelial cells
1997
The prostaglandin transporter is widely expressed in ocular tissues
Schuster V, Lu R, Coca-Prados M. The prostaglandin transporter is widely expressed in ocular tissues. Survey Of Ophthalmology 1997, 41: s41-s45. PMID: 9154275, DOI: 10.1016/s0039-6257(97)80006-9.Peer-Reviewed Original Research
1996
Identification of a Neuropeptide and Neuropeptide‐Processing Enzymes in Aqueous Humor Confers Neuroendocrine Features to the Human Ocular Ciliary Epithelium
Ortego J, Escribano J, Crabb J, Coca‐Prados M. Identification of a Neuropeptide and Neuropeptide‐Processing Enzymes in Aqueous Humor Confers Neuroendocrine Features to the Human Ocular Ciliary Epithelium. Journal Of Neurochemistry 1996, 66: 787-796. PMID: 8592153, DOI: 10.1046/j.1471-4159.1996.66020787.x.Peer-Reviewed Original ResearchMeSH KeywordsAdultAgedAnimalsAqueous HumorBase SequenceCarboxypeptidase HCarboxypeptidasesCell LineChild, PreschoolChromograninsCiliary BodyEpithelial CellsEpitheliumFluorescent Antibody Technique, IndirectHumansMixed Function OxygenasesMolecular Sequence DataMultienzyme ComplexesNeurosecretory SystemsProteinsRatsConceptsNeuropeptide processing enzymesCarboxypeptidase ECiliary epithelial cellsOcular ciliary epitheliumSecretogranin IICell-cell communicationEpithelial cellsHuman ocular ciliary epitheliumCDNA clonesCell signalingNonpigmented ciliary epithelial cellsCultured ciliary epithelial cellsProcessing enzymesMolecular markersPeptidylglycine alphaPhorbol esterSpecialized groupSpecific probesMammalian eyeNeuroendocrine tissuesEnzymeCiliary epitheliumKey functionsCellsPolymerase chain reaction
1995
Isolation and Characterization of Cell-Specific cDNA Clones from a Subtractive Library of the Ocular Ciliary Body of a Single Normal Human Donor: Transcription and Synthesis of Plasma Proteins1
Escribano J, Ortego J, Coca-Prados M. Isolation and Characterization of Cell-Specific cDNA Clones from a Subtractive Library of the Ocular Ciliary Body of a Single Normal Human Donor: Transcription and Synthesis of Plasma Proteins1. The Journal Of Biochemistry 1995, 118: 921-931. PMID: 8749308, DOI: 10.1093/jb/118.5.921.Peer-Reviewed Original ResearchConceptsSubtractive cDNA libraryOcular ciliary bodyCDNA clonesCDNA libraryCell-restricted expressionPartial DNA sequencesCell-specific genesPotential candidate genesSubtractive libraryComplement component C4Significant homologyHomology searchProtein databaseDNA sequencesCiliary bodyCandidate genesTranscriptional expressionNorthern hybridizationSignificant genesGenesIntraocular pressureCiliary epithelial cellsPlasma proteinsProteinVascular endothelial cells