2024
Neuroendocrine Properties of the Ciliary Epithelium
Coca-Prados M. Neuroendocrine Properties of the Ciliary Epithelium. 2024 DOI: 10.1016/b978-0-443-13820-1.00083-9.Peer-Reviewed Original ResearchGene expressionExpression of bioactive peptidesIdentity of genesGene expression of enzymesMicroarray-based analysisExpression of enzymesSensor proteinsRegulate metabolismGenesPhysiological processesCiliary epitheliumPhysiological functionsT4 to T3Neuronal Ca2Neuroendocrine propertiesVasoconstrictive functionVasoactive aminesPeptide receptorBioactive peptidesIon channelsMetabolismPeptideEyesEnzymeProtein
2017
Whole-Exome Sequencing of Congenital Glaucoma Patients Reveals Hypermorphic Variants in GPATCH3, a New Gene Involved in Ocular and Craniofacial Development
Ferre-Fernández JJ, Aroca-Aguilar JD, Medina-Trillo C, Bonet-Fernández JM, Méndez-Hernández CD, Morales-Fernández L, Corton M, Cabañero-Valera MJ, Gut M, Tonda R, Ayuso C, Coca-Prados M, García-Feijoo J, Escribano J. Whole-Exome Sequencing of Congenital Glaucoma Patients Reveals Hypermorphic Variants in GPATCH3, a New Gene Involved in Ocular and Craniofacial Development. Scientific Reports 2017, 7: 46175. PMID: 28397860, PMCID: PMC5387416, DOI: 10.1038/srep46175.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarrier ProteinsChromosome SegregationEmbryo, NonmammalianExome SequencingEyeFaceFamilyFemaleGene Expression Regulation, DevelopmentalGene Knockdown TechniquesGlaucomaHumansMaleMiddle AgedMutationOrgan SpecificityPedigreePhenotypePromoter Regions, GeneticReceptors, CXCR4SkullSubcellular FractionsTranscriptional ActivationZebrafishConceptsNew genesZebrafish embryosCraniofacial developmentEarly zebrafish embryosNeural crest cell migrationCrest cell migrationNew disease genesMesenchymal-like cellsHigh genetic heterogeneityUnidentified functionTransient overexpressionProximal promoterDisease genesGene Pitx2Whole-exome sequencingGenesCell migrationGenetic heterogeneityExome sequencingSkeletal muscleRare variantsCraniofacial abnormalitiesEmbryosSequencingProteinQuantitative distribution of Zn, Fe and Cu in the human lens and study of the Zn–metallothionein redox system in cultured lens epithelial cells by elemental MS
González-Iglesias H, Petrash C, Rodríguez-Menéndez S, García M, Álvarez L, Fernández-Vega Cueto L, Fernández B, Pereiro R, Sanz-Medel A, Coca-Prados M. Quantitative distribution of Zn, Fe and Cu in the human lens and study of the Zn–metallothionein redox system in cultured lens epithelial cells by elemental MS. Journal Of Analytical Atomic Spectrometry 2017, 32: 1746-1756. DOI: 10.1039/c6ja00431h.Peer-Reviewed Original ResearchLens epithelial cellsMolecular mass proteinsMass proteinsCultured human lens epithelial cellsHigh molecular mass proteinsEpithelial cellsCultured lens epithelial cellsHuman lens epithelial cellsHuman lensOxidative cellular damageLocalization of ZnEndogenous stressorsImportant enzymeMT proteinCellular distributionLens epithelial cell layerProteinRedox systemEpithelial cell layerElemental mass spectrometryCellular damageMetallothioneinOxidative stressHuman lensesCells
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
2004
Identification 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
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 glaucomaGenesExpression 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: 155-169. DOI: 10.1076/1381-6810(200009)2131-zft155.Peer-Reviewed Original ResearchTIGR 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
Effects of hypotonic swelling on the cellular distribution and expression of pICln in human nonpigmented ciliary epithelial cells
Sánchez-Torres J, Huang W, Civan M, Coca-Prados M. Effects of hypotonic swelling on the cellular distribution and expression of pICln in human nonpigmented ciliary epithelial cells. Current Eye Research 1999, 18: 408-416. PMID: 10435827, DOI: 10.1076/ceyr.18.6.408.5266.Peer-Reviewed Original ResearchConceptsOpen reading frameCiliary epithelial cellsPlasma membraneFusion proteinWestern blot analysisEpithelial cellsCellular distributionTag fusion proteinCandidate gene productsBlot analysisHuman nonpigmented ciliary epithelial cellsTotal cell extractsHypotonic treatmentHuman ciliary epithelial cellsMammalian cellsPolyclonal antibodiesReading frameGene productsNonpigmented ciliary epithelial cellsCultured ciliary epithelial cellsPerinuclear regionCellular localizationCell extractsCultured cellsProtein
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
1987
Evidence that the α and α(+) isoforms of the catalytic subunit of (Na+,K+)-ATPase reside in distinct ciliary epithelial cells of the mammalian eye
Coca-Prados M, López-Briones L. Evidence that the α and α(+) isoforms of the catalytic subunit of (Na+,K+)-ATPase reside in distinct ciliary epithelial cells of the mammalian eye. Biochemical And Biophysical Research Communications 1987, 145: 460-466. PMID: 3036129, DOI: 10.1016/0006-291x(87)91343-x.Peer-Reviewed Original ResearchConceptsCatalytic subunitCiliary epithelial cellsEpithelial cellsNPE cellsCultured ciliary epithelial cellsBasolateral surfaceImmunoblot analysisCiliary processesIntact ciliary processesMammalian eyeATPasePE cellsSubunitsPolyclonal antibodiesCanine kidneyCellsAlpha formAlphaIndirect immunofluorescenceIsoformsProteinBovine eyes
1983
Protein Phosphorylation in Cultured Human Ciliary Epithelia in Response to Activators of Adenylate Cyclase, Cyclic AMP and Analogues
Coca-Prados M, Kondo K, Sears M. Protein Phosphorylation in Cultured Human Ciliary Epithelia in Response to Activators of Adenylate Cyclase, Cyclic AMP and Analogues. 1983, 1-6. DOI: 10.1007/978-3-642-69096-9_1.Peer-Reviewed Original ResearchSpecific substrate proteinsDiverse cell systemsProtein kinase activityState of phosphorylationCyclic AMPSubstrate proteinsProtein phosphorylationEndogenous proteinsKinase activitySecond messengerHuman ciliary epitheliumPhosphorylationMembrane permeabilityProteinCell systemAdenylate cyclaseCiliary epitheliumBiologic responseMessengerActivatorAMPCyclaseResponse