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 ResearchLocalization of Multidrug Resistance-Associated Protein 2 in the Nonpigmented Ciliary Epithelium of the Eye
Pelis RM, Shahidullah M, Ghosh S, Coca-Prados M, Wright SH, Delamere NA. Localization of Multidrug Resistance-Associated Protein 2 in the Nonpigmented Ciliary Epithelium of the Eye. Journal Of Pharmacology And Experimental Therapeutics 2009, 329: 479-485. PMID: 19201990, PMCID: PMC2672870, DOI: 10.1124/jpet.108.149625.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsATP Binding Cassette Transporter, Subfamily BBlotting, WesternCiliary BodyElectrophoresis, Polyacrylamide GelEpitheliumHumansIn Vitro TechniquesProtein TransportReverse Transcriptase Polymerase Chain ReactionRNASwineConceptsNonpigmented epitheliumMicroM MK571Ciliary bodyMultidrug resistance associated protein 2Therapeutic drugsMrp2 proteinIntracellular accumulationBlood-aqueous barrierNonpigmented ciliary epitheliumProtein 2Human ciliary bodyMicroM indomethacinMRP inhibitorsIntraocular tissuesAqueous humorApical membraneMRP2 mRNAWestern blotMultidrug resistanceCiliary epitheliumMicroM cyclosporinPorcine eyesMRP2Cell layerNative human
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
1992
Expression and cellular distribution of the al gap junction gene product in the ocular pigmented ciliary epithelium
Coca-Prados M, Ghosh S, Gilula N, Kumar N. Expression and cellular distribution of the al gap junction gene product in the ocular pigmented ciliary epithelium. Current Eye Research 1992, 11: 113-122. PMID: 1374005, DOI: 10.3109/02713689209000061.Peer-Reviewed Original ResearchConceptsPigmented ciliary epithelial cellsGene productsCiliary epithelial cellsApical plasma membrane domainPlasma membrane domainsEpithelial cellsAlpha 3Plasma membrane regionGap junction genesPE cellsNorthern blot analysisGap junction proteinImmunofluorescence localization studiesAlpha 1 transcriptsIndirect immunofluorescence localization studiesIntact tissueMembrane domainsAlpha 1 mRNABeta 1Predominant transcriptGap junction mRNAMembrane regionsJunction genesLocalization studiesCell types
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 ResearchMeSH KeywordsCells, CulturedCiliary BodyElectrophoresis, Polyacrylamide GelEpitheliumHydrolysisInositol PhosphatesParasympathomimeticsPhosphatidylinositolsReceptors, MuscarinicSimian virus 40TransfectionConceptsPI 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/
1985
Regulation of protein phosphorylation of the intermediate-sized filament vimentin in the ciliary epithelium of the mammalian eye.
Coca-Prados M. Regulation of protein phosphorylation of the intermediate-sized filament vimentin in the ciliary epithelium of the mammalian eye. Journal Of Biological Chemistry 1985, 260: 10332-10338. PMID: 4019517, DOI: 10.1016/s0021-9258(17)39252-9.Peer-Reviewed Original ResearchConceptsBeta-adrenergic agonistsMammalian eyeAlpha-adrenergic agonist phenylephrineBeta-adrenergic antagonist timololCiliary epitheliumCultured ciliary epithelial cellsCyclic AMPCellular cyclic AMPEpithelial-derived cellsAgonist phenylephrineCiliary epithelial cellsProstaglandin E1Catecholamine hormonesMicroM forskolinSerum-free mediumCiliary processesMonoclonal antibodiesRabbit ciliary processesVimentinAdenylate cyclaseEpithelial cellsPhosphorylation of vimentinIndirect immunofluorescence microscopyIntermediate-sized filamentsAgonists
1979
Intracellular forms of simian virus 40 nucleoprotein complexes. II. Biochemical and electron microscopic analysis of simian virus 40 virion assembly
Coca-Prados M, Hsu M. Intracellular forms of simian virus 40 nucleoprotein complexes. II. Biochemical and electron microscopic analysis of simian virus 40 virion assembly. Journal Of Virology 1979, 31: 199-208. PMID: 228054, PMCID: PMC353436, DOI: 10.1128/jvi.31.1.199-208.1979.Peer-Reviewed Original ResearchCapsidCentrifugation, Density GradientDNA, ViralElectrophoresis, Polyacrylamide GelMicroscopy, ElectronMorphogenesisSimian virus 40Viral ProteinsVirion