2015
LOXL1 gene variants and their association with pseudoexfoliation glaucoma (XFG) in Spanish patients
Álvarez L, García M, González-Iglesias H, Escribano J, Rodríguez-Calvo PP, Fernández-Vega L, Coca-Prados M. LOXL1 gene variants and their association with pseudoexfoliation glaucoma (XFG) in Spanish patients. BMC Medical Genomics 2015, 16: 72. PMID: 26319397, PMCID: PMC4593192, DOI: 10.1186/s12881-015-0221-y.Peer-Reviewed Original Research
2011
WDR36 and P53 Gene Variants and Susceptibility to Primary Open-Angle Glaucoma: Analysis of Gene-Gene Interactions
Blanco-Marchite C, Sánchez-Sánchez F, López-Garrido MP, Iñigez-de-Onzoño M, López-Martínez F, López-Sánchez E, Alvarez L, Rodríguez-Calvo PP, Méndez-Hernández C, Fernández-Vega L, García-Sánchez J, Coca-Prados M, García-Feijoo J, Escribano J. WDR36 and P53 Gene Variants and Susceptibility to Primary Open-Angle Glaucoma: Analysis of Gene-Gene Interactions. Investigative Ophthalmology & Visual Science 2011, 52: 8467-8478. PMID: 21931130, PMCID: PMC3208188, DOI: 10.1167/iovs.11-7489.Peer-Reviewed Original ResearchAgedAmino Acid SequenceBase SequenceCase-Control StudiesChromatography, High Pressure LiquidDNA Mutational AnalysisEpistasis, GeneticEye ProteinsFemaleGenetic Predisposition to DiseaseGenetic VariationGenotypeGlaucoma, Open-AngleHumansIntraocular PressureMaleMiddle AgedMolecular Sequence DataOcular HypertensionPolymerase Chain ReactionPolymorphism, Single NucleotideRegulatory Sequences, Nucleic AcidRisk FactorsSequence Analysis, DNATumor Suppressor Protein p53Interaction 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
2007
Role of MYOC and OPTN sequence variations in Spanish patients with primary open-angle glaucoma.
López-Martínez F, López-Garrido M, Sánchez-Sánchez F, Campos-Mollo E, Coca-Prados M, Escribano J. Role of MYOC and OPTN sequence variations in Spanish patients with primary open-angle glaucoma. Molecular Vision 2007, 13: 862-72. PMID: 17615537, PMCID: PMC2770203.Peer-Reviewed Original ResearchMeSH KeywordsAge of OnsetAmino Acid SequenceCell Cycle ProteinsCell LineCytoskeletal ProteinsExonsEye ProteinsFemaleGene FrequencyGenome, HumanGlaucoma, Open-AngleGlycoproteinsHaplotypesHumansLinkage DisequilibriumMaleMembrane Transport ProteinsMiddle AgedMolecular Sequence DataMutationOcular HypertensionOpen Reading FramesPhenotypePolymorphism, Single-Stranded ConformationalPromoter Regions, GeneticSpainTranscription Factor TFIIIAWhite PeopleConceptsPrimary open-angle glaucomaOcular hypertensionOpen-angle glaucomaPOAG patientsSpanish patientsSequence variationExons of myocilinHeterozygous disease-causing mutationsPathogenic mutationsSingle nucleotide polymorphismsPromoter regionRole of myocilinDNA sequence variationPolymorphic GT microsatelliteCommon single nucleotide polymorphismsPCR-DNA sequencingT cellsComplete coding regionPatientsUnrelated patientsMYOC geneOPTN geneGlaucomaDisease-causing mutationsGT microsatellite
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
2003
Production, purification, and functional analysis of recombinant human and mouse 17β-hydroxysteroid dehydrogenase type 7
Törn S, Nokelainen P, Kurkela R, Pulkka A, Menjivar M, Ghosh S, Coca-Prados M, Peltoketo H, Isomaa V, Vihko P. Production, purification, and functional analysis of recombinant human and mouse 17β-hydroxysteroid dehydrogenase type 7. Biochemical And Biophysical Research Communications 2003, 305: 37-45. PMID: 12732193, DOI: 10.1016/s0006-291x(03)00694-6.Peer-Reviewed Original ResearchConceptsPeripheral tissuesType 7Primary open-angle glaucomaEarly-onset prostate cancerOpen-angle glaucomaSex steroid hormonesIntracrine regulatorAdrenal glandProstate cancerEstrogenic milieuPotent androgenInactive metabolitesEstrogenic metabolitesSteroid metabolismPotent estrogenSteroid hormonesCancer 1DihydrotestosteroneRecombinant humanTissue distributionHormoneTissueHuman tissuesPresent studyMetabolic roleCRALBP transcriptional regulation in ciliary epithelial, retinal Müller and retinal pigment epithelial cells
Kennedy BN, Li C, Ortego J, Coca-Prados M, Sarthy VP, Crabb JW. CRALBP transcriptional regulation in ciliary epithelial, retinal Müller and retinal pigment epithelial cells. Experimental Eye Research 2003, 76: 257-260. PMID: 12565814, DOI: 10.1016/s0014-4835(02)00308-1.Peer-Reviewed Original ResearchConceptsTranscriptional regulationBinding Protein FunctionsCell-specific expressionPromoter analysisProtein functionRepressor elementEnhancer elementsPromoter constructsReporter activityRetinal pigment epithelial cellsPigment epithelial cellsCiliary epitheliumEpithelial cellsVisual cycleRPE cellsBPRegulationRetinal pigment epitheliumCellsMüller cellsGenesMutationsRLBP1 geneEpitheliumWildtype
1999
Identification, expression and chromosome localization of a human gene encoding a novel protein with similarity to the pilB family of transcriptional factors (pilin) and to bacterial peptide methionine sulfoxide reductases
Huang W, Escribano J, Sarfarazi M, Coca-Prados M. Identification, expression and chromosome localization of a human gene encoding a novel protein with similarity to the pilB family of transcriptional factors (pilin) and to bacterial peptide methionine sulfoxide reductases. Gene 1999, 233: 233-240. PMID: 10375640, DOI: 10.1016/s0378-1119(99)00131-6.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsBase SequenceChromosome MappingChromosomes, Human, Pair 10Ciliary BodyDNA, ComplementaryFluorescent Antibody Technique, IndirectHelicobacter pyloriHumansMethionine Sulfoxide ReductasesMicrofilament ProteinsMolecular Sequence DataOxidoreductasesPhylogenySequence Homology, Amino AcidStreptococcus pneumoniaeTranscription FactorsConceptsPeptide methionine sulfoxide reductaseCBS-1Ocular ciliary bodyChromosome localizationNovel proteinSignificant identitySulfoxide reductaseTranscription factorsCarboxyl terminusAmino acid sequence identityMammalian transcription factorsGlycine-rich proteinTerminal regionAmino acidsMethionine sulfoxide reductaseOpen reading frameRegulation of expressionAmino-terminal regionAmino acid sequenceCarboxyl-terminal regionMarkers WIIntergenic regionChromosome 10p12Human genesReading frameEffects 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
1998
Identification ofPKD2L,a HumanPKD2-Related Gene: Tissue-Specific Expression and Mapping to Chromosome 10q25
Wu G, Hayashi T, Park J, Dixit M, Reynolds D, Li L, Maeda Y, Cai Y, Coca-Prados M, Somlo S. Identification ofPKD2L,a HumanPKD2-Related Gene: Tissue-Specific Expression and Mapping to Chromosome 10q25. Genomics 1998, 54: 564-568. PMID: 9878261, DOI: 10.1006/geno.1998.5618.Peer-Reviewed Original ResearchAmino Acid SequenceBlotting, NorthernCalcium ChannelsChromosomes, Human, Pair 10Cloning, MolecularExpressed Sequence TagsGene Expression RegulationGenetic MarkersHumansLiverLiver DiseasesMembrane GlycoproteinsMembrane ProteinsMolecular Sequence DataOrgan SpecificityPhosphoproteinsPolycystic Kidney, Autosomal DominantPolymorphism, GeneticReceptors, Cell SurfaceRetinaSequence Homology, Amino AcidTissue DistributionTRPP Cation ChannelsSequence Analysis and Homology Modeling Suggest That Primary Congenital Glaucoma on 2p21 Results from Mutations Disrupting Either the Hinge Region or the Conserved Core Structures of Cytochrome P4501B1
Stoilov I, Akarsu A, Alozie I, Child A, Barsoum-Homsy M, Turacli M, Or M, Lewis R, Ozdemir N, Brice G, Aktan S, Chevrette L, Coca-Prados M, Sarfarazi M. Sequence Analysis and Homology Modeling Suggest That Primary Congenital Glaucoma on 2p21 Results from Mutations Disrupting Either the Hinge Region or the Conserved Core Structures of Cytochrome P4501B1. American Journal Of Human Genetics 1998, 62: 573-584. PMID: 9497261, PMCID: PMC1376958, DOI: 10.1086/301764.Peer-Reviewed Original Research
1997
Cloning and characterization of subtracted cDNAs from a human ciliary body library encoding TIGR, a protein involved in juvenile open angle glaucoma with homology to myosin and olfactomedin
Ortego J, Escribano J, Coca-Prados M. Cloning and characterization of subtracted cDNAs from a human ciliary body library encoding TIGR, a protein involved in juvenile open angle glaucoma with homology to myosin and olfactomedin. FEBS Letters 1997, 413: 349-353. PMID: 9280311, DOI: 10.1016/s0014-5793(97)00934-4.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCiliary BodyCloning, MolecularCytoskeletal ProteinsDNA, ComplementaryExtracellular Matrix ProteinsEyeEye ProteinsGene LibraryGlaucoma, Open-AngleGlycoproteinsHumansMolecular Sequence DataMyosinsOrgan SpecificityRNA, MessengerSequence Homology, Amino AcidSequence Homology, Nucleic Acid
1996
Association of ClC-3 Channel with Cl− Transport by Human Nonpigmented Ciliary Epithelial Cells
Coca-Prados M, Sánchez-Torres J, Peterson-Yantorno K, Civan M. Association of ClC-3 Channel with Cl− Transport by Human Nonpigmented Ciliary Epithelial Cells. The Journal Of Membrane Biology 1996, 150: 197-208. PMID: 8661780, DOI: 10.1007/s002329900044.Peer-Reviewed Original ResearchIdentification 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
Cell-specific expression of the human Na+,K(+)-ATPase beta 2 subunit isoform in the nonpigmented ciliary epithelium.
Coca-Prados M, Fernández-Cabezudo M, Sánchez-Torres J, Crabb J, Ghosh S. Cell-specific expression of the human Na+,K(+)-ATPase beta 2 subunit isoform in the nonpigmented ciliary epithelium. Investigative Ophthalmology & Visual Science 1995, 36: 2717-28. PMID: 7499094.Peer-Reviewed Original ResearchConceptsBeta 2 isoformNonpigmented ciliary epithelial cellsOcular tissuesCiliary epitheliumBeta 1NPE cell linesNonpigmented ciliary epitheliumNPE cellsHuman ocular tissuesSubunit isoformsBlot analysisATPase subunit isoformsSpecific anti-peptide antibodiesRestricted cellular distributionPolymerase chain reactionCiliary epithelial cellsBeta-subunit isoformsAlpha-subunit isoformsAnti-peptide antibodiesODM-2Polymerase chain reaction amplificationChain reaction amplificationHuman ciliary epitheliumCell-specific distributionPattern of expressionIsolation 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 cellsPKC-sensitive Cl- channels associated with ciliary epithelial homologue of pICln
Coca-Prados M, Anguita J, Chalfant M, Civan M. PKC-sensitive Cl- channels associated with ciliary epithelial homologue of pICln. American Journal Of Physiology 1995, 268: c572-c579. PMID: 7534980, DOI: 10.1152/ajpcell.1995.268.3.c572.Peer-Reviewed Original ResearchMeSH KeywordsAlkaloidsAnimalsBase SequenceBlotting, NorthernCells, CulturedChild, PreschoolChloride ChannelsCiliaCystic Fibrosis Transmembrane Conductance RegulatorElectric ConductivityEpitheliumHumansIon ChannelsKineticsMembrane ProteinsMolecular Sequence DataPolymerase Chain ReactionProtein Kinase CRatsRNA, MessengerStaurosporine
1994
Nucleotide sequence of a cDNA for the β2 subunit isoform of Na+, K+-ATPase from human retina
Hernando N, Martin-Vasallo P, Ghosh S, Ghosh P, Swaroop A, Coca-Prados M. Nucleotide sequence of a cDNA for the β2 subunit isoform of Na+, K+-ATPase from human retina. Biochimica Et Biophysica Acta 1994, 1189: 109-111. PMID: 8305453, DOI: 10.1016/0005-2736(94)90287-9.Peer-Reviewed Original Research
1993
Cloning of the Bovine Plasma Selenium-Dependent Glutathione Peroxidase (GP) cDNA from the Ocular Ciliary Epithelium: Expression of the Plasma and Cellular Forms within the Mammalian Eye1
Martín-Alonso J, Ghosh S, Coca-Prados M. Cloning of the Bovine Plasma Selenium-Dependent Glutathione Peroxidase (GP) cDNA from the Ocular Ciliary Epithelium: Expression of the Plasma and Cellular Forms within the Mammalian Eye1. The Journal Of Biochemistry 1993, 114: 284-291. PMID: 8262911, DOI: 10.1093/oxfordjournals.jbchem.a124168.Peer-Reviewed Original ResearchConceptsOcular ciliary epitheliumGlutathione peroxidase cDNAMammalian eyeCorresponding amino acid sequencesDifferential gene expressionOpen reading frameAmino acid sequenceBovine glutathione peroxidasePeroxidase cDNAMolecular cloningOverall identityReading frameHuman GPxAcid sequenceGene expressionCellular formCiliary epitheliumFunctional roleAmino acidsTranscriptsOxidative damageGlutathione peroxidaseCloningOxidative stressExpressionDifferential Expression of the Cellular Retinaldehyde-binding Protein in Bovine Ciliary Epithelium
Martı̀n-Alonso J, Ghosh S, Hernando N, Crabb J, Coca-Prados M. Differential Expression of the Cellular Retinaldehyde-binding Protein in Bovine Ciliary Epithelium. Experimental Eye Research 1993, 56: 659-669. PMID: 8595808, DOI: 10.1006/exer.1993.1083.Peer-Reviewed Original Research