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
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