2009
ADAMTS-7, a Direct Target of PTHrP, Adversely Regulates Endochondral Bone Growth by Associating with and Inactivating GEP Growth Factor
Bai X, Wang D, Kong L, Zhang Y, Luan Y, Kobayashi T, Kronenberg H, Yu X, Liu C. ADAMTS-7, a Direct Target of PTHrP, Adversely Regulates Endochondral Bone Growth by Associating with and Inactivating GEP Growth Factor. Molecular And Cellular Biology 2009, 29: 4201-4219. PMID: 19487464, PMCID: PMC2715794, DOI: 10.1128/mcb.00056-09.Peer-Reviewed Original ResearchMeSH KeywordsADAM ProteinsADAMTS7 ProteinAnimalsBlotting, WesternBone and BonesBone DevelopmentCell DifferentiationCell LineCell Line, TumorChondrocytesGene Expression ProfilingHumansImmunohistochemistryImmunoprecipitationIntercellular Signaling Peptides and ProteinsMiceMice, KnockoutParathyroid Hormone-Related ProteinProgranulinsProtein BindingProtein PrecursorsReverse Transcriptase Polymerase Chain ReactionTissue Culture TechniquesTwo-Hybrid System TechniquesConceptsADAMTS-7Granulin-epithelin precursorEndochondral bone formationEndochondral bone growthGrowth factorBone formationChondrocyte differentiationBone growthDirect targetAutocrine growth factorGrowth plate chondrocytesProteolytic activityPTHrPChondrogenic growth factorsChondrocyte hypertrophyExtracellular matrix proteinsCartilage extracellular matrix proteinsImportant targetADAMTS familyInhibitionSkeletal developmentMatrix proteinsExpression patternsExtracellular matrixArthritis
2007
The Retinoblastoma Protein Is an Essential Mediator of Osteogenesis That Links the p204 Protein to the Cbfa1 Transcription Factor Thereby Increasing Its Activity*
Luan Y, Yu XP, Xu K, Ding B, Yu J, Huang Y, Yang N, Lengyel P, Di Cesare PE, Liu CJ. The Retinoblastoma Protein Is an Essential Mediator of Osteogenesis That Links the p204 Protein to the Cbfa1 Transcription Factor Thereby Increasing Its Activity*. Journal Of Biological Chemistry 2007, 282: 16860-16870. PMID: 17439944, DOI: 10.1074/jbc.m610943200.Peer-Reviewed Original ResearchConceptsGene activationTranscription factorsRetinoblastoma proteinProtein-protein interactionsChromatin immunoprecipitation assaysMesenchymal cell lineSkeletal muscle myotubesP204 expressionP204 proteinCore-binding factor alpha1Numerous proteinsImmunoprecipitation assaysSuch mutantsOsteocalcin geneReporter geneGene expressionAntisense RNAMuscle myotubesOsteoblast differentiationCbfa1Factor alpha1ProteinEssential mediatorTernary complexCell lines
2006
ADAMTS-12 Associates with and Degrades Cartilage Oligomeric Matrix Protein*
Liu C, Kong W, Xu K, Luan Y, Ilalov K, Sehgal B, Yu S, Howell R, Di Cesare P. ADAMTS-12 Associates with and Degrades Cartilage Oligomeric Matrix Protein*. Journal Of Biological Chemistry 2006, 281: 15800-15808. PMID: 16611630, PMCID: PMC1483932, DOI: 10.1074/jbc.m513433200.Peer-Reviewed Original ResearchConceptsCartilage oligomeric matrix proteinADAMTS-12Matrix proteinsOligomeric matrix proteinCOMP degradationNoncollagenous matrix componentsSynovium of patientsProgression of arthritisEpidermal growth factor-like repeat domainRepeat domainExtracellular matrix breakdownFunctional domainsArticular cartilageMolecular mechanismsArthritis patientsRheumatoid arthritisSynovial fluidMatrix breakdownArthritisMatrix componentsDegradative fragmentsPatientsSynoviumProteinNormal cartilage