Featured Publications
Progranulin Recruits HSP70 to β-Glucocerebrosidase and Is Therapeutic Against Gaucher Disease
Jian J, Tian Q, Hettinghouse A, Zhao S, Liu H, Wei J, Grunig G, Zhang W, Setchell K, Sun Y, Overkleeft H, Chan G, Liu C. Progranulin Recruits HSP70 to β-Glucocerebrosidase and Is Therapeutic Against Gaucher Disease. EBioMedicine 2016, 13: 212-224. PMID: 27789271, PMCID: PMC5264254, DOI: 10.1016/j.ebiom.2016.10.010.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineDisease Models, AnimalFibroblastsGaucher DiseaseGlucosylceramidaseHSP70 Heat-Shock ProteinsHumansIntercellular Signaling Peptides and ProteinsLysosome-Associated Membrane GlycoproteinsLysosomesMiceMice, KnockoutPhenotypeProgranulinsProtein AggregatesProtein BindingRecombinant ProteinsStress, PhysiologicalConceptsGaucher diseaseLysosomal storage diseaseStorage diseaseCommon lysosomal storage diseaseNew therapeutic interventionsΒ-glucocerebrosidaseProgranulin insufficiencyAnimal modelsTherapeutic interventionsDiseasePGRNDisease phenotypePatient fibroblastsGCaseComplex-associated proteinsLysosomal localizationHSP70Deficiency
2013
The promotion of bone healing by progranulin, a downstream molecule of BMP-2, through interacting with TNF/TNFR signaling
Zhao Y, Tian Q, Frenkel S, Liu C. The promotion of bone healing by progranulin, a downstream molecule of BMP-2, through interacting with TNF/TNFR signaling. Biomaterials 2013, 34: 6412-6421. PMID: 23746860, PMCID: PMC3713419, DOI: 10.1016/j.biomaterials.2013.05.030.Peer-Reviewed Original ResearchConceptsBone healing processBone formationHealing processEctopic bone formationTNF-α transgenic miceBone healingTNFR2-deficient miceRole of PGRNTreatment of fracturesTNF-α signalingEndochondral ossificationPotential molecular targetsEctopic bone formation modelInflammatory osteoclastogenesisTNF/TNFRPGRN deficiencyInflammatory conditionsDeficient miceRecombinant PGRNBone regenerationTransgenic micePGRNMiceCritical mediatorGrowth factor
2011
GEP constitutes a negative feedback loop with MyoD and acts as a novel mediator in controlling skeletal muscle differentiation
Wang D, Bai X, Tian Q, Lai Y, Lin E, Shi Y, Mu X, Feng J, Carlson C, Liu C. GEP constitutes a negative feedback loop with MyoD and acts as a novel mediator in controlling skeletal muscle differentiation. Cellular And Molecular Life Sciences 2011, 69: 1855-1873. PMID: 22179841, PMCID: PMC3319484, DOI: 10.1007/s00018-011-0901-5.Peer-Reviewed Original ResearchConceptsMyoD transcription factorGranulin-epithelin precursorTranscription factorsMyoblast fusionMyotube formationMuscle-specific transcription factorsC2C12 myoblast fusionE-box sequenceSkeletal muscle differentiationFusion of myoblastsNegative feedback loopGrowth factorEmbryonic developmentRegulatory regionsMuscle differentiationSkeletal muscle tissueC2C12 myoblastsRegulatory loopSiRNA approachNovel mediatorAutocrine growth factorJunBKnockdown miceMyoblastsTissue repair
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
2008
Regulation of chondrocyte differentiation by ADAMTS-12 metalloproteinase depends on its enzymatic activity
Bai X, Wang D, Luan Y, Yu X, Liu C. Regulation of chondrocyte differentiation by ADAMTS-12 metalloproteinase depends on its enzymatic activity. Cellular And Molecular Life Sciences 2008, 66: 667. PMID: 19151918, PMCID: PMC11131527, DOI: 10.1007/s00018-008-8633-x.Peer-Reviewed Original ResearchConceptsADAMTS-12Chondrocyte differentiationGrowth plate chondrocytesType X collagen expressionThrombospondin motifsPTHrPCollagen expressionAltered expressionMRNA levelsProminent expressionDownstream moleculesADAMTS familyMetalloproteinaseInhibitionEnzymatic activityNovel regulatorProteolytic activityChondrocytesExpressionChondrogenesisDifferentiationActivityMediation of Chondrogenic and Osteogenic Differentiation by an Interferon-Inducible p202 Protein
Kong L, Liu C. Mediation of Chondrogenic and Osteogenic Differentiation by an Interferon-Inducible p202 Protein. Cellular And Molecular Life Sciences 2008, 65: 3494-3506. PMID: 18791844, PMCID: PMC11131663, DOI: 10.1007/s00018-008-8342-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell DifferentiationCell LineChondrocytesChondrogenesisFeedback, PhysiologicalGene Expression Regulation, DevelopmentalGene Knockdown TechniquesGenes, ReporterGrowth PlateIntracellular Signaling Peptides and ProteinsMiceMice, Inbred C3HMice, KnockoutMice, TransgenicOsteoblastsOsteogenesisParathyroid Hormone-Related ProteinPluripotent Stem CellsRNA, Small InterferingSmad ProteinsConceptsParathyroid hormone-related peptideExpression of PTHrPHormone-related peptideCourse of osteogenesisGrowth plate chondrocytesInterferon-inducible proteinMolecular mechanism studiesInterferon-inducible p200 familyImportant mediatorP202 proteinOsteogenic differentiationSiRNA approachMouse embryosP202 expressionChondrocyte differentiationPositive feedback loopSmad transcription factorsTransgenic mouse embryosOsteoblast differentiationDifferential expressionExpressionC3H10T1/2 cellsC2C12 cellsDifferentiationCellsp204 Protein Overcomes the Inhibition of Core Binding Factor α-1–mediated Osteogenic Differentiation by Id Helix-Loop-Helix Proteins
Luan Y, Yu X, Yang N, Frenkel S, Chen L, Liu C. p204 Protein Overcomes the Inhibition of Core Binding Factor α-1–mediated Osteogenic Differentiation by Id Helix-Loop-Helix Proteins. Molecular Biology Of The Cell 2008, 19: 2113-2126. PMID: 18287524, PMCID: PMC2366862, DOI: 10.1091/mbc.e07-10-1057.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseAmino Acid SequenceAnimalsBone Morphogenetic Protein 2Bone Morphogenetic ProteinsCell DifferentiationCell LineCell NucleusCore Binding Factor alpha SubunitsFemaleHelix-Loop-Helix MotifsHumansInhibitor of Differentiation ProteinsMiceMice, Inbred BALB CNuclear Export SignalsNuclear ProteinsOsteoblastsOsteocalcinOsteogenesisPhosphoproteinsPromoter Regions, GeneticProteasome Endopeptidase ComplexProtein BindingProtein TransportTransforming Growth Factor betaUbiquitinConceptsD proteinsOsteogenic differentiationSequence-specific bindingUbiquitin-proteasome pathwayCore binding factor αExpression of Cbfa1Factor alpha 1P204 proteinExport signalHelix proteinsHelix-LoopRegulatory circuitsTarget genesInterferon-inducible proteinOsteocalcin geneMolecular mechanismsALP activityOsteoblast differentiationDiminished transcriptionCytoplasmic translocationId2Cbfa1Differentiation proteinProteinAlkaline phosphatase
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