2023
Pathogenic mechanisms of glucocorticoid-induced osteoporosis
Chen M, Fu W, Xu H, Liu C. Pathogenic mechanisms of glucocorticoid-induced osteoporosis. Cytokine & Growth Factor Reviews 2023, 70: 54-66. PMID: 36906448, PMCID: PMC10518688, DOI: 10.1016/j.cytogfr.2023.03.002.Peer-Reviewed Original ResearchConceptsGlucocorticoid-induced osteoporosisExogenous glucocorticoidsGC excessBone cellsBone formationImpaired bone formationMultiple adverse effectsLong-term useExcessive glucocorticoidsAutoimmune diseasesBone resorptionPrescribed medicinesEnhanced osteoclastogenesisPathogenic mechanismsProcess of osteoblastogenesisGlucocorticoidsHigh dosesOsteoclast apoptosisApoptosis of osteoblastsMature osteoclastsAdverse effectsOsteoclastsDifferentiation of osteoblastsOsteoporosisOsteoclastogenesis
2021
Progranulin promotes bone fracture healing via TNFR pathways in mice with type 2 diabetes mellitus
Ding Y, Wei J, Hettinghouse A, Li G, Li X, Einhorn T, Liu C. Progranulin promotes bone fracture healing via TNFR pathways in mice with type 2 diabetes mellitus. Annals Of The New York Academy Of Sciences 2021, 1490: 77-89. PMID: 33543485, PMCID: PMC8138780, DOI: 10.1111/nyas.14568.Peer-Reviewed Original ResearchConceptsType 2 diabetes mellitusRole of progranulinBone fracture healingFracture healingDiabetes mellitusT2DM modelType 1 diabetic conditionAnti-inflammatory activityTranscription-polymerase chain reactionLocal administrationBone marrow cellsExogenous progranulinMKR micePGRN effectsPrimary bone marrow cellsFracture riskDiabetic conditionsPGRN mRNABone fragilityImmunohistochemical stainingMetabolic disordersRecombinant progranulinBone fracturesProgranulinTherapeutic potential
2020
In Vitro Physical and Functional Interaction Assays to Examine the Binding of Progranulin Derivative Atsttrin to TNFR2 and Its Anti-TNFα Activity
Fu W, Hettinghouse A, Liu C. In Vitro Physical and Functional Interaction Assays to Examine the Binding of Progranulin Derivative Atsttrin to TNFR2 and Its Anti-TNFα Activity. Methods In Molecular Biology 2020, 2248: 109-119. PMID: 33185871, PMCID: PMC8112733, DOI: 10.1007/978-1-0716-1130-2_8.Peer-Reviewed Original ResearchConceptsAnti-TNFα activityAutoimmune diseasesTartrate-resistant acid phosphatase (TRAP) stainingAnti-TNFα therapyCollagen-induced arthritisInflammatory disease modelsGood therapeutic effectAcid phosphatase stainingGrowth factor-like moleculesTNF inhibitorsTherapeutic effectTNFα activityProgranulinFunctional inhibitionTNFR2AtsttrinDisease modelsPhosphatase stainingTNFRTNFαDiseaseInhibitionCritical roleDirect bindingHigh affinity
2016
Extracellular matrix protein 1, a direct targeting molecule of parathyroid hormone‐related peptide, negatively regulates chondrogenesis and endochondral ossification via associating with progranulin growth factor
Kong L, Zhao Y, Tian Q, Feng J, Kobayashi T, Merregaert J, Liu C. Extracellular matrix protein 1, a direct targeting molecule of parathyroid hormone‐related peptide, negatively regulates chondrogenesis and endochondral ossification via associating with progranulin growth factor. The FASEB Journal 2016, 30: 2741-2754. PMID: 27075243, PMCID: PMC4970607, DOI: 10.1096/fj.201600261r.Peer-Reviewed Original ResearchConceptsExtracellular matrix protein 1Matrix protein 1Protein 1Endochondral ossificationCellular signaling pathwaysGrowth factorRegulation of chondrogenesisEndochondral bone formationUnrecognized regulatorChondrogenic growth factorsInteraction networksPTHrP regulationCartilage developmentSignaling pathwaysParathyroid hormone-related peptideTarget transgeneMatrix proteinsChondrocyte differentiationCellular interactionsHormone-related peptideChondrogenesisChondrocyte hypertrophyPTHrP actionOverexpressionPathway
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
2010
Interaction between cartilage oligomeric matrix protein and extracellular matrix protein 1 mediates endochondral bone growth
Kong L, Tian Q, Guo F, Mucignat M, Perris R, Sercu S, Merregaert J, Di Cesare P, Liu C. Interaction between cartilage oligomeric matrix protein and extracellular matrix protein 1 mediates endochondral bone growth. Matrix Biology 2010, 29: 276-286. PMID: 20138147, PMCID: PMC2862898, DOI: 10.1016/j.matbio.2010.01.007.Peer-Reviewed Original ResearchConceptsExtracellular matrix protein 1Matrix protein 1EGF domainsFunctional genetic screensProtein 1Endochondral bone growthGenetic screenEndochondral bone formationBiological functionsC-terminusMatrix proteinsMatrix mineralizationBiological significanceCartilage oligomeric matrix proteinOligomeric matrix proteinChondrocyte hypertrophyFirst evidenceBone growthInhibitionGrowthColocalizeBone formationDomainProteinInteraction
2008
Mediation 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