Search results for "ACTIVATOR"

showing 8 items of 488 documents

Osteoprotegerin: multiple partners for multiple functions.

2013

Osteoprotegerin (OPG) is an essential secreted protein in bone turnover due to its role as a decoy receptor for the Receptor Activator of Nuclear Factor-kB ligand (RANKL) in the osteoclasts, thus inhibiting their differentiation. However, there are additional ligands of OPG that confer various biological functions. OPG can promote cell survival, cell proliferation and facilitates migration by binding TNF-related apoptosis inducing ligand (TRAIL), glycosaminoglycans or proteoglycans. A large number of in vitro, pre-clinical and clinical studies provide evidences of OPG involvement in vascular, bone, immune and tumor biology. This review describes an overview of the different OPG ligands regu…

musculoskeletal diseasesCell SurvivalEndocrinology Diabetes and MetabolismImmunologyOsteoclastsGeneral Biochemistry Genetics and Molecular BiologyTNF-Related Apoptosis-Inducing LigandOsteoprotegerinImmunology and AllergyAnimalsHumansCell adhesionReceptorCell ProliferationbiologyActivator (genetics)Cell growthChemistryRANK LigandOsteoprotegerinCell DifferentiationIn vitroCell biologyBiochemistryRANKLbiology.proteinDecoyCytokinegrowth factor reviews
researchProduct

Evaluation of the osteoclastogenic process associated with RANK / RANK-L / OPG in odontogenic myxomas

2018

Background Odontogenic myxoma (OM) is a benign intraosseous neoplasm that exhibits local aggressiveness and high recurrence rates. Osteoclastogenesis is an important phenomenon in the tumor growth of maxillary neoplasms. RANK (Receptor Activator of Nuclear Factor κappa B) is the signaling receptor of RANK-L (Receptor activator of nuclear factor kappa-Β ligand) that activates the osteoclasts. OPG (osteoprotegerin) is a decoy receptor for RANK-L that inhibits pro-osteoclastogenesis. The RANK / RANKL / OPG system participates in the regulation of osteolytic activity under normal conditions, and its alteration has been associated with greater bone destruction, and also with tumor growth. Object…

musculoskeletal diseasesMaleOdontogenic myxomaRANK-LRANKOdontogenic myxoma03 medical and health sciences0302 clinical medicineOsteoprotegerinOsteoclastogenesis.MedicineNeoplasmHumansMIXOMAReceptorGeneral DentistryLanguageOSTEOGENESISDental follicleOral Medicine and PathologybiologyActivator (genetics)business.industryResearch030206 dentistry:CIENCIAS MÉDICAS [UNESCO]medicine.diseaseDental follicleLIGANDO RANKOtorhinolaryngologyRANKL030220 oncology & carcinogenesisUNESCO::CIENCIAS MÉDICASCancer researchbiology.proteinImmunohistochemistryOPGSurgerybusinessMyxomaMedicina Oral, Patología Oral y Cirugía Bucal
researchProduct

The role of biosilica in the osteoprotegerin/RANKL ratio in human osteoblast-like cells

2010

Abstract Earlier studies have demonstrated that biosilica, synthesized by the enzyme silicatein, induces hydroxyapatite formation in osteoblast-like SaOS-2 cells. Here we study the effect of biosilica on the expressions of osteoprotegerin [OPG] and the receptor activator for NF-κB ligand [RANKL] in the SaOS-2 cell model. We show that during growth of SaOS-2 cells on biosiliceous matrices hydroxyapatite formation is induced, while syntheses of cartilaginous proteoglycans and sulfated glycosaminoglycans are down-regulated. Furthermore, quantitative real-time RT-PCR analysis revealed a strong time-depended increase in expression of OPG in biosilica exposed SaOS-2 cells while the steady-state e…

musculoskeletal diseasesMaterials scienceCell Culture TechniquesBiophysicsBiocompatible MaterialsBioengineeringCell LineBiomaterialsGlycosaminoglycanSulfationOsteoprotegerinMaterials TestingmedicineAnimalsHumansReceptorchemistry.chemical_classificationOsteoblastsbiologyActivator (genetics)RANK LigandOsteoprotegerinOsteoblastSilicon DioxideCathepsinsExtracellular MatrixCell biologyEnzymemedicine.anatomical_structurechemistryBiochemistryMechanics of MaterialsRANKLCeramics and Compositesbiology.proteinBiomaterials
researchProduct

Role of the NF-kB pathway and nitric oxide in mammary gland involution after weaning. Implications in breast cancer

2013

INTRODUCCIÓN La glándula mamaria es un órgano dinámico que alcanza su máximo desarrollo funcional con la lactancia, momento en el cual, a través de la producción de leche, aporta nutrientes y protección inmunológica a las crías de los mamíferos. Cuando la lactancia finaliza con el destete, el exceso de tejido glandular debe desaparecer y la glándula sufre una extensa remodelación hasta alcanzar nuevamente un estado pre-gestacional, preparada para un nuevo ciclo. La involución del tejido mamario es un proceso complejo durante el cual se suceden de forma coordinada una serie de eventos como la muerte de las células epiteliales secretoras, la proliferación de tejido adiposo circundante y la re…

nitrotyrosineweaningapoptosiscathepsin DUNESCO::CIENCIAS DE LA VIDA::Biología celularnuclear factor κappa B (NF-κB)mammary gland involutionsignal transducer and activator of transcription (STAT)breast cancer:CIENCIAS DE LA VIDA::Biología celular [UNESCO]inflammationnitric oxideUNESCO::CIENCIAS MÉDICAS::Ciencias clínicas::OncologíaNOS2-KO:CIENCIAS MÉDICAS::Ciencias clínicas::Oncología [UNESCO]
researchProduct

Regulatory networks underlying mycorrhizal development delineated by genome-wide expression profiling and functional analysis of the transcription fa…

2017

Background: Ectomycorrhizal (ECM) fungi develop a mutualistic symbiotic interaction with the roots of their host plants. During this process, they undergo a series of developmental transitions from the running hyphae in the rhizosphere to the coenocytic hyphae forming finger-like structures within the root apoplastic space. These transitions, which involve profound, symbiosis-associated metabolic changes, also entail a substantial transcriptome reprogramming with coordinated waves of differentially expressed genes. To date, little is known about the key transcriptional regulators driving these changes, and the aim of the present study was to delineate and functionally characterize the trans…

polypeptidelcsh:QH426-470Transcription factors; symbiosis; secreted proteins; transcriptional activator trap assay; yeast; transcriptome; ectomycorrhiza developmentlcsh:BiotechnologyTranscription Factors/geneticslaccaria bicolorpopulusyeastectomycorrhizasecreted proteinsLaccariadéveloppement biologiquelcsh:TP248.13-248.65MycorrhizaeTranscription factorsgenomicsGene Regulatory Networkstranscriptional activator trap assayLaccaria/geneticsectomycorrhiza developmentGene Expression ProfilingMycorrhizae/geneticsfungiMicrobiology and Parasitologypseudotsuga menziesiisymbiosisMicrobiologie et Parasitologielcsh:Genetics[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyontogenyectomycorhizeTranscription factors;ectomycorrhiza development;secreted proteins;symbiosis;transcriptional activator trap assay;transcriptome;yeastsymbiosetranscriptomefacteur de transcriptionResearch Article
researchProduct

Rac1 and PAK1 are upstream of IKK-ε and TBK-1 in the viral activation of interferon regulatory factor-3

2004

The anti-viral type I interferon (IFN) response is initiated by the immediate induction of IFN beta, which is mainly controlled by the IFN-regulatory factor-3 (IRF-3). The signaling pathways mediating viral IRF-3 activation are only poorly defined. We show that the Rho GTPase Rac1 is activated upon virus infection and controls IRF-3 phosphorylation and activity. Inhibition of Rac1 leads to reduced IFN beta promoter activity and to enhanced virus production. As a downstream mediator of Rac signaling towards IRF-3, we have identified the kinase p21-activated kinase (PAK1). Furthermore, both Rac1 and PAK1 regulate the recently described IRF-3 activators, I kappa B kinase- and TANK-binding kina…

rac1 GTP-Binding ProteinTranscription GeneticBiophysicsIκB kinaseProtein Serine-Threonine KinasesSignal transductionBiologyVirus ReplicationBiochemistryCell LineDogsPAK1Structural BiologyInterferonGeneticsmedicineAnimalsHumansPhosphorylationPromoter Regions Geneticp21-activated kinasesMolecular BiologyRNA Double-StrandedKinaseRho GTPaseI-Kappa-B KinaseNuclear ProteinsInterferon-betaCell BiologyCREB-Binding ProteinI-kappa B KinaseDNA-Binding ProteinsEnzyme Activationp21-Activated KinasesInfluenza A virusViral infectionAnti-viral responseTrans-ActivatorsCancer researchInterferon Regulatory Factor-3Transcription factorSignal transductionDimerizationTranscription FactorsInterferon regulatory factorsmedicine.drugFEBS Letters
researchProduct

Mouse models of cytomegalovirus latency: overview.

2002

Abstract Background: The molecular regulation of viral latency and reactivation is a central unsolved issue in the understanding of cytomegalovirus (CMV) biology. Like human CMV (hCMV), murine CMV (mCMV) can establish a latent infection in cells of the myeloid lineage. Since mCMV genome remains present in various organs after its clearance from hematopoietic cells first in bone marrow and much later in blood, there must exist one or more widely distributed cell type(s) representing the cellular site(s) of enduring mCMV latency in host tissues. Endothelial cells and histiocytes are candidates, but the question is not yet settled. Another long debated problem appears to be solved: mCMV establ…

virusesCytomegalovirusBiologymedicine.disease_causeVirusHerpesviridaeImmediate-Early ProteinsTransactivationMiceViral ProteinsVirologyVirus latencymedicineCytotoxic T cellAnimalsHumansLatency (engineering)GeneMice Inbred BALB Cvirus diseasesmedicine.diseaseVirologyVirus LatencyHaematopoiesisDisease Models AnimalInfectious DiseasesImmunologyCytomegalovirus InfectionsTrans-ActivatorsVirus ActivationJournal of clinical virology : the official publication of the Pan American Society for Clinical Virology
researchProduct

In vitro studies on the activation of the hepatitis C virus NS3 proteinase by the NS4A cofactor.

1996

AbstractProteolytic processing of the nonstructural proteins of the hepatitis C virus (HCV) is mediated by two viral proteinases: the NS2-3 proteinase cleaving at the NS2/3 junction and the NS3 serine-type proteinase responsible for processing at the NS3/4A, NS4A/B, NS4B/5A, and NS5A/B sites. Activity of the NS3 proteinase is modulated by NS4A. In the absence of this cofactor processing at the NS3-dependent sites does not occur or, in the case of the NS5A/B junction, is poor but increased when NS4A is present. Although recent studies demonstrated that proteinase activation requires direct interaction between NS3 and NS4A, the mechanism by which NS4A exerts the activation function is not kno…

virusesMolecular Sequence DataHepacivirusBiologyViral Nonstructural ProteinsCell LineEnzyme activatorProteinase 3VirologyCricetinaeMicrosomesAnimalsHumansAmino Acid SequenceBinding siteNS5APeptide sequenceSequence Deletionchemistry.chemical_classificationNS3Binding SitesBase Sequencevirus diseasesIntracellular Membranesbiochemical phenomena metabolism and nutritionMolecular biologyIn vitrodigestive system diseasesAmino acidEnzyme ActivationBiochemistrychemistryDNA ViralPeptidesHeLa CellsVirology
researchProduct