Search results for "BLAST"

showing 10 items of 2136 documents

Mild Heat Stress Enhances Angiogenesis in a Co-culture System Consisting of Primary Human Osteoblasts and Outgrowth Endothelial Cells

2013

The repair and regeneration of large bone defects, including the formation of functional vasculature, represents a highly challenging task for tissue engineering and regenerative medicine. Recent studies have shown that vascularization and ossification can be stimulated by mild heat stress (MHS), which would offer the option to enhance the bone regeneration process by relatively simple means. However, the mechanisms of MHS-enhanced angiogenesis and osteogenesis, as well as potential risks for the treated cells are unclear. We have investigated the direct effect of MHS on angiogenesis and osteogenesis in a co-culture system of human outgrowth endothelial cells (OECs) and primary osteoblasts …

Hot TemperatureCell SurvivalAngiogenesisCellular differentiationBiomedical EngineeringNeovascularization PhysiologicMedicine (miscellaneous)ApoptosisBioengineeringBiologyRegenerative medicineArticleTissue engineeringOsteogenesisHeat shock proteinHumansRNA MessengerHeat shockBone regenerationCells CulturedCaspase 7OsteoblastsCaspase 3Regeneration (biology)Endothelial CellsCell DifferentiationCoculture TechniquesCapillariesUp-RegulationCell biologyImmunologyHeat-Shock ResponseTissue Engineering Part C: Methods
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Hsp70 localizes differently from chaperone Hsc70 in mouse mesoangioblasts under physiological growth conditions

2008

Mouse A6 mesoangioblasts express Hsp70 even in the absence of cellular stress. Its expression and its intracellular localization were investigated under normal growth conditions and under hyperthermic stress. Immunofluorescence assays indicated that without any stress a fraction of Hsp70 co-localized with actin microfilaments, in the cell cortex and in the contractile ring of dividing cells, while the Hsc70 chaperone did not. Hsp70 immunoprecipitation assays confirmed that a portion of Hsp70 binds actin. Immunoblot assays showed that both proteins were present in the nucleus. After heat treatment Hsp70 and actin continued to co-localize in the leading edge of A6 cells but not on microfilame…

Hot TemperatureHistologyPhysiologyImmunoprecipitationHsp70 Hsc70 Mesoangioblastmacromolecular substancesMicrofilamentCell LineMiceStress PhysiologicalCell cortexAnimalsHumansHSP70 Heat-Shock ProteinsActinbiologyStem CellsHSC70 Heat-Shock ProteinsCell BiologyGeneral MedicineActinsGlomerular MesangiumHsp70Cell biologyCell cultureChaperone (protein)biology.proteinCell DivisionCytokinesisMolecular ChaperonesJournal of Molecular Histology
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Human HSP10 variants downregulation after cigarette smoke extract exposure in lung cells

2009

The impact of cigarette-smoke stress (a form of oxidative stress) on human lung fibroblasts and epithelial cells, particularly its effect on Hsp10 expression, has not been characterized despite the fact that a role for mitochondrial chaperonins in the development of lung diseases, ranging from chronic obstructive pulmonary disease to bronchial carcinogenesis, has been suggested (1). We studied the effects of non-lethal doses of cigarette smoke extract (CSE) on the expression of Hsp10 in human lung fibroblasts (HFL-1 line) and epithelial cells (16HBE line). Proteomics was carried out using 2D-IPG, silver stain, western blotting, and mass-spectrometry; mRNA was measured by RT-PCR. Database se…

Hsp10 cigarette smoke bronchial epithelial cells lung fibroblasts oxidative stress 2D-electrophoresis IPG isoelectric variants chaperoninsSettore BIO/16 - Anatomia Umana
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Hsp70 in mesoangioblast A6 stem cells.

2006

Hsp70 mesoangioblast stem cells
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Hsp70 level regulates MMP2 expression in mesoangioblast stemj cells

2013

Hsp70 mesoangioblasts stem cells MMP2
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Intracellular and extracellular Hsp70 in mouse mesoangioblast stem cells

2008

Hsp70 mouse mesoangioblast stem cell
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The Complex Regulatory Role of Cytomegalovirus Nuclear Egress Protein pUL50 in the Production of Infectious Virus

2021

The regulation of the nucleocytoplasmic release of herpesviral capsids is defined by the process of nuclear egress. Due to their large size, nuclear capsids are unable to traverse via nuclear pores, so that herpesviruses evolved to develop a vesicular transport pathway mediating their transition through both leaflets of the nuclear membrane. This process involves regulatory proteins, which support the local distortion of the nuclear envelope. For human cytomegalovirus (HCMV), the nuclear egress complex (NEC) is determined by the pUL50-pUL53 core that initiates multicomponent assembly with NEC-associated proteins and capsids. Hereby, pUL50 serves as a multi-interacting determinant that recru…

Human cytomegalovirusGene Expression Regulation ViralProteomicsefficiency of infectious virus productionQH301-705.5Nuclear Envelope[SDV]Life Sciences [q-bio]virusesQuantitative proteomicsCytomegalovirusconditional expressionGenome Viralnuclear egress complex (NEC)Virus ReplicationArticleCell LineViral ProteinsCapsidNEC protein pUL50DNA PackagingmedicineHumansddc:610Biology (General)Nuclear poreNuclear membraneregulation of viral replicationGenes Immediate-EarlyCell Nucleusfunctional propertiesChemistryVirionGeneral MedicineFibroblastsmedicine.diseaseCell biologyVesicular transport protein[SDV] Life Sciences [q-bio]Kineticsmedicine.anatomical_structureLytic cycleCapsidhuman cytomegalovirusLamin
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Modification of the major tegument protein pp65 of human cytomegalovirus inhibits virus growth and leads to the enhancement of a protein complex with…

2010

The tegument protein pp65 of human cytomegalovirus (HCMV) is abundant in lytically infected human foreskin fibroblasts (HFF), as well as in virions and subviral dense bodies (DB). Despite this, we showed previously that pp65 is dispensable for growth in HFF. In the process of refining a DB-based vaccine candidate, different HCMV mutants were generated, expressing a dominant HLA-A2-presented peptide of the IE1 protein fused to pp65. One of the mutant viruses (RV-VM1) surprisingly showed marked impairment in virus release from HFF. We hypothesized that analysis of the phenotypic alterations of RV-VM1 would provide insight into the functions of pp65, poorly defined thus far. RV-VM1 infection r…

Human cytomegalovirusImmunoprecipitationvirusesMutantCytomegalovirusBiologyVirus ReplicationVirusInclusion bodiesViral Matrix ProteinsViral ProteinsVirologymedicineHumansImmunoprecipitationCells Culturedvirus diseasesRNAViral tegumentFibroblastsPhosphoproteinsmedicine.diseaseVirologyFusion proteinTrans-ActivatorsProtein MultimerizationProtein BindingJournal of General Virology
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Polyethylenimine is a strong inhibitor of human papillomavirus and cytomegalovirus infection.

2012

ABSTRACT Polyethylenimines are cationic polymers with potential as delivery vectors in gene therapy and with proven antimicrobial activity. However, the antiviral activity of polyethylenimines has not been addressed in detail thus far. We have studied the inhibitory effects of a linear 25-kDa polyethylenimine on infections with human papillomaviruses and human cytomegaloviruses. Preincubation of cells with polyethylenimine blocked primary attachment of both viruses to cells, resulting in a significant reduction of infection. In addition, the dissemination of human cytomegalovirus in culture cells was efficiently reduced by recurrent administration of polyethylenimine. Polyethylenimine conce…

Human cytomegalovirusKeratinocytesGenetic enhancementCongenital cytomegalovirus infectionCytomegalovirusVirus AttachmentBiologyAntiviral Agentschemistry.chemical_compoundCationsChlorocebus aethiopsmedicineCytotoxic T cellAnimalsHumansPolyethyleneiminePharmacology (medical)Human papillomavirusPapillomaviridaePharmacologyPolyethyleniminePapillomavirus InfectionsFibroblastsAntimicrobialmedicine.diseaseVirologyMicrobicides for sexually transmitted diseasesInfectious DiseasesHEK293 CellschemistryMicroscopy FluorescenceOrgan SpecificityCOS CellsCytomegalovirus InfectionsHeLa CellsAntimicrobial agents and chemotherapy
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Protein delivery by subviral particles of human cytomegalovirus

2003

Direct protein delivery is an emerging technology in vaccine development and gene therapy. We could previously show that subviral dense bodies (DB) of human cytomegalovirus (HCMV), a beta-herpesvirus, transport viral proteins into target cells by membrane fusion. Thus these non-infectious particles provide a candidate delivery system for the prophylactic and therapeutic application of proteins. Here we provide proof of principle that DB can be modified genetically. A 55 kDa fusion protein consisting of the green fluorescent protein and the neomycin phosphotransferase could be packed in and delivered into cells by recombinant DB in a functional fashion. Furthermore, transfer of protein into …

Human cytomegalovirusRecombinant Fusion ProteinsGenetic enhancementGenetic VectorsGreen Fluorescent ProteinsCongenital cytomegalovirus infectionCytomegalovirusGene ExpressionBiologylaw.inventionGreen fluorescent proteinlawVaccines DNAGeneticsmedicineHumansMolecular BiologyKanamycin KinaseSecretory VesiclesLipid bilayer fusionDendritic CellsGenetic TherapyFibroblastsmedicine.diseaseFusion proteinVirologyCell biologyLuminescent ProteinsFluorescent Antibody Technique DirectRecombinant DNAMolecular MedicineDelivery systemGenetic EngineeringGene Therapy
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