Search results for "Sp1"

showing 10 items of 82 documents

Reorganization of Nuclear Domain 10 Induced by Papillomavirus Capsid Protein L2

2002

AbstractNuclear domains (ND) 10 are associated with proteins implicated in transcriptional regulation, growth suppression, and apoptosis. We now show that the minor capsid protein L2 of human papillomavirus (HPV) type 33 induces a reorganization of ND10-associated proteins. Whereas the promyelocytic leukemia protein, the major structural component of ND10, was unaffected by L2, Sp100 was released from ND10 upon L2 expression. The total cellular amount of Sp100, but not of Sp100 mRNA, decreased significantly, suggesting degradation of Sp100. Proteasome inhibitors induced the dispersal of Sp100 and inhibited the nuclear translocation of L2. In contrast to Sp100, Daxx was recruited to ND10 by …

Co-Repressor ProteinsImmunoprecipitationFluorescent Antibody TechniqueVaccinia virusPromyelocytic Leukemia ProteinAutoantigenspapillomavirusCell LinePromyelocytic leukemia proteinCapsidDeath-associated protein 6DaxxVirologyHumansSp100RNA MessengerAdaptor Proteins Signal TransducingCell NucleusRecombination GeneticbiologyTumor Suppressor ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsND10Signal transducing adaptor proteinAntigens NuclearOncogene Proteins ViralL2biochemical phenomena metabolism and nutritionBlotting NorthernMolecular biologyNeoplasm ProteinsTransport proteinCell biologyProtein TransportProteasomeCapsidbiology.proteinRNACapsid ProteinsFemaleCarrier ProteinsCo-Repressor ProteinsMolecular ChaperonesTranscription FactorsVirology
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Reciprocal regulation of the human sterol regulatory element binding protein (SREBP)-1a promoter by Sp1 and EGR-1 transcription factors.

2007

AbstractSterol regulatory element binding protein (SREBP)-1a is a transcription factor that is highly expressed in actively growing cells, and is involved in the biosynthesis of cholesterol, fatty acids and phospholipids. We have mapped the minimal human SREBP-1a promoter region to 75bp upstream of the translation start site where we discovered a functional role for the 3 GC-boxes containing overlapping sites for the Sp1 and EGR-1 transcription factors. Intact SP1-binding sites are essential for promoter activity, whereas EGR-1 suppresses the transcription of the human SREBP-1a promoter. These results reveal a novel physiologically relevant transcriptional mechanism for the reciprocal regul…

Egr-1Chromatin ImmunoprecipitationSp1 Transcription FactorSREBP-1aResponse elementMolecular Sequence DataBiophysicsElectrophoretic Mobility Shift AssayBiologyBiochemistrySp1Cell LineUpstream activating sequenceStructural BiologyTranscription (biology)Sequence Homology Nucleic AcidGene expressionGeneticsHumansPromoter Regions GeneticMolecular BiologyTranscription factorGeneral transcription factorBase SequenceReverse Transcriptase Polymerase Chain ReactionPromoterPromoterCell BiologySterol regulatory element-binding proteinBiochemistryEarly Growth Response Transcription Factorslipids (amino acids peptides and proteins)Gene expressionSterol Regulatory Element Binding Protein 1FEBS letters
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Selective Activation of Trophoblast-specific PLAC1 in Breast Cancer by CCAAT/Enhancer-binding Protein β (C/EBPβ) Isoform 2

2009

The trophoblast-specific gene PLAC1 (placenta-specific 1) is ectopically expressed in a wide range of human malignancies, most frequently in breast cancer, and is essentially involved in cancer cell proliferation, migration, and invasion. Here we show that basal activity of the PLAC1 promoter is selectively controlled by ubiquitous transcription factor SP1 and isoform 2 of CCAAT/enhancer-binding protein beta that we found to be selectively expressed in placental tissue and cancer cells. Binding of both factors to their respective elements within the PLAC1 promoter was essential to attain full promoter activity. Estrogen receptor alpha (ERalpha) signaling further augmented transcription and …

Gene isoformSp1 Transcription FactorMolecular Sequence DataEstrogen receptorBreast NeoplasmsPregnancy ProteinsBiologyBiochemistryTransactivationMolecular Basis of Cell and Developmental BiologyTranscription (biology)Cell Line TumorGene expressionHumansProtein IsoformsPromoter Regions GeneticMolecular BiologyCell ProliferationSp1 transcription factorBase SequenceCcaat-enhancer-binding proteinsCCAAT-Enhancer-Binding Protein-betaEstrogen Receptor alphaEstrogensCell BiologyMolecular biologyTrophoblastsGene Expression Regulation NeoplasticChromatin immunoprecipitationJournal of Biological Chemistry
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TMPRSS4 is a type II transmembrane serine protease involved in cancer and viral infections.

2012

Abstract Proteolytic enzymes are involved in almost all biological processes reflecting their importance in health and disease. The human genome contains nearly 600 protease-encoding genes forming more than 2% of the total human proteome. The serine proteases, with about 180 members, built the oldest and second largest family of human proteases. Ten years ago, a novel serine protease family named the type II transmembrane family (TTSP) was identified. This minireview summarizes the up-to-date knowledge about the still growing TTSPs, particularly focusing on the pathophysiological functions of the family member type II transmembrane serine protease (TMPRSS) 4. Recent studies provided importa…

GeneticsSerine proteaseTMPRSS6ProteasesClinical BiochemistrySerine EndopeptidasesProteolytic enzymesMembrane ProteinsBiologyBiochemistryTransmembrane proteinSerineBiochemistryVirus DiseasesNeoplasmsbiology.proteinHuman proteome projectAnimalsHumansMolecular BiologyMASP1Biological chemistry
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Novel in vitro and in vivo data on the cellular localization of Hsp10 in smokers affected by COPD and in lung-derived cell lines exposed to cigarette…

2013

Cigarette smoke is a potent stressor for the respiratory system, contributing to pathogenesis, for instance in chronic obstructive pulmonary disease (COPD), but its effects on the expression, function, and cellular localization of mitochondrial chaperonins are still largely unknown. We studied in vivo (airways biopsies) the localization of Hsp10 and Hsp60 in patients (smokers and non-smokers) affected by mild-moderate COPD, and characterized the effects of non-lethal doses of cigarette smoke extract (CSE) on the expression of these molecules in two human cell lines: lung fibroblasts (HFL-1) and bronchial epithelial (16HBE). We applied various in vitro methods: immunohistochemistry (IHC), su…

Hsp10 copd immunosystem
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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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Comparative analysis of Hsp10 and Hsp90 expression in healthy mucosa and adenocarcinoma of the large bowel.

2014

Heat shock proteins (Hsps) assist other proteins in their folding and drive the degradation of defective proteins. During evolution, these proteins have also acquired other roles. Hsp10 is involved in immunomodulation and tumor progression. Hsp90 stabilizes a range of "client" proteins involved in cell signaling. The present study evaluated the expression levels of Hsp10 and Hsp90 in normal mucosa and adenocarcinoma samples of human large bowel.Samples of normal mucosa and adenocarcinoma were collected and Reverse transcriptase-polymerase chain reaction RT-PCR, western blotting (WB) analyses, as well as immunohistochemistry were performed to evaluate the expression levels of Hsp10 and Hsp90…

Hsp10Reverse Transcriptase Polymerase Chain Reactionlarge bowel adenocarcinomaBlotting WesternColonic NeoplasmsRT-PCRChaperonin 10HumansHsp90HSP90 Heat-Shock ProteinsAdenocarcinomaIntestinal MucosaImmunohistochemistryAnticancer research
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Comparative analysis of Hsp10 and Hsp90 in large bowel healthy mucosa and adenocarcinomas

2015

Heat shock proteins (Hsps) are an important class of molecules with various functions. Their classic role is to assist other proteins in folding and re-folding and, when proteins are defective or irreversibly misfolded, to drive their degradation. For this reason, some Hsps are also named molecular chaperones. During evolution, this class of proteins has also acquired extrachaperoning roles such as participation in immune system regulation, cell differentiation, programmed cell death and carcinogenesis. Hsp10 is a partner of Hsp60 in the Hsp60/10 folding machine, but numerous scientific studies have shown that Hsp10 may also play other roles. In fact, Hsp10 seems to have an immunomodulatory…

Hsp10adenocarcinomasHsp90large bowel mucosa
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Serological identification of HSP105 as a novel non-Hodgkin lymphoma therapeutic target.

2011

Abstract We reported that the clinical efficacy of dendritic cell–based vaccination is strongly associated with immunologic responses in relapsed B-cell non-Hodgkin lymphoma (B-NHL) patients. We have now investigated whether postvaccination antibodies from responders recognize novel shared NHL-restricted antigens. Immunohistochemistry and flow cytometry showed that they cross-react with allogeneic B-NHLs at significantly higher levels than their matched prevaccination samples or nonresponders' antibodies. Western blot analysis of DOHH-2 lymphoma proteome revealed a sharp band migrating at approximately 100 to 110 kDa only with postvaccine repertoires from responders. Mass spectrometry ident…

ImmunologyMice SCIDBiochemistryAntibodiesFlow cytometryAntigen-Antibody ReactionsCohort StudiesHSP105MiceAntigenhemic and lymphatic diseasesCell Line TumormedicineAnimalsHumansSerologic TestsHSP110 Heat-Shock Proteinsmedicine.diagnostic_testbiologybusiness.industryLymphoma Non-HodgkinHSP105; non-Hodgkin lymphoma.Cell BiologyHematologyCell cyclemedicine.diseaseImmunohistochemistryLymphomaGranzyme BGene Expression Regulation Neoplasticnon-Hodgkin lymphoma.Spectrometry Mass Matrix-Assisted Laser Desorption-IonizationImmunologybiology.proteinImmunohistochemistryAntibodybusinessDiffuse large B-cell lymphoma
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Dissection of human papillomavirus type 33 L2 domains involved in nuclear domains (ND) 10 homing and reorganization

2003

Abstract We have recently shown that the minor capsid protein L2 of human papillomavirus type 33 (HPV33) recruits the transcriptional repressor Daxx into nuclear domains (ND) 10 and causes the loss of the transcriptional activator Sp100 from these subnuclear structures (Florin et al., 2002b) . In order to dissect L2 domains involved in nuclear translocation, ND10 homing, loss of Sp100, and recruitment of Daxx, a detailed deletion mutagenesis of L2 was performed. Using immunofluorescence and green fluorescent protein fusions, we have identified two nuclear localization signals (NLS) in the central and C-terminal part of L2, respectively, homologous to previously identified NLS in HPV6B L2 (S…

ImmunoprecipitationRecombinant Fusion ProteinsGreen Fluorescent ProteinsNuclear Localization SignalsActive Transport Cell NucleusFluorescent Antibody TechniqueBiologyImmunofluorescenceAutoantigensGreen fluorescent proteinDeath-associated protein 6DaxxVirologyTumor Cells CulturedmedicineSp100HumansNLSPapillomaviridaeAdaptor Proteins Signal TransducingCell Nucleusmedicine.diagnostic_testIntracellular Signaling Peptides and ProteinsND10Nuclear ProteinsAntigens NuclearL2Oncogene Proteins ViralPapillomavirusbiochemical phenomena metabolism and nutritionMolecular biologyDeletion MutagenesisLuminescent ProteinsCapsidMutagenesisCapsid ProteinsCarrier ProteinsCo-Repressor ProteinsGene DeletionNuclear localization sequenceMolecular ChaperonesVirology
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