Search results for "CDC42"

showing 10 items of 26 documents

Pattern of Invasion in Human Pancreatic Cancer Organoids Is Associated with Loss of SMAD4 and Clinical Outcome

2020

Abstract Pancreatic ductal adenocarcinoma (PDAC) is an aggressive malignancy characterized by extensive local invasion and systemic spread. In this study, we employed a three-dimensional organoid model of human pancreatic cancer to characterize the molecular alterations critical for invasion. Time-lapse microscopy was used to observe invasion in organoids from 25 surgically resected human PDAC samples in collagen I. Subsequent lentiviral modification and small-molecule inhibitors were used to investigate the molecular programs underlying invasion in PDAC organoids. When cultured in collagen I, PDAC organoids exhibited two distinct, morphologically defined invasive phenotypes, mesenchymal an…

0301 basic medicineCancer Researchendocrine system diseasesPancreatic ductal adenocarcinoma (PDAC)RAC1CDC42AdenocarcinomaBiologyArticle03 medical and health sciences0302 clinical medicineHuman Pancreatic CancerCell MovementPancreatic cancerBiomarkers TumorTumor Cells CulturedmedicineOrganoidHumansNeoplasm InvasivenessCell ProliferationSmad4 ProteinRegulation of gene expressionCell growthMesenchymal stem cellPrognosismedicine.diseasePhenotypedigestive system diseasesGene Expression Regulation NeoplasticOrganoidsPancreatic NeoplasmsSurvival Rate030104 developmental biologyOncology030220 oncology & carcinogenesisembryonic structuresCancer researchCarcinoma Pancreatic DuctalSignal TransductionCancer Research
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Alterations in Tight- and Adherens-Junction Proteins Related to Glaucoma Mimicked in the Organotypically Cultivated Mouse Retina Under Elevated Press…

2020

Purpose To scrutinize alterations in cellular interactions and cell signaling in the glaucomatous retina, mouse retinal explants were exposed to elevated pressure. Methods Retinal explants were prepared from C57bl6 mice and cultivated in a pressure chamber under normotensive (atmospheric pressure + 0 mm Hg), moderately elevated (30 mm Hg), and highly elevated (60 mm Hg) pressure conditions. The expression levels of proteins involved in the formation of tight junctions (zonula occludens 1 [ZO-1], occludin, and claudin-5) and adherens junctions (VE-cadherin and β-catenin) and in cell-signaling cascades (Cdc42 and activated Cdc42 kinase 1 [ACK1]), as well as the expression levels of the growth…

0301 basic medicineelevated pressureBlotting WesternVimentinReal-Time Polymerase Chain ReactionOccludinRetinaTight JunctionsAdherens junctionMice03 medical and health scienceschemistry.chemical_compoundOrgan Culture Techniques0302 clinical medicineAntigens CDOccludinmedicinecell signalingAnimalscell contactsEye Proteinscdc42 GTP-Binding ProteinReceptorretina explantsmousebeta CateninRetinabiologyTight junctionGlial fibrillary acidic proteinChemistryGlaucomaRetinalAdherens JunctionsProtein-Tyrosine KinasesCadherinsImmunohistochemistryCell biologyMice Inbred C57BLAtmospheric Pressure030104 developmental biologymedicine.anatomical_structure030220 oncology & carcinogenesisZonula Occludens-1 Proteinbiology.proteinInvestigative Opthalmology & Visual Science
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Delineation of the catalytic domain of Clostridium difficile toxin B-10463 to an enzymatically active N-terminal 467 amino acid fragment.

2006

Abstract In an attempt to directly approach the postulated toxic domain of Clostridium difficile 's TcdB-10463, eight subclones of different size and locations in the N-terminal third of the toxin were generated. Expression of these toxin fragments was checked in Western blots and the enzymatic activity of the expressed proteins was analyzed by glucosylating Ras related small GTP-binding proteins. Two polypeptides of 875 aa (TcdBc1–3) and 557 aa (TcdBc1-H) glucosylated their targets Rho, Rac and Cdc42 with the same activity and specificity as the holotoxin. In comparison 516 aa (TcdBc1-N) and 467 aa (TcdBc1-A) protein fragments exhibited highly reduced activity, while Tcdc1 and TcdB2–3 (aa …

Bacterial ToxinsMolecular Sequence DataClostridium difficile toxin Bmedicine.disease_causeMicrobiologyStructure-Activity RelationshipGTP-binding protein regulatorsClostridiumBacterial ProteinsGeneticsmedicineMolecular Biologychemistry.chemical_classificationBinding SitesbiologyBase SequenceToxinbiology.organism_classificationMolecular biologyPeptide FragmentsRecombinant ProteinsAmino acidEnzymechemistryCdc42 GTP-Binding ProteinBiochemistryGlucosyltransferasesbiology.proteinGlucosyltransferaseFEMS microbiology letters
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cIAP1 regulates TNF-mediated cdc42 activation and filopodia formation

2013

International audience; umour necrosis factor-α (TNF) is a cytokine endowed with multiple functions, depending on the cellular and environmental context. TNF receptor engagement induces the formation of a multimolecular complex including the TNFR-associated factor TRAF2, the receptor-interaction protein kinase RIP1 and the cellular inhibitor of apoptosis cIAP1, the latter being essential for NF-κB activation. Here, we show that cIAP1 also regulates TNF-induced actin cytoskeleton reorganization through a cdc42-dependent, NF-κB-independent pathway. Deletion of cIAP1 prevents TNF-induced filopodia and cdc42 activation. The expression of cIAP1 or its E3-ubiquitin ligase-defective mutant restore…

Cancer ResearchLung NeoplasmsBlotting WesternFluorescent Antibody Techniquemacromolecular substancesCDC42BiologyTransfectionInhibitor of Apoptosis ProteinsMice03 medical and health sciences0302 clinical medicineCell AdhesionGeneticsAnimalsHumansImmunoprecipitationNeoplasm InvasivenessPseudopodia[SPI.NANO]Engineering Sciences [physics]/Micro and nanotechnologies/Microelectronicscdc42 GTP-Binding ProteinMolecular Biology030304 developmental biology0303 health sciencesTumor Necrosis Factor-alphaActin cytoskeleton reorganizationCell PolarityActin remodelingSurface Plasmon ResonanceActin cytoskeletonCell biologyActin CytoskeletonDisease Models AnimalHEK293 CellsCdc42 GTP-Binding Protein030220 oncology & carcinogenesisNIH 3T3 CellsHeterografts[ SPI.NANO ] Engineering Sciences [physics]/Micro and nanotechnologies/MicroelectronicsPseudopodiaSignal transductionFilopodiaSignal TransductionOncogene
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Microbial strategies to exploit host cells

2005

The European Research Conference (EURESCO) on Spatial and Temporal Dynamics of the Endomembrane System was held in sunny San Feliu de Guixols, Spain, between 16 and 21 October 2004. The conference was organized by D. Holden and H. Stenmark ![][1] By bringing together scientists from the fields of microbiology and cell biology, the European Research Conference (EURESCO) on ‘Spatial and Temporal Dynamics of the Endomembrane System’ combined the best of both worlds at the intersection where intracellular pathogens and host cells meet. The mixture of studies, which focused on the molecular mechanisms behind endocytic and secretory transport, and the pathogenic microbes that exploit these pathwa…

EffectorEndocytic cycleCDC42Golgi apparatusBiologyEndocytosisBiochemistryCell biologysymbols.namesakeGeneticssymbolsEndomembrane systemSecretionMolecular BiologyPhagosomeEMBO reports
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Isolation and characterization of Wnt pathway-related genes from Porifera.

2006

The Wnt signal acts by binding to Frizzled receptors, with the subsequent activation of two different signal transduction cascades, the canonical and the non-canonical Wnt pathways, involved in cell growth, differentiation, migration and fate. The canonical pathway functions through the translocation of beta-catenin to the nucleus and the activation of TCF/LEF transcription factors; it plays an important role in developmental patterning and cell fate decisions during embryogenesis. The non-canonical Wnt pathway is responsible for the planar cell polarity process in invertebrates, and for the convergent-extension movements during vertebrate gastrulation. The final effect of the non-canonical…

FrizzledMyosin Light ChainsMolecular Sequence DataGTPaseCell fate determinationGlycogen Synthase Kinase 3AnimalsAmino Acid Sequencecdc42 GTP-Binding ProteinCells CulturedPhylogenybiologyGene Expression ProfilingWnt signaling pathwayIntracellular Signaling Peptides and ProteinsLRP6LRP5Cell BiologyGeneral Medicinebiology.organism_classificationFrizzled ReceptorsCell biologyPoriferaSuberites domunculaWnt ProteinsGene Expression RegulationSignal transductionTCF Transcription FactorsrhoA GTP-Binding ProteinCell biology international
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miR-124-regulated RhoG reduces neuronal process complexity via ELMO/Dock180/Rac1 and Cdc42 signalling

2012

The small GTPase RhoG plays a central role in actin remodelling during diverse biological processes such as neurite outgrowth, cell migration, phagocytosis of apoptotic cells, and the invasion of pathogenic bacteria. Although it is known that RhoG stimulates neurite outgrowth in the rat pheochromocytoma PC12 cell line, neither the physiological function nor the regulation of this GTPase in neuronal differentiation is clear. Here, we identify RhoG as an inhibitor of neuronal process complexity, which is regulated by the microRNA miR-124. We find that RhoG inhibits dendritic branching in hippocampal neurons in vitro and in vivo. RhoG also inhibits axonal branching, acting via an ELMO/Dock180/…

General Immunology and MicrobiologyNeuriteDock180General NeuroscienceCell migrationRAC1CDC42GTPaseBiologyGeneral Biochemistry Genetics and Molecular BiologyCell biologynervous systemSmall GTPaseRhoGMolecular BiologyThe EMBO Journal
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EPCR/PAR1 Signaling Navigates Long-Term Repopulating Hematopoietic Stem Cell Bone Marrow Homing to Thrombomodulin-Enriched Blood Vessels

2015

Abstract Bone marrow (BM) homing and lodgment of long-term repopulating hematopoietic stem cells (LT-HSCs) is an active and essential first step in clinical stem cell transplantation. EPCR is expressed by murine BM LT-HSCs endowed with the highest repopulation potential and its ligand, activated protein C (aPC), has anticoagulant and anti-sepsis effects in EPCR+/PAR1+ endothelial cells. We recently found that signaling cascades, traditionally viewed as coagulation and inflammation related, also independently control EPCR+ LT-HSC BM retention and recruitment to the blood via distinct PAR1 mediated pathways. EPCR/PAR1 signaling retains LT-HSCs in the BM by restricting nitric oxide (NO) produc…

ImmunologyHematopoietic stem cellCell BiologyHematologyBiologyBiochemistryCell biologyTransplantationEndothelial stem cellHaematopoiesismedicine.anatomical_structureCdc42 GTP-Binding ProteinImmunologymedicineStem cellProgenitor cellHoming (hematopoietic)Blood
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Integrin alpha 2 beta 1 promotes activation of protein phosphatase 2A and dephosphorylation of Akt and glycogen synthase kinase 3 beta.

2002

The integrins are a large family of heterodimeric transmembrane receptors composed of α and β subunits (22). In addition to mediating cell-matrix interactions, integrins have been shown to activate intracellular signaling pathways which, in collaboration with growth factor-induced signals, regulate cellular functions (46). Some integrin signaling cascades are activated via the β subunit cytoplasmic domain, and they are therefore triggered by several integrin heterodimers. These signals include the activation of protein tyrosine kinases of the Src and focal adhesion kinase (FAK) families (9, 47). More-recent studies have revealed signaling events that are activated specifically by an α subun…

IntegrinsReceptors CollagenIntegrinProtein Serine-Threonine KinasesCD49cp38 Mitogen-Activated Protein KinasesCollagen receptorGlycogen Synthase Kinase 3Proto-Oncogene ProteinsCell AdhesionPhosphoprotein PhosphatasesHumansIntegrin-linked kinaseProtein Phosphatase 2cdc42 GTP-Binding ProteinMolecular BiologyCell Growth and DevelopmentCells CulturedbiologyAkt/PKB signaling pathwayCell adhesion moleculeGlycogen Synthase KinasesCell BiologyCell biologyEnzyme ActivationBiochemistryIntegrin alpha MCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinIntegrin beta 6CollagenMitogen-Activated Protein KinasesProto-Oncogene Proteins c-aktProtein BindingSignal TransductionMolecular and cellular biology
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Rho protein inhibition blocks protein kinase C translocation and activation.

1998

Small GTP-binding proteins of the Ras and Rho family participate in various important signalling pathways. Large clostridial cytotoxins inactivate GTPases by UDP-glucosylation. Using Clostridium difficile toxin B-10463 (TcdB) for inactivation of Rho proteins (RhoA/Rac/Cdc42) and Clostridium sordellii lethal toxin-1522 (TcsL) for inactivation of Ras-proteins (Ras/Rac/Ral, Rap) the role of these GTPases in protein kinase C (PKC) stimulation was studied. Phorbol-myristate-acetate (PMA) induced a rapid PKC translocation to and activation in the particulate cell fraction as determined by PKC-activity measurements and Western blots for PKC alpha. These effects were blocked by TcdB inhibiting Rho …

LipopolysaccharidesRHOASwineBiophysicsClostridium difficile toxin ABronchiCell Cycle ProteinsGTPaseCDC42PKC alphaBiochemistryGTP-Binding ProteinsRHO protein GDP dissociation inhibitorAnimalsHumanscdc42 GTP-Binding ProteinMolecular BiologyProtein kinase CCells CulturedProtein Kinase CbiologyEpithelial CellsCell BiologyMolecular biologyCell biologyEnzyme ActivationCdc42 GTP-Binding Proteinbiology.proteinras ProteinsTetradecanoylphorbol AcetateEndothelium VascularrhoA GTP-Binding ProteinBiochemical and biophysical research communications
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