Search results for "CDC42"

showing 10 items of 26 documents

An immune escape screen reveals Cdc42 as regulator of cancer susceptibility to lymphocyte-mediated tumor suppression.

2007

Abstract Adoptive cellular immunotherapy inducing a graft-versus-tumor (GVT) effect is the therapeutic mainstay of allogeneic hematopoietic stem cell transplantation (ASCT) for high-risk leukemias. Autologous immunotherapies using vaccines or adoptive transfer of ex vivo–manipulated lymphocytes are clinically explored in patients with various cancer entities. Main reason for failure of ASCT and cancer immunotherapy is progression of the underlying malignancy, which is more prevalent in patients with advanced disease. Elucidating the molecular mechanisms contributing to immune escape will help to develop strategies for the improvement of immunologic cancer treatment. To this end, we have und…

MAPK/ERK pathwayCytotoxicity ImmunologicAdoptive cell transferTranscription GeneticMAP Kinase Signaling Systemmedicine.medical_treatmentImmunologyMolecular Sequence DataApoptosisBiologyBiochemistryMiceImmune systemCancer immunotherapyNeoplasmsmedicineCytotoxic T cellAnimalsHumansLymphocytescdc42 GTP-Binding ProteinCells CulturedBase SequenceCancerCell BiologyHematologymedicine.diseaseGene Expression Regulation NeoplasticMice Inbred C57BLCdc42 GTP-Binding ProteinProto-Oncogene Proteins c-bcl-2ImmunologyCancer cellCancer researchDisease SusceptibilityNeoplasm TransplantationBlood
researchProduct

New neurons use Slit-Robo signaling to migrate through the glial meshwork and approach a lesion for functional regeneration

2018

Appropriate positioning of new neurons in the brain promotes post-stroke functional recovery.

Male0301 basic medicineanimal structuresNeurogenesisBiologyLesionMice03 medical and health sciences0302 clinical medicineDevelopmental NeuroscienceNeuroblastCell MovementNeuroblast migrationmental disordersmedicineAnimalsRegenerationcardiovascular diseasesReceptors ImmunologicProgenitor cellcdc42 GTP-Binding ProteinResearch Articlesreproductive and urinary physiologyMice KnockoutNeuronsMultidisciplinaryRegeneration (biology)fungiNeurogenesisSciAdv r-articlesBrainActin cytoskeletonSlit-RoboActin Cytoskeleton030104 developmental biologynervous systemCellular NeuroscienceAstrocytesembryonic structuresIntercellular Signaling Peptides and ProteinsProtein Multimerizationmedicine.symptomNeurogliaNeurosciencepsychological phenomena and processes030217 neurology & neurosurgeryResearch ArticleProtein BindingSignal TransductionScience Advances
researchProduct

Variant toxin B and a functional toxin A produced by Clostridium difficile C34.

2001

A particular property of Clostridium difficile strain C34 is an insertion of approximately 2 kb in the tcdA-C34 gene that does not hinder expression of a fully active TcdA-C34 molecule. Intoxication with TcdA-C34 induced an arborized appearance in eukaryotic cells (D-type cytopathic effect); intoxication with TcdB-C34 induced a spindle-like appearance of cells (S-type cytopathic effect). Inactivation of GTPases with purified toxins revealed that Rho, Rac, Cdc42, and Rap are substrates of TcdA-C34. The variant cytotoxin TcdB-C34 inactivated Rho, Rac, Cdc42, Rap, Ral, and R-Ras. Hence, this is the first ‘S-type’ cytotoxin which inactivates both Rho and R-Ras, and is coexpressed with a ‘D-type…

MaleCell SurvivalBacterial ToxinsClostridium difficile toxin AClostridium difficile toxin BGTPaseEnterotoxinCHO CellsBiologymedicine.disease_causeMicrobiologyMicrobiologyEnterotoxinsBacterial ProteinsCricetinaeGeneticsmedicineAnimalsHumansMolecular BiologyCells CulturedCytopathic effectSkinToxinClostridioides difficileCytotoxinsGenetic VariationClostridium difficileMolecular biologyCdc42 GTP-Binding ProteinDNA Transposable ElementsMicroscopy Electron ScanningFEMS microbiology letters
researchProduct

Profilin 1 is required for peripheral nervous system myelination

2014

Myelination allows rapid saltatory propagation of action potentials along the axon and is an essential prerequisite for the normal functioning of the nervous system. During peripheral nervous system (PNS) development, myelin-forming Schwann cells (SCs) generate radial lamellipodia to sort and ensheath axons. This process requires controlled cytoskeletal remodeling, and we show that SC lamellipodia formation depends on the function of profilin 1 (Pfn1), an actin-binding protein involved in microfilament polymerization. Pfn1 is inhibited upon phosphorylation by ROCK, a downstream effector of the integrin linked kinase pathway. Thus, a dramatic reduction of radial lamellipodia formation is obs…

Nervous systemrac1 GTP-Binding ProteinNeurogenesisCèl·lulesSchwann cellRAC1CDC42Axonal TransportBiotecnologiaMiceProfilinsPeripheral Nervous SystemmedicineAnimalsIntegrin-linked kinasePeripheral NervesPseudopodiaAxonMolecular BiologyCells CulturedMyelin SheathMice KnockoutbiologyNeuropeptidesCell biologyMice Inbred C57BLmedicine.anatomical_structureProfilinnervous systemImmunologybiology.proteinSchwann CellsLamellipodiumProteïnesDevelopmental BiologyDevelopment (Cambridge)
researchProduct

Rho protein inactivation induced apoptosis of cultured human endothelial cells.

2002

Small GTP-binding Rho GTPases regulate important signaling pathways in endothelial cells, but little is known about their role in endothelial cell apoptosis. Clostridial cytotoxins specifically inactivate GTPases by glucosylation [ Clostridium difficile toxin B-10463 (TcdB-10463), C. difficile toxin B-1470 (TcdB-1470)] or ADP ribosylation ( C. botulinum C3 toxin). Exposure of human umbilical cord vein endothelial cells (HUVEC) to TcdB-10463, which inhibits RhoA/Rac1/Cdc42, or to C3 toxin, which inhibits RhoA, -B, -C, resulted in apoptosis, whereas inactivation of Rac1/Cdc42 with TcdB-1470 was without effect, suggesting that Rho inhibition was responsible for endothelial apoptosis. Disruptio…

Pulmonary and Respiratory Medicinerac1 GTP-Binding Proteinrho GTP-Binding ProteinsProgrammed cell deathUmbilical VeinsEndotheliumPhysiologyBacterial ToxinsCASP8 and FADD-Like Apoptosis Regulating ProteinApoptosisBcl-2-associated X proteinBacterial ProteinsPhysiology (medical)Proto-Oncogene ProteinsmedicineCyclic AMPIn Situ Nick-End LabelingHumanscdc42 GTP-Binding ProteinCells Culturedbcl-2-Associated X ProteinAdenosine Diphosphate RibosebiologyCaspase 3Intracellular Signaling Peptides and ProteinsCell BiologyCaspase 9Cell biologyNeoplasm ProteinsEndothelial stem cellmedicine.anatomical_structureCdc42 GTP-Binding ProteinProto-Oncogene Proteins c-bcl-2Cell cultureApoptosisCaspasesbiology.proteinMyeloid Cell Leukemia Sequence 1 ProteinEndothelium VascularSignal transductionCarrier ProteinsrhoA GTP-Binding ProteinBH3 Interacting Domain Death Agonist ProteinSignal TransductionAmerican journal of physiology. Lung cellular and molecular physiology
researchProduct

PAR1 signaling regulates the retention and recruitment of EPCR-expressing bone marrow hematopoietic stem cells

2015

Retention of long-term repopulating hematopoietic stem cells (LT-HSCs) in the bone marrow is essential for hematopoiesis and for protection from myelotoxic injury. We report that signaling cascades that are traditionally viewed as coagulation related also control retention of endothelial protein C receptor-positive (EPCR(+)) LT-HSCs in the bone marrow and their recruitment to the blood via two pathways mediated by protease activated receptor 1 (PAR1). Thrombin-PAR1 signaling induces nitric oxide (NO) production, leading to EPCR shedding mediated by tumor necrosis factor-α-converting enzyme (TACE), enhanced CXCL12-CXCR4-induced motility and rapid stem and progenitor cell mobilization. Conver…

Receptors CXCR4Receptors Cell SurfaceADAM17 ProteinIntegrin alpha4beta1BiologyNitric OxideArticleGeneral Biochemistry Genetics and Molecular BiologyMiceBone MarrowCell MovementCell AdhesionmedicineAnimalsReceptor PAR-1Progenitor cellcdc42 GTP-Binding ProteinCell adhesionEndothelial protein C receptorThrombinEndothelial Protein C ReceptorGeneral MedicineHematopoietic Stem CellsChemokine CXCL12Cell biologyMice Inbred C57BLTransplantationADAM ProteinsHaematopoiesismedicine.anatomical_structureCdc42 GTP-Binding ProteinImmunologyBone marrowStem cellProtein CSignal TransductionNature Medicine
researchProduct

Ras, Rap, and Rac Small GTP-binding Proteins Are Targets for Clostridium sordellii Lethal Toxin Glucosylation

1996

Lethal toxin (LT) from Clostridium sordellii is one of the high molecular mass clostridial cytotoxins. On cultured cells, it causes a rounding of cell bodies and a disruption of actin stress fibers. We demonstrate that LT is a glucosyltransferase that uses UDP-Glc as a cofactor to covalently modify 21-kDa proteins both in vitro and in vivo. LT glucosylates Ras, Rap, and Rac. In Ras, threonine at position 35 was identified as the target amino acid glucosylated by LT. Other related members of the Ras GTPase superfamily, including RhoA, Cdc42, and Rab6, were not modified by LT. Incubation of serum-starved Swiss 3T3 cells with LT prevents the epidermal growth factor-induced phosphorylation of m…

ThreonineUridine Diphosphate GlucoseRHOABacterial ToxinsMolecular Sequence DataClostridium sordelliimacromolecular substancesCDC42GTPaseBiologyCell morphologyBiochemistryGTP PhosphohydrolasesProto-Oncogene Proteins p21(ras)MiceGTP-binding protein regulatorsGTP-Binding ProteinsAnimalsHumansAmino Acid SequenceMolecular BiologyClostridiumEpidermal Growth FactorKinase3T3 CellsCell Biologybiology.organism_classificationMolecular biologyActinsrac GTP-Binding ProteinsActin CytoskeletonKineticsGlucoserap GTP-Binding ProteinsGlucosyltransferasesCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinPhosphorylationGuanosine TriphosphateHeLa CellsJournal of Biological Chemistry
researchProduct

cIAP1 oncogenic properties analysis : contribution of its partners cdc42 and E2F1

2014

The inhibitor of apoptosis protein cIAP1 (cellular inhibitor of apoptosis protein-1) from the IAP family (Inhibitor of Apoptosis Protein) is an oncogene with an E3 ubiquitin ligase activity. cIAP1 is relocalized from the nucleus to the cytoplasm during the differentiation of many kind of cellular models (macrophages, dendritic cells, colon epithelial cells, hematopoietic stem cells, cardiomyocytes) and this relocalization is associated with a proliferation arrest. The well-known functions of cIAP1 are associated with its cytoplasmic localization, where it regulates the TNFa receptors and NF-?B signaling pathways. However, cIAP1 is mainly expressed in the nucleus on many cell types which is …

[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyTNF-aFilipodiaProliferationActin cytoskeleton[SDV.BC]Life Sciences [q-bio]/Cellular BiologyCIAP1E2F1Rho GTPasesHRasCytosquelette d’actineOncogenic transformation[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyCdc42ProliférationFilipodes[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyTransformation oncogénique
researchProduct

GTPases of the Rho Subfamily Are Required for Brucella abortus Internalization in Nonprofessional Phagocytes

2001

Members of the genus Brucella are intracellular -Proteobacteria responsible for brucellosis, a chronic disease of humans and animals. Little is known about Brucella virulence mechanisms, but the abilities of these bacteria to invade and to survive within cells are decisive factors for causing disease. Transmission electron and fluorescence microscopy of infected nonprofessional phagocytic HeLa cells revealed minor membrane changes accompanied by discrete recruitment of F-actin at the site of Brucella abortus entry. Cell uptake of B. abortus was negatively affected to various degrees by actin, actin-myosin, and microtubule chemical inhibitors. Modulators of MAPKs and protein-tyrosine kinases…

biologymedia_common.quotation_subjectIntracellular parasiteBRUCELLA ABORTUSVirulenceCell BiologyCDC42BrucellaGTPasebiology.organism_classificationBiochemistryMicrobiologyBRUCELOSISCytotoxic T cellBRUCELLAESCHERICHIA COLIBACTERIASInternalizationMolecular BiologyIntracellularmedia_commonJournal of Biological Chemistry
researchProduct

Impact of amino acids 22-27 of Rho-subfamily GTPases on glucosylation by the large clostridial cytotoxins TcsL-1522, TcdB-1470 and TcdB-8864

1999

Here we report data describing some principles of the interaction between small GTP-binding proteins and large Clostridial cytotoxins (LCTs). Our investigation was based on the differential glucosylation of Rac1 versus RhoA by LCTs TcsL-1522, TcdB-1470 and TcdB-8864. Chimeric RhoA/Rac1 proteins and GTPases mutated at defined regions or single amino acids were used as substrates. Starting with chimeric Rac/Rho proteins we demonstrated that proteins containing the N-terminal 73 amino acids of Rac1 (but not those of RhoA) were efficiently glucosylated. Within this stretch, three regions differ significantly in Rac1 and RhoA. Regions containing amino acids 41-45 and 50-54 had no effect on toxin…

chemistry.chemical_classificationRHOAGlycosylationbiologyRAC1GTPaseBiochemistryAmino acidchemistry.chemical_compoundBiochemistrychemistryCdc42 GTP-Binding Proteinbiology.proteinBinding sitePeptide sequenceEuropean Journal of Biochemistry
researchProduct