Search results for "immunoblotting"

showing 4 items of 124 documents

An alternative role of C1q in cell migration and tissue remodeling: contribution to trophoblast invasion and placental development.

2010

Abstract Fetal trophoblast cells invading the decidua in the early phase of pregnancy establish complex interaction with the maternal extracellular matrix. We discovered that C1q was widely distributed in human decidual stroma in the absence of C4 and C3 and was actively synthesized by migrating extravillous trophoblasts. The cells expressed the messages for the three chains of C1q and secreted this complement component that interacted with the proteins of the decidual extracellular matrix. Solid phase-bound C1q promoted trophoblast adhesion and migration, and cell binding to C1q resulted in activation of ERK1/2 MAPKs. Ab inhibition experiments showed that the receptors for the globular hea…

medicine.medical_specialtyImmunologyCellIntegrinImmunoblottingchemical and pharmacologic phenomenaBiologyExtracellular matrixMicePre-Eclampsiaimmune system diseasesPregnancyInternal medicinemedicineCell AdhesionImmunology and AllergyAnimalsHumansImmunoprecipitationskin and connective tissue diseasesReceptorCell adhesionreproductive and urinary physiologyMicroscopy ConfocalC1q placental development.Reverse Transcriptase Polymerase Chain ReactionComplement C1qDeciduaTrophoblastPlacentationImmunohistochemistryPlacentationCell biologyTrophoblastsMice Inbred C57BLChemotaxis Leukocytemedicine.anatomical_structureEndocrinologyembryonic structuresbiology.proteinFemaleJournal of immunology (Baltimore, Md. : 1950)
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Corticotropin-Releasing Hormone-Mediated Induction of Intracellular Signaling Pathways and Brain-Derived Neurotrophic Factor Expression Is Inhibited …

2005

CRH receptor (CRHR) 1 and the cannabinoid receptor 1 (CB1) are both G protein-coupled receptors. Activation of CRHR1 leadstoincreasesincAMPproductionandphosphorylationof the transcription factor cAMP response element-binding protein (CREB). In contrast, CB1 is negatively coupled to the cAMP signaling cascade. In this study, we analyzed a putative interaction between these two systems focusing on the regulation of the expression of brain-derived neurotrophic factor (BDNF), a CREB-regulated gene. In situ hybridization revealed coexpression of CRHR1 and CB1 receptors in the granular layer of the cerebellum. Therefore, we analyzed the effects of CRH and the CB1 agonist WIN-55,212-2 on BDNF expr…

medicine.medical_specialtyTime FactorsCorticotropin-Releasing HormoneMorpholinesmedicine.medical_treatmentImmunoblottingEnzyme-Linked Immunosorbent AssayTropomyosin receptor kinase BNaphthalenesCREBModels BiologicalRats Sprague-DawleyMiceEndocrinologyNeurotrophic factorsCerebellumInternal medicineCannabinoid Receptor ModulatorsCyclic AMPmedicineAnimalsRNA MessengerCyclic AMP Response Element-Binding ProteinReceptorEgtazic AcidCells CulturedIn Situ HybridizationNeuronsBrain-derived neurotrophic factorSulfonamidesbiologyReverse Transcriptase Polymerase Chain ReactionBrain-Derived Neurotrophic FactorCalcium Channel BlockersIsoquinolinesEndocannabinoid systemBenzoxazinesRatsMice Inbred C57BLPyrimidinesEndocrinologynervous systembiology.proteinCalciumCannabinoidSignal transductionEndocannabinoidsProtein BindingSignal TransductionEndocrinology
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Critical role of dipeptidyl peptidase IV in neuropeptide Y-mediated endothelial cell migration in response to wounding

2001

Recently, we have discovered that neuropeptide Y (NPY), a sympathetic neurotransmitter, is also present in human umbilical endothelial cells (HUVECs), and is potently chemotactic and angiogenic by acting on one or several of Y1-Y5 receptors. In HUVECs, NPY is co-localized with dipeptidyl peptidase IV (DPPIV) which cleaves Tyr(1)-Pro(2) from NPY(1-36) to form NPY(3-36) resulting in the formation of a non-Y1 receptor agonist, which remains angiogenic. Presently we studied the effects of DPPIV's blockade using monoclonal antibodies (mAbs) on migration of HUVECs in response to NPY(1-36) or NPY(3-36) following cell wounding. Both peptides caused similar dose-dependent increases in cell migration…

medicine.medical_specialtyTime FactorsEndotheliumPhysiologyDipeptidyl Peptidase 4Blotting WesternImmunoblottingBiologyBiochemistryDipeptidyl peptidaseUmbilical CordCellular and Molecular NeuroscienceEndocrinologyWestern blotCell MovementInternal medicinemental disordersmedicineHumansNeuropeptide YReceptormedicine.diagnostic_testChemotaxisNeuropeptide Y receptorhumanitiesCell biologyBlotEndothelial stem cellEndocrinologymedicine.anatomical_structureWounds and InjuriesEndothelium VascularPeptides
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RAB18 Loss Interferes With Lipid Droplet Catabolism and Provokes Autophagy Network Adaptations

2020

Autophagy is dependent on appropriate lipid supply for autophagosome formation. The regulation of lipid acquisition and the autophagy network response to lipid-limiting conditions are mostly elusive. Here, we show that the knockout of the RAB GTPase RAB18 interferes with lipid droplet catabolism, causing an impaired fatty acid release. The resulting reduced lipid-droplet-derived lipid availability influences autophagy and provokes adaptive modifications of the autophagy network. These adjustments include increased expression and phosphorylation of ATG2B as well as augmented formation of the ATG12-ATG5 conjugate. Moreover, ATG9A shows an enhanced phosphorylation at amino acid residues tyrosi…

rab3 GTP-Binding ProteinsImmunoblottingGTPaseReal-Time Polymerase Chain Reaction03 medical and health sciences0302 clinical medicineMicroscopy Electron TransmissionStructural BiologyLipid dropletAutophagyHumansPhosphorylationTyrosineMolecular Biology030304 developmental biology0303 health sciencesMicroscopy ConfocalChemistryCatabolismAutophagyAutophagosomesLipid DropletsImmunohistochemistryCell biologyrab GTP-Binding ProteinsPhosphorylationlipids (amino acids peptides and proteins)RabCRISPR-Cas Systems030217 neurology & neurosurgeryRAB18HeLa CellsJournal of Molecular Biology
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