Search results for "Endoplasm"

showing 10 items of 323 documents

Reply to Dr Michaudet al.

2015

There is no abstract

Cholagogues and Cholereticsbusiness.industryEndoplasmic reticulumAmyotrophic Lateral SclerosisTaurochenodeoxycholic acidTauroursodeoxycholic acidMitochondrionPharmacologyEndoplasmic Reticulummedicine.diseaseTaurochenodeoxycholic Acidchemistry.chemical_compoundNeurologychemistryImmunologyUnfolded Protein ResponsemedicineUnfolded protein responseAnimalsHumansTUDCA ALSSettore MED/26 - NeurologiaNeurology (clinical)Amyotrophic lateral sclerosisbusinessEuropean Journal of Neurology
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Endoplasmic reticulum‐resident chaperones modulate the inflammatory and angiogenic responses of endothelial cells

2015

SummaryBackground Wound healing depends on a well-balanced regulation of inflammation and angiogenesis. In chronic wounds the healing process is disturbed and inflammation persists. Regulation of wound closure is controlled by transmembrane and extracellular proteins, the folding and maturation of which occur in the endoplasmic reticulum (ER) by ER-resident chaperone machinery. Objectives To study the role of the ER-resident chaperones BiP/Grp78, its cochaperone Mdg1/ERdJ4, and Grp94 in chronic, nonhealing wounds. Methods Immunohistochemical staining of these chaperones in individual human biopsies and investigation of the possible role of BiP and Mdg1 in endothelial cells, focusing on thei…

Chronic woundChemokineAngiogenesisDown-RegulationNeovascularization PhysiologicInflammationDermatologyEndoplasmic ReticulumProinflammatory cytokinemedicineHumansEndoplasmic Reticulum Chaperone BiPCells CulturedHeat-Shock ProteinsInflammationWound HealingMembrane GlycoproteinsbiologyTumor Necrosis Factor-alphaEndoplasmic reticulumEndothelial CellsMembrane ProteinsHSP40 Heat-Shock ProteinsCell biologyChaperone (protein)Chronic Diseasebiology.proteinmedicine.symptomWound healingMolecular ChaperonesBritish Journal of Dermatology
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Endoplasmic Reticulum and Mitochondria: Independent Roles and Crosstalk in Fatty Liver Diseases and Hepatic Inflammation.

2015

Proper function of the endoplasmic reticulum (ER) and mitochondria is essential for cellular homeostasis and the regulation of metabolic pathways. Perturbation of their function has been linked to pathophysiological states, including metabolic and liver diseases. Fatty liver diseases are a major health problem whose prevalence is dramatically increasing, may be induced by several factors (mainly chronic alcohol consumption, drugs or metabolic alterations), and share common features as lipid deposition, inflammation, oxidative stress and progression to more severe clinical stages, such as fibrosis, cirrhosis or even hepatocellular carcinoma. Besides their independent contributions to metabol…

CirrhosisAnti-Inflammatory AgentsCellular homeostasisInflammation010501 environmental sciencesBiologyMitochondrionEndoplasmic Reticulum01 natural sciences03 medical and health sciences0302 clinical medicineDrug DiscoverymedicineAnimalsHumans0105 earth and related environmental sciencesPharmacologyInflammationEndoplasmic reticulumLiver DiseasesAutophagyFatty livermedicine.diseaseCell biologyMitochondriaFatty LiverCrosstalk (biology)030220 oncology & carcinogenesismedicine.symptomCurrent pharmaceutical design
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Organelle pH studies using targeted avidin and fluorescein–biotin

2000

Abstract Background: Mammalian organelles of the secretory pathway are of differing pH. The pH values form a decreasing gradient: the endoplasmic reticulum (ER) is nearly neutral, the Golgi is mildly acidic and the secretory granules are more acidic still (∼pH 5). The mechanisms that regulate pH in these organelles are still unknown. Results: Using a novel method, we tested whether differences in H + ‘leak' and/or counterion conductances contributed to the pH difference between two secretory pathway organelles. A pH-sensitive, membrane-permeable fluorescein–biotin was targeted to endoplasmic-reticulum- and Golgi-localized avidin-chimera proteins in HeLa cells. In live, intact cells, ER pH (…

Clinical BiochemistryBiotinGolgi ApparatusEndoplasmic ReticulumBiochemistrysymbols.namesakechemistry.chemical_compoundChloridesBiotinOrganelleDrug DiscoveryHumansMicroscopy ImmunoelectronMolecular BiologySecretory pathwayFluorescent DyesOrganellesPharmacologyIon TransportFlubi-2ChemistryEndoplasmic reticulumBafilomycinIntracellular MembranesGeneral MedicineHydrogen-Ion ConcentrationProton PumpsGolgi apparatusAvidinCytosolTargeted fluorescenceMembraneBiochemistryH+ pumpPotassiumsymbolsMolecular MedicineFluoresceinHeLa CellsH+ leakChemistry & Biology
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Material-driven fibronectin assembly rescues matrix defects due to mutations in collagen IV in fibroblasts

2020

Basement membranes (BMs) are specialised extracellular matrices that provide structural support to tissues as well as influence cell behaviour and signalling. Mutations in COL4A1/COL4A2, a major BM component, cause a familial form of eye, kidney and cerebrovascular disease, including stroke, while common variants in these genes are a risk factor for intracerebral haemorrhage in the general population. These phenotypes are associated with matrix defects, due to mutant protein incorporation in the BM and/or its absence by endoplasmic reticulum (ER) retention. However, the effects of these mutations on matrix stiffness, the contribution of the matrix to the disease mechanism(s) and its effects…

Collagen Type IVCell signalingPopulationIntegrinBiophysicsBioengineering02 engineering and technologyMatrix (biology)medicine.disease_causeBasement MembraneArticleBiomaterialsExtracellular matrix03 medical and health sciences0302 clinical medicineLamininmedicineExtracellularHumanseducationCell adhesion030304 developmental biologyeducation.field_of_study0303 health sciencesMutationbiologyChemistryEndoplasmic reticulumFibroblasts021001 nanoscience & nanotechnologyPhenotypeExtracellular MatrixFibronectinsCell biologyFibronectinMechanics of MaterialsMutationCeramics and Compositesbiology.protein0210 nano-technology030217 neurology & neurosurgeryBiomaterials
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A closer look at the cholesterol sensor

2002

Abstract Transport of the sterol regulatory element-binding protein (SREBP) cleavage-activating protein (SCAP)–SREBP complex from the endoplasmic reticulum (ER) to the Golgi is the central event mediating the cholesterol-feedback process in mammalian cells. A conformational change in SCAP is a crucial step; when cholesterol levels are high, the conformation of SCAP enables the SCAP–SREBP complex to associate with an insulin-induced gene (INSIG) retention protein in the ER. By contrast, when cholesterol levels are low, SCAP switches to a conformation that enables the dissociation of the retention protein and the association of SCAP–SREBP with COP II vesicles.

Conformational changeCholesterolEndoplasmic reticulumVesicleBiologyGolgi apparatusBiochemistrySterolSterol regulatory element-binding proteinCell biologysymbols.namesakechemistry.chemical_compoundBiochemistryStructural biologychemistrypolycyclic compoundssymbolslipids (amino acids peptides and proteins)Molecular BiologyTrends in Biochemical Sciences
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Sorting signals in the cytosolic tail of membrane proteins involved in the interaction with plant ARF1 and coatomer.

2004

Summary In mammals and yeast, a cytosolic dilysine motif is critical for endoplasmic reticulum (ER) localization of type I membrane proteins. Retrograde transport of type I membrane proteins containing dilysine motifs at their cytoplasmic carboxy (C)-terminal tail involves the interaction of these motifs with the COPI coat. The C-terminal dilysine motif has also been shown to confer ER localization to type I membrane proteins in plant cells. Using in vitro binding assays, we have analyzed sorting motifs in the cytosolic tail of membrane proteins, which may be involved in the interaction with components of the COPI coat in plant cells. We show that a dilysine motif in the −3,−4 position (rel…

CooperativityPlant ScienceBiologyCoatomer Proteinchemistry.chemical_compoundGeneticsAmino Acid SequencePlant ProteinsBinding SitesSequence Homology Amino AcidEndoplasmic reticulumProtoplastsMembrane ProteinsOryzaCell BiologyEndoplasmic reticulum localizationCOPIBrefeldin APeptide FragmentsCell biologyKineticsProtein SubunitsMembrane proteinchemistryAmino Acid SubstitutionCoatomerCytoplasmADP-Ribosylation Factor 1Sequence AlignmentSignal TransductionThe Plant journal : for cell and molecular biology
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Multiple modes of cell death in neuroendocrine tumors induced by artesunate.

2020

Abstract Background The paucity of effective treatment in neuroendocrine tumors (NETs) encouraged us to investigate the therapeutic value of artesunate (ART) promised by its inhibitory effect against various tumors and broad safety profile. Methods We evaluated the impact of ART on three NET cell lines, BON-1, QGP-1 and NCI-H727 on cellular and molecular levels. Results Our results showed that ART induced endoplasmic reticulum (ER) stress through phosphorylation of eIF2α, which further gave rise to autophagy in all three NET cell lines. Specifically, apoptosis and ferroptosis were also observed in BON-1 cells, which made BON-1 cell line more vulnerable upon ART treatment. The different sens…

Cyclin-Dependent Kinase Inhibitor p21NiacinamideProgrammed cell deathPharmaceutical ScienceArtesunateAntineoplastic AgentsApoptosisNeuroendocrine tumorsBiology03 medical and health scienceschemistry.chemical_compound0302 clinical medicineDownregulation and upregulationCell Line TumorDrug DiscoveryAntineoplastic Combined Chemotherapy ProtocolsmedicineAutophagyFerroptosisHumans030304 developmental biologyPharmacology0303 health sciencesEndoplasmic reticulumPhenylurea CompoundsAutophagymedicine.diseaseEndoplasmic Reticulum StressNeuroendocrine TumorsComplementary and alternative medicinechemistryCell cultureApoptosisArtesunate030220 oncology & carcinogenesisCancer researchMolecular MedicinePhytomedicine : international journal of phytotherapy and phytopharmacology
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ER stress in human hepatic cells treated with Efavirenz: Mitochondria again

2013

Background & Aims ER stress is associated with a growing number of liver diseases, including drug-induced hepatotoxicity. The non-nucleoside analogue reverse transcriptase inhibitor Efavirenz, a cornerstone of the multidrug strategy employed to treat HIV1 infection, has been related to the development of various adverse events, including metabolic disturbances and hepatic toxicity, the mechanisms of which remain elusive. Recent evidence has pinpointed a specific mitochondrial effect of Efavirenz in human hepatic cells. This study assesses the induction of ER stress by Efavirenz in the same model and the implication of mitochondria in this process. Methods Primary human hepatocytes and Hep3B…

CyclopropanesEfavirenzXBP1Anti-HIV AgentsMitochondria LiverMitochondrionBiologyPharmacologyModels BiologicalCell Linechemistry.chemical_compoundMicroscopy Electron TransmissionDownregulation and upregulationHumansSide effectsEndoplasmic Reticulum Chaperone BiPCells CulturedHepatologyEndoplasmic reticulumHepatotoxicityATF4HIVEndoplasmic Reticulum StressHIV Reverse TranscriptaseBenzoxazinesMitochondriachemistryAlkynesHepatocytesHepatic stellate cellUnfolded protein responseReverse Transcriptase InhibitorsThapsigarginCalciumEfavirenzER stressBiomarkersJournal of Hepatology
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ER-to-Golgi Transport: The COPII-Pathway

2006

The endoplasmic reticulum (ER) is the starting site of the journey of newly synthesized proteinsto the apoplast, plasma membrane and to the vacuolar compartments. Transport between these membranecompartments of the secretory pathway in eukaryotic cells is mediated by vesicles, which are producedby a budding mechanism involving coat proteins that capture specific cargo molecules and helppackage them into coated vesicles. These vesicles are known as COPII-coated vesicles, and are usuallyisolated after their induction in vitro using microsomal membranes, cytosol and a non-hydrolyzableGTP-analogue. COPII-coated vesicles are formed at specific sites in the ER known as ER-exit sites(ERES). ERES a…

Cytosolsymbols.namesakeChemistryEndoplasmic reticulumVesicleMicrosomesymbolsCoated vesicleGolgi apparatusCOPIISecretory pathwayCell biology
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