Search results for "nucleoplasmic reticulum"

showing 2 items of 2 documents

Itraconazole inhibits nuclear delivery of extracellular vesicle cargo by disrupting the entry of late endosomes into the nucleoplasmic reticulum

2021

ABSTRACT Extracellular vesicles (EVs) are mediators of intercellular communication under both healthy and pathological conditions, including the induction of pro‐metastatic traits, but it is not yet known how and where functional cargoes of EVs are delivered to their targets in host cell compartments. We have described that after endocytosis, EVs reach Rab7+ late endosomes and a fraction of these enter the nucleoplasmic reticulum and transport EV biomaterials to the host cell nucleoplasm. Their entry therein and docking to outer nuclear membrane occur through a tripartite complex formed by the proteins VAP‐A, ORP3 and Rab7 (VOR complex). Here, we report that the antifungal compound itracona…

Models MolecularHistologyAntifungal AgentsEndosomeNuclear EnvelopeNucleoplasmic reticulumActive Transport Cell NucleusVesicular Transport ProteinsHost cell nucleoplasmEndosomesEndocytosisFatty Acid-Binding ProteinsExosomeCell LineExtracellular VesiclesCell MovementSettore BIO/13 - Biologia ApplicataHumanscancerexosomemetastasisendosomeResearch ArticlesCholestenonesmicro‐vesicleQH573-671Chemistryrab7 GTP-Binding ProteinsCell BiologyExtracellular vesicleSaponinsEndocytosisCell biologyKetoconazoleCancer cellintercellular communicationnucleoplasmic reticulumcancer endosome exosome intercellular communication metastasis micro-vesicle nucleoplasmicreticulumItraconazoleCytologyIntracellularResearch ArticleJournal of Extracellular Vesicles
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Nuclear calcium signaling by inositol trisphosphate in GH3 pituitary cells

2008

It has been proposed that nuclear and cytosolic Ca2+ ([Ca2+]N and [Ca2+]C) may be regulated independently. We address here the issue of whether inositol trisphosphate (IP3) can, bypassing changes of [Ca2+]C, produce direct release of Ca2+ into the nucleoplasm. We have used targeted aequorins to selectively measure and compare the changes in [Ca2+]C and [Ca2+]N induced by IP3 in GH3 pituitary cells. Heparin, an IP3 inhibitor that does not permeate the nuclear pores, abolished the [Ca2+]C peaks but inhibited only partly the [Ca2+]N peaks. The permeant inhibitor 2-aminoethoxy-diphenyl-borate (2-APB) blocked both responses. Removal of ATP also inhibited more strongly the [Ca2+]C than [Ca2+]N pe…

endocrine systemCytoplasm[SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT]PhysiologyAequorinNucleoplasmic reticulumaequorinInositol 145-TrisphosphateCell Line03 medical and health scienceschemistry.chemical_compound0302 clinical medicinenuclear signal transductionmedicineAnimalsInositol 145-Trisphosphate Receptorsinositol trisphosphate receptorsCalcium SignalingReceptorMolecular Biology030304 developmental biologyCell Nucleus0303 health sciencesNucleoplasmbiologypituitary cellsInositol trisphosphateCell Biologyherpes simplex virusMolecular biologyRatsCytosolmedicine.anatomical_structurechemistryCytoplasmPituitary Glandbiology.proteinnucleoplasmic reticulumNucleus030217 neurology & neurosurgery
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