Search results for "Secretory pathway"

showing 10 items of 46 documents

Effects of Constant and Doublet Frequency Electrical Stimulation Patterns on Force Production of Knee Extensor Muscles

2016

International audience; This study compared knee extensors' neuromuscular fatigue in response to two 30-minute stimulation patterns: constant frequency train (CFT) and doublet frequency train (DFT). Fifteen men underwent two separate sessions corresponding to each pattern. Measurements included torque evoked by each contraction and maximal voluntary contractions (MVC) measured before and immediately after the stimulation sessions. In addition, activation level and torque evoked during doublets (Pd) and tetanic contractions at 80-Hz (P80) and 20-Hz (P20) were determined in six subjects. Results indicated greater mean torque during the DFT stimulation session as compared with CFT. But, no dif…

MalecontractionsMuscle PhysiologyCritical Care and Emergency MedicineContraction (grammar)Knee JointRefractory Period ElectrophysiologicalPhysiologyRefractory periodKneeslcsh:MedicineStimulationKnee JointsIsometric exerciseElectromyographyPathology and Laboratory MedicineEndoplasmic Reticulum0302 clinical medicineNuclear magnetic resonanceMedicine and Health Scienceslcsh:ScienceSpinal Cord InjuryMusculoskeletal SystemTrauma MedicinePhysicsSecretory PathwayMultidisciplinarymedicine.diagnostic_test[ SDV.MHEP.PHY ] Life Sciences [q-bio]/Human health and pathology/Tissues and Organs [q-bio.TO]PhysicsClassical MechanicsAnatomyNeurologyCell ProcessesPhysical SciencesMuscle FatigueLegsspinal-cord-injuryAnatomyCellular Structures and Organellesmedicine.symptomadaptationsTraumatic InjuryindividualsResearch ArticleMuscle ContractionMuscle contractionAdulthuman skeletal-muscleSurgical and Invasive Medical ProcedurestrainsMotion03 medical and health sciencesSigns and SymptomsDiagnostic MedicineIsometric ContractionSarcoplasmic Reticula[SDV.MHEP.PHY]Life Sciences [q-bio]/Human health and pathology/Tissues and Organs [q-bio.TO]medicineHumansFunctional electrical stimulationMuscle SkeletalpotentiationFunctional Electrical StimulationMuscle fatigueElectromyographylcsh:RLimbs (Anatomy)Biology and Life SciencesCell Biology030229 sport sciencesElectric StimulationJoints (Anatomy)Torquerecruitmentresponseslcsh:Qfatigue030217 neurology & neurosurgery
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How to Make a Vesicle: Coat Protein-Membrane Interactions

2018

MembraneChemistryVesicleVesicle coatPlant cellEukaryotic cellSecretory pathwayCell biology
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Putative p24 complexes in Arabidopsis contain members of the delta and beta subfamilies and cycle in the early secretory pathway

2013

p24 proteins are a family of type I membrane proteins localized to compartments of the early secretory pathway and to coat protein I (COPI)- and COPII-coated vesicles. They can be classified, by sequence homology, into four subfamilies, named p24α, p24β, p24γ, and p24δ. In contrast to animals and fungi, plants contain only members of the p24β and p24δ subfamilies, the latter probably including two different subclasses. It has previously been shown that transiently expressed red fluorescent protein (RFP)-p24δ5 (p24δ1 subclass) localizes to the endoplasmic reticulum (ER) at steady state as a consequence of highly efficient COPI-based recycling from the Golgi apparatus. It is now shown that tr…

PhysiologyArabidopsisGolgi ApparatusPlant ScienceEndoplasmic ReticulumGreen fluorescent proteinsymbols.namesakeArabidopsisImmunoprecipitationER–Golgi transportcoat protein II (COPII)Secretory pathwayMicroscopy ConfocalSecretory PathwaybiologyArabidopsis ProteinsEndoplasmic reticulumcoat protein I (COPI)COPIImmunogold labellingGolgi apparatussecretory pathway.biology.organism_classificationImmunohistochemistryCell biologyMicroscopy Electronp24 proteinsMembrane proteinsymbolsResearch PaperPlasmidsJournal of Experimental Botany
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Coupled transport of Arabidopsis p24 proteins at the ER–Golgi interface

2012

p24 proteins are a family of type I membrane proteins localized to compartments of the early secretory pathway and to coat protein I (COPI)- and COPII-coated vesicles. They can be classified, by sequence homology, into four subfamilies, named p24α, p24β, p24γ, and p24δ. In contrast to animals and fungi, plants contain only members of the p24β and p24δ subfamilies. It has previously been shown that transiently expressed red fluorescent protein (RFP)–p24δ5 localizes to the endoplasmic reticulum (ER) as a consequence of highly efficient COPI-based recycling from the Golgi apparatus. Using specific antibodies, endogenous p24δ5 has now been localized to the ER and p24β2 to the Golgi apparatus in…

PhysiologyMolecular Sequence DataArabidopsisGolgi ApparatusPlant ScienceBiologyEndoplasmic Reticulumcoat protein (COP) IIcoat protein (COP) Isymbols.namesakeAmino Acid SequenceER–Golgi transportCOPIISecretory pathwayArabidopsis ProteinsVesicular-tubular clusterEndoplasmic reticulumMembrane ProteinsCOPIGolgi apparatussecretory pathwayTransport proteinCell biologyProtein TransportSecretory proteinp24 proteinssymbolsProtein BindingResearch PaperJournal of Experimental Botany
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Out for a Walk Along the Secretory Pathway During Programmed Cell Death

2015

This chapter provides a comprehensive updated analysis on the role of the secretory pathway in the orchestration of cell’s demise, an emerging and promising research topic in the field of plant programmed cell death (PCD). Since my first review on this topic, a plethora of data has been published supporting the concept that endomembrane system-forming subcellular compartments cooperate to coordinate cellular responses to developmental and environmental cues and thereby can dictate a cell’s ultimate fate. Thus, the early secretory pathway, encompassing the endoplasmic reticulum and Golgi apparatus, can be involved in the perception of extrinsic and intrinsic stimuli. It can also be an active…

Programmed cell deathEndoplasmic reticulumfungifood and beveragesVacuoleBiologyGolgi apparatusCell biologysymbols.namesakeOrganellesymbolsCompartment (development)Endomembrane systemSecretory pathway
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Dithiothreitol Treatment of Madin-Darby Canine Kidney Cells Reversibly Blocks Export from the Endoplasmic Reticulum but Does Not Affect Vectorial Tar…

1995

Addition of dithiothreitol (DTT) to the culture medium of Madin-Darby canine kidney (MDCK) cells blocks transport of newly synthesized gp80 (clusterin, apolipoprotein J), a soluble marker protein for apical exocytosis in this epithelial cell line. In cells treated with DTT during pulse labeling, gp80 is retained in the endoplasmic reticulum. After removal of the reducing agent, gp80 is posttranslationally oxidized and secreted at the apical surface of MDCK cell monolayers. This demonstrates that when folded and oxidized posttranslationally, gp80 can acquire a conformation that exhibits sorting signals for vectorial targeting. In the continuous presence of DTT, the transepithelial electrical…

Protein FoldingProtein ConformationBiologyEndoplasmic ReticulumKidneySulfur RadioisotopesBiochemistryEpitheliumExocytosisDithiothreitolCell LineMembrane Potentialssymbols.namesakechemistry.chemical_compoundDogsMethioninemedicineAnimalsCysteineSalivary Proteins and PeptidesMolecular BiologySecretory pathwayGlycoproteinsTight junctionEndoplasmic reticulumCell MembraneCell BiologyGolgi apparatusEpitheliumCell biologyDithiothreitolClusterinmedicine.anatomical_structureSecretory proteinchemistrysymbolsOxidation-ReductionProtein Processing Post-TranslationalMolecular ChaperonesJournal of Biological Chemistry
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Calcium negatively regulates meprin β activity and attenuates substrate cleavage

2015

The meprin β metalloproteinase is an important enzyme in extracellular matrix turnover, inflammation, and neurodegeneration in humans and mice. Previous studies showed a diminished cleavage of certain meprin β substrates in the presence of calcium, although the mechanism was not clear. With the help of a specific fluorogenic peptide assay and the human amyloid precursor protein as substrate, we demonstrated that the influence of calcium is most likely a direct effect on human meprin β itself. Analyzing the crystal structures of pro- and mature meprin β helped to identify a cluster of negatively charged amino acids forming a potential calcium binding site. Mutation of 2 of these residues (D2…

Protein Foldingchemistry.chemical_elementCalciumEndoplasmic ReticulumBiochemistryCell LineSubstrate SpecificityAmyloid beta-Protein PrecursorChlorocebus aethiopsGeneticsAmyloid precursor proteinAnimalsHumansAmino Acid SequenceBinding siteProtein precursorMolecular BiologyCellular localizationSecretory pathwayMetalloproteinaseAmyloid beta-PeptidesBinding SitesbiologyEndoplasmic reticulumMetalloendopeptidasesCell biologyHEK293 CellschemistryCOS CellsMutationMetalloproteasesbiology.proteinCalciumAmyloid Precursor Protein SecretasesSequence AlignmentBiotechnologyThe FASEB Journal
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Secretory Pathway Research: The More Experimental Systems the Better

2012

Transient gene expression, in plant protoplasts or specific plant tissues, is a key technique in plant molecular cell biology, aimed at exploring gene products and their modifications to examine functional subdomains, their interactions with other biomolecules, and their subcellular localization. Here, we highlight some of the major advantages and potential pitfalls of the most commonly used transient gene expression models and illustrate how ectopic expression and the use of dominant mutants can provide insights into protein function.

Protein functionMolecular cell biologySecretory PathwayProtoplastsResearchfungiMutantfood and beveragesBiological TransportCell BiologyPlant ScienceBiologySubcellular localizationCell biologyPlant LeavesPerspectiveGene expressionEctopic expressionGeneSecretory pathwayFluorescent DyesThe Plant Cell
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The ER-Membrane Transport System Is Critical for Intercellular Trafficking of the NSm Movement Protein and Tomato Spotted Wilt Tospovirus.

2015

Plant viruses move through plasmodesmata to infect new cells. The plant endoplasmic reticulum (ER) is interconnected among cells via the ER desmotubule in the plasmodesma across the cell wall, forming a continuous ER network throughout the entire plant. This ER continuity is unique to plants and has been postulated to serve as a platform for the intercellular trafficking of macromolecules. In the present study, the contribution of the plant ER membrane transport system to the intercellular trafficking of the NSm movement protein and Tomato spotted wilt tospovirus (TSWV) is investigated. We showed that TSWV NSm is physically associated with the ER membrane in Nicotiana benthamiana plants. An…

RNA viruses0301 basic medicineLeavesCell MembranesNicotiana benthamianaPlant ScienceEndoplasmic ReticulumPathology and Laboratory MedicineBiochemistrySolanum lycopersicumTospovirusBunyavirusesMedicine and Health SciencesArabidopsis thalianaMovement proteinBiology (General)Integral membrane proteinSecretory PathwaybiologyPlant BiochemistryPlant AnatomyPlasmodesmataProteïnes de membranafood and beveragesPlantsPlants Genetically ModifiedCell biologyTransport proteinPlant Viral Movement ProteinsProtein TransportMedical MicrobiologyCell ProcessesViral PathogensVirusesPathogensCellular Structures and OrganellesTomato Spotted Wilt VirusResearch ArticleBioquímicaCell PhysiologyQH301-705.5Arabidopsis ThalianaImmunologyPlant PathogensBrassicaPlasmodesmaResearch and Analysis MethodsMicrobiologyPlant Viral Pathogens03 medical and health sciencesModel OrganismsPlant and Algal ModelsVirologyTobaccoGeneticsIntegral Membrane ProteinsSecretionMicrobial PathogensMolecular BiologyPlant DiseasesBiology and life sciencesEndoplasmic reticulumfungiOrganismsMembrane ProteinsCell BiologyPlant PathologyRC581-607biology.organism_classificationVirosis (Plantes)VirologyPlant Leaves030104 developmental biologyMembrane TraffickingParasitologyImmunologic diseases. AllergyPLoS Pathogens
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In vivo Trafficking and Localization of p24 Proteins in Plant Cells

2008

p24 proteins constitute a family of putative cargo receptors that traffic in the early secretory pathway. p24 proteins can be divided into four subfamilies (p23, p24, p25 and p26) by sequence homology. In contrast to mammals and yeast, most plant p24 proteins contain in their cytosolic C-terminus both a dilysine motif in the -3, -4 position and a diaromatic motif in the -7, -8 position. We have previously shown that the cytosolic tail of Arabidopsis p24 proteins has the ability to interact with ARF1 and coatomer (through the dilysine motif) and with COPII subunits (through the diaromatic motif). Here, we establish the localization and trafficking properties of an Arabidopsis thaliana p24 pr…

Recombinant Fusion ProteinsMolecular Sequence DataArabidopsisGolgi ApparatusVacuoleProtein Sorting SignalsBiologyEndoplasmic ReticulumBiochemistrysymbols.namesakeStructural BiologyArabidopsisGeneticsAnimalsHumansProtein IsoformsAmino Acid SequenceMolecular BiologyCOPIISecretory pathwayArabidopsis ProteinsLysineEndoplasmic reticulumMembrane ProteinsCell BiologyCOPIGolgi apparatusbiology.organism_classificationActinsCell biologyDNA-Binding ProteinsProtein TransportBiochemistryCoatomerVacuolessymbolsCOP-Coated VesiclesCarrier ProteinsTranscription FactorsTraffic
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