Search results for "Secretor"

showing 10 items of 159 documents

A further analysis of secretory structures of some taxa belonging to the genus Hypericum (Clusiaceae) in relation to the leaf vascular pattern

2014

This work extends knowledge about the distribution of secretory structures (black nodules, translucent glands, and type A and B secretory canals) to other species of the genus Hypericum L., as only H. perforatum L. appears to have been widely investigated. Moreover, the current study was extended to include leaf vascular patterns. In the species studied, a possible correlation between the presence of black nodules and a particular biological form, that of hemicryptophytes scapose perennials such as H. perfoliatum L., H. perforatum L., H. pubescens Boiss., H. tetrapterum Fr., and H. triquetrifolium Turra, was noted. These black nodules are not present in H. androsaemum L. and H. hircinum L.,…

Perennial plantbiologyXylemClusiaceaePlant Scienceblack nodulebiology.organism_classificationTetrapterumTaxonsecretory canalKey words: Hypericumleaf vascular patternblack nodulessecretory canalstranslucent glandsGenustranslucent glandsBotanyHypericum leaf vascular pattern black nodules secretory canals translucent glandsleaf vascular patternHypericumHypericum
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In vitro release of lectins by Phallusia mamillata hemocytes.

1991

Abstract α-Lactose specific lectins are released from Phallusia mamillata hemocytes during short-term cultures. The molecular weight of the subunits, the immunological cross-reaction and the sugar specificity suggest that the released lectins are similar to those isolated from the sonicated hemocytes. Because lectin release appears to take place independently of active protein synthesis, the possibility exists that lectins are pre-formed, stored in hemocytes and released when in vitro conditions stimulate the cells.

PhallusiaAmanitinsHemocytesHemocyteImmunologyBiologyTunicateLectinsAnimalsUrochordataCycloheximideCells Culturedchemistry.chemical_classificationLectinActive proteinbiology.organism_classificationIn vitroCulture MediaBiochemistrychemistryReleasebiology.proteinDactinomycinLiberationGlycoproteinSecretory RateLectinDevelopmental BiologyDevelopmental and comparative immunology
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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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A membrane associated metalloprotease cleaves Cry3Aa Bacillus thuringiensis toxin reducing pore formation in Colorado potato beetle brush border memb…

2007

AbstractInsect proteases are implicated in Bacillus thuringiensis insecticidal proteins mode of action determining toxin specificity and sensitivity. Few data are available on the involvement of proteases in the later steps of toxicity such as protease interaction with toxin–receptor complexes and the pore formation process. In this study, a Colorado potato beetle (CPB) midgut membrane metalloprotease was found to be involved in the proteolytic processing of Cry3Aa. Interaction of Cry3Aa with BBMV membrane proteases resulted in a distinct pattern of proteolysis. Cleavage was demonstrated to occur in protease accessible regions of domain III and was specifically inhibited by the metalloprote…

ProteasesCell Membrane PermeabilityPore formationProteolysismedicine.medical_treatmentBacterial ToxinsBacillus thuringiensisBiophysicsInsecticidal toxinBiochemistryCry3Aa proteolysisHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineColorado potato beetleAnimalsMetalloprotease inhibitorMetalloproteinaseBinding SitesProteaseBacillus thuringiensis ToxinsMicrovillibiologymedicine.diagnostic_testSecretory VesiclesAcetohydroxamic acidColorado potato beetleCell Biologybiology.organism_classificationProteaseColeopteraEndotoxinsModels ChemicalBiochemistryPorosityProtein Bindingmedicine.drugBiochimica et Biophysica Acta (BBA) - Biomembranes
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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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Identification of Prostate-Enriched Proteins by In-depth Proteomic Analyses of Expressed Prostatic Secretions in Urine

2012

Urinary expressed prostatic secretion or "EPS-urine" is proximal tissue fluid that is collected after a digital rectal exam (DRE). EPS-urine is a rich source of prostate-derived proteins that can be used for biomarker discovery for prostate cancer (PCa) and other prostatic diseases. We previously conducted a comprehensive proteome analysis of direct expressed prostatic secretions (EPS). In the current study, we defined the proteome of EPS-urine employing Multidimensional Protein Identification Technology (MudPIT) and providing a comprehensive catalogue of this body fluid for future biomarker studies. We identified 1022 unique proteins in a heterogeneous cohort of 11 EPS-urines derived from …

Proteomics prostate cancer expressed prostatic secretions urineMaleProteomicsProstatic DiseasesProteomeProstatic Secretory ProteinsHuman Protein AtlasComputational biologyProstatic DiseasesBiologyProteomicsBioinformaticsBiochemistryArticleMass SpectrometryProstate cancerSettore BIO/13 - Biologia ApplicataProstatemedicineHumansBiomarker discoveryDatabases ProteinChromatography High Pressure LiquidGene Expression ProfilingProstateProstatic NeoplasmsProstatic Secretory ProteinsReproducibility of ResultsGeneral Chemistrymedicine.diseasemedicine.anatomical_structureCase-Control StudiesProteomeJournal of Proteome Research
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