Search results for "Plakin"

showing 10 items of 14 documents

New Acyclic Cytotoxic Jasplakinolide Derivative from the Marine Sponge Jaspis splendens

2019

A new acylic jasplakinolide congener (2), another acyclic derivative requiring revision (4), together with two jasplakinolide derivatives including the parent compound jasplakinolide (1) were isolated from the Indonesian marine sponge Jaspis splendens. The chemical structures of the new and known compounds were unambiguously elucidated based on HRESIMS and exhaustive 1D and 2D NMR spectral analysis as well as a comparison of their NMR data with those of jasplakinolide (1). The isolated jasplakinolides inhibited the growth of mouse lymphoma (L5178Y) cells in vitro with IC50 values in the low micromolar to nanomolar range.

0106 biological sciencesStereochemistryPharmaceutical Science01 natural sciencesjasplakinolide Z<sub>5</sub>Drug Discovery<i>Jaspis splendens</i>Ic50 valuesCytotoxic T cellSpectral analysisPharmacology Toxicology and Pharmaceutics (miscellaneous)lcsh:QH301-705.5cytotoxic activitybiology010405 organic chemistryChemistry010604 marine biology & hydrobiologyMouse LymphomaJaspis splendensbiology.organism_classificationIn vitro0104 chemical sciencesSpongelcsh:Biology (General)Two-dimensional nuclear magnetic resonance spectroscopyjasplakinolide Z<sub>6</sub>Marine Drugs
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Effect of intermittent shear stress on corneal epithelial cells using an in vitro flow culture model.

2018

Abstract Purpose The aim of this study was to establish and to evaluate an in vitro model for culturing human telomerase-immortalized corneal epithelial (hTCEpi) cells under adjustable medium flow mimicking the movements of the tear film on the ocular surface. Methods Using an IBIDI pump system, cells were cultured under unidirectional, continuous or oscillating, discontinuous medium flow. Cell surface and cytoskeletal architecture were investigated by scanning electron microscopy and immunofluorescence. Gene expression of e-cadherin, occludin, tight junction protein (TJP), desmoplakin, desmocollin and mucins was investigated by real-time PCR. Protein expression of desmoplakin, TJP, occludi…

0301 basic medicineStress fiberTight junctionbiologyBlinkingDesmoplakinChemistryEpithelium CornealMucinsEpithelial CellsOccludinCell junctionModels BiologicalCell biology03 medical and health sciencesOphthalmology030104 developmental biologyCell culturebiology.proteinShear stressHumansStress MechanicalMUC1BiomarkersCells CulturedThe ocular surface
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Intermediate filaments and desmosomal plaque proteins in testicular seminomas and non-seminomatous germ cell tumours as revealed by immunohistochemis…

1987

Seminomas and non-seminomatous testicular germ cell tumours were studied for the presence of cytokeratin and vimentin filaments and desmosomes using immunohistochemical methods. In the majority of the classical seminomas and in seminomatous areas of mixed tumours most tumour cells appeared to lack cytokeratin filaments. Some seminomas contained a focally variable proportion of cells exhibiting cytokeratin-positive structures while other cases contained only few seminoma cells with a well developed fibrillar cytokeratin network. Gel electrophoresis of cytoskeletal proteins from microdissected regions revealed cytokeratin polypeptides nos. 8 and 18 typical of simple epithelia. In one seminoma…

AdultMalePathologymedicine.medical_specialtyendocrine system diseasesAdolescentIntermediate FilamentsFluorescent Antibody TechniqueVimentinmacromolecular substancesAntigen-Antibody ComplexDysgerminomaBiologyurologic and male genital diseasesAntibodiesPathology and Forensic MedicineEmbryonal carcinomaCytokeratinTesticular NeoplasmsmedicineCarcinomaHumansVimentinIntermediate filamentMolecular BiologyCytoskeletonDesmoplakinMembrane ProteinsCell BiologyGeneral MedicineSeminomaDesmosomesmedicine.diseaseCytoskeletal ProteinsMicroscopy Electronmedicine.anatomical_structureDesmoplakinsbiology.proteinKeratinsGerm cellVirchows Archiv. A, Pathological anatomy and histopathology
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Shortstop Recruits EB1/APC1 and Promotes Microtubule Assembly at the Muscle-Tendon Junction

2003

Abstract Background: Shot (previously named Kakapo), is a Drosophila Plakin family member containing both Actin binding and microtubule binding domains. In Drosophila , it is required for a wide range of processes, including axon extension, dendrite formation, axonal terminal arborization at the neuromuscular junction, tendon cell development, and adhesion of wing epithelium. Results: To address how Shot exerts its activity at the molecular level, we investigated the molecular interactions of Shot with candidate proteins in mature larval tendon cells. We show that Shot colocalizes with EB1/APC1 and with a compact microtubule array extending between the muscle-tendon junction and the cuticle…

Blotting WesternFluorescent Antibody TechniqueBiologyTransfectionMicrotubulesCell junctionGeneral Biochemistry Genetics and Molecular BiologyTendonsTendon cellMicrotubuleAnimalsDrosophila ProteinsCytoskeletonActinPlakinAgricultural and Biological Sciences(all)Biochemistry Genetics and Molecular Biology(all)MusclesAxon extensionMicrofilament ProteinsfungiPrecipitin TestsCell biologyCytoskeletal ProteinsIntercellular JunctionsLarvaMuscle tendon junctionDrosophilaGeneral Agricultural and Biological SciencesCurrent Biology
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Complexus adhaerentes, a new group of desmoplakin-containing junctions in endothelial cells: II. Different types of lymphatic vessels.

1994

Abstract In diverse mammalian species, including (man, cow and rat) the very flat endothelial cells of lymphatic vessels of various organs, including the retothelial meshwork of sinus of lymph nodes, are connected by zonula -like plaque-bearing junctions which differ from the similarly structured junctions of blood vessel endothelia by the presence of desmoplakin or an as yet unknown but closely related plaque protein. These extended junctions, which also contain plakoglobin but none of the presently known desmogleins and desmocollins, are therefore different from the spot-like desmosomes ( maculae adhaerentes ) present in epithelia, myocardium and dendritic reticulum cells of lymphatic fol…

Cancer ResearchEndotheliumgovernment.form_of_governmentGuinea PigsPlakoglobinCell junctionAdherens junctionLymphatic SystemMicemedicineCell AdhesionAnimalsHumansMolecular BiologyDesmocollinsbiologyDesmoplakinCadherinCell BiologyAnatomyImmunohistochemistryCell biologyRatsLymphatic EndotheliumCytoskeletal ProteinsLymphatic systemmedicine.anatomical_structureIntercellular JunctionsDesmoplakinsMicroscopy Fluorescencebiology.proteingovernmentCattleEndothelium Vasculargamma CateninDesmogleinsCell Adhesion MoleculesDevelopmental BiologyDifferentiation; research in biological diversity
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Synaptophysin expressed in the bronchopulmonary tract: neuroendocrine cells, neuroepithelial bodies, and neuroendocrine neoplasms.

1987

Synaptophysin is an integral membrane glycoprotein with an Mr of 38,000 that occurs in the small, clear vesicles present in neuronal cells and tumors as well as in pancreatic islet cells and various neuroendocrine (NE) carcinomas. We found that synaptophysin is also expressed in normal NE cells of the lungs of newborn rabbits and mice as well as of human fetuses. In bronchial ganglion cells and in nerves, synaptophysin is coexpressed with neurofilament proteins (NFPs), whereas in solitary NE cells and in at least some of the neuroepithelial bodies (NEBs) of the bronchial mucosal lining, synaptophysin coexists with cytokeratins. We also studied a series of NE neoplasms of the lung covering t…

Cancer Researchmedicine.medical_specialtyPathologyLung NeoplasmsCellular differentiationImmunocytochemistrySynaptophysinNeuropeptideFluorescent Antibody TechniqueMiceInternal medicinemedicineAnimalsHumansMolecular BiologyLungImmunoassayLungbiologyDesmoplakinHistocytochemistryMembrane ProteinsCell DifferentiationEpithelial CellsCell BiologyNeurosecretory SystemsGanglionMembrane glycoproteinsEndocrinologymedicine.anatomical_structurenervous systemAnimals NewbornSynaptophysinbiology.proteinKeratinsRabbitsDevelopmental BiologyDifferentiation; research in biological diversity
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TCDD-dependent downregulation of gamma-catenin in rat liver epithelial cells (WB-F344).

2002

TCDD (2,3,7,8-tetrachlorodibenzo-p-dioxin) is the most potent tumor promoter ever tested in rodents. Although it is known that most of the effects of TCDD are mediated by binding to the aryl hydrocarbon receptor (AHR), the mechanisms leading to tumor promotion still remain to be elucidated. Loss of contact-inhibition is a characteristic hallmark in tumorigenesis. In WB-F344 cells, TCDD induces a release from contact-inhibition manifested by a 2- to 3-fold increase in DNA-synthesis and the emergence of foci when TCDD (1 nM) is given to confluent cells. We focussed our interest on potential cell membrane proteins mediating contact-inhibition in WB-F344 cells, namely E-cadherin, alpha,- beta,-…

Cancer Researchmedicine.medical_specialtyPolychlorinated DibenzodioxinsTime FactorsOctoxynolBlotting WesternDetergentsDown-RegulationDownregulation and upregulationInternal medicinemedicineAnimalsFluorescent Antibody Technique IndirectCells Culturedbeta CateninConfluencybiologyReverse Transcriptase Polymerase Chain ReactionLiver NeoplasmsContact inhibitionEpithelial CellsDNAAryl hydrocarbon receptorActin cytoskeletonBlotting NorthernCadherinsCell biologyRatsCytoskeletal ProteinsEndocrinologyPhenotypeOncologyDesmoplakinsLiverMicroscopy FluorescenceCateninMutationbiology.proteinProteasome inhibitorCarcinogensTrans-ActivatorsTumor promotionEnvironmental Pollutantsgamma CateninCell Divisionalpha Cateninmedicine.drugInternational journal of cancer
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In vivo detection of cytokeratin filament network breakdown in cells treated with the phosphatase inhibitor okadaic acid.

2001

We have previously described vulva carcinoma-derived A-431 subclone AK13-1, which stably expresses fluorescently labeled cytokeratin filaments (CKFs). Time-lapse fluorescence microscopy of these cells permits the continuous monitoring of the dynamics of the CKF cytoskeleton in vivo. To study mechanisms and principles of CKF disassembly as it occurs, e.g., during mitosis and liver disease, we have treated cells with the phosphatase inhibitor okadaic acid (OA), which induces complete CKF network breakdown within 3–5 h without significantly affecting the organization of the actin- and tubulin-based cytofilaments. In time-lapse movies, we find that the network breakdown starts at the cell perip…

HistologyTime FactorsRecombinant Fusion ProteinsGreen Fluorescent ProteinsPathology and Forensic Medicinechemistry.chemical_compoundCytokeratinAdenosine TriphosphateStress FibersOkadaic AcidFluorescence microscopeTumor Cells CulturedHumansEnzyme InhibitorsPhosphorylationCytoskeletonMitosisActinCytoskeletonbiologyVulvar NeoplasmsEpithelial CellsCell BiologyOkadaic acidCell biologyCytoskeletal ProteinsLuminescent ProteinsTubulinchemistryDesmoplakinsMicroscopy FluorescenceCytoplasmbiology.proteinKeratinsFemaleIndicators and ReagentsCell and tissue research
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Subcellular Localization of β-Catenin Is Regulated by Cell Density

2002

It is generally accepted that subcellular distribution of beta-catenin regulates its function. Membrane-bound beta-catenin mediates cell-cell adhesion, whereas elevation of the cytoplasmic and nuclear pool of the protein is associated with an oncogenic function. Although the role of beta-catenin in transformed cells is relatively well characterized, little is known about its importance in proliferation and cell-cycle control of nontransformed epithelial cells. Using different approaches we show that in human keratinocytes (HaCaT) beta-catenin is distributed throughout the cells in subconfluent, proliferating cultures. In contrast, beta-catenin is nearly exclusively located at the plasma mem…

KeratinocytesBiophysicsBiologyBiochemistryCell LineHumansFluorescent Antibody Technique IndirectMolecular Biologybeta CateninContact InhibitionCell MembraneContact inhibitionCell BiologyAdhesionCadherinsSubcellular localizationCell biologyCytoskeletal ProteinsKineticsProtein TransportHaCaTMembraneDesmoplakinsCytoplasmCateninTrans-ActivatorsCell DivisionFunction (biology)Biochemical and Biophysical Research Communications
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Cleavage of desmoglein 3 can explain its depletion from keratinocytes in pemphigus vulgaris.

2008

We have previously demonstrated that serum of patients with pemphigus vulgaris induces reduction of desmoglein 3 (Dsg3) half-life in keratinocytes (FEBS Lett 2006: 580: 3276). This phenomenon seems to occur as a consequence of the progressive depletion of Dsg3 from desmosomes. Here we reported that reduction of full-length Dsg3 may be due to its progressive cleavage, leading to the formation of two fragmentation products with apparent molecular masses of about 60 kDa (fragment 1) and 70 kDa (fragment 2), as revealed by Western blotting. Unexpectedly, analysis of fragmentation pattern suggested cleavage to occur intracellularly. Consistently, fragment 1 was shed and localized within the cyto…

KeratinocytesPathologymedicine.medical_specialtyBlotting WesternPlakoglobinDermatologyBiologyCleavage (embryo)BiochemistryCell LinemedicineHumanseducationMolecular Biologyeducation.field_of_studyDesmoglein 3Desmoglein 1Pemphigus vulgarisBlood Proteinsmedicine.diseaseMolecular biologyBlotPemphigusmedicine.anatomical_structureDesmoplakinsDesmoglein 1Desmoglein 3gamma CateninKeratinocytePemphigusExperimental dermatology
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