Search results for "ENDOPLASMIC RETICULUM"

showing 10 items of 306 documents

Interaction between mesenchymal cells and the posterior iris epithelium in chicken embryos

1977

The iris anlage of 3--10 day old chicken embryos was studied by both light and electron microscopy. Serial semithin sections showed that some of the mesenchymal cells overlying the eye cup moved into the primitive eye cavity by the 3rd day of incubation. On the 4th day some of these cells came into close contact with the basement membrane of the dorsal iris epithelium. The bases of the epithelial cells were flat at this stage. Towards the 10th day they formed cytoplasmic processes which did not penetrate the basement membrane. Fine mesenchymal cytoplasmic processes and a large number of extracellular fibrils developed in the epithelial--mesenchymal interface. The fine mesenchymal processes …

EmbryologyTime FactorsIrisChick EmbryoBiologyEndoplasmic ReticulumFibrilBasement MembraneEpitheliumlaw.inventionMesodermCell MovementlawmedicineAnimalsIris (anatomy)Basement membraneEndoplasmic reticulumMesenchymal stem cellCell DifferentiationCell BiologyAnatomyEpitheliumMicroscopy Electronmedicine.anatomical_structureCytoplasmAnatomyElectron microscopeDevelopmental BiologyAnatomy and Embryology
researchProduct

Ultrastructure of the sternal glands inThrips validus uzel (Thysanoptera, terebrantia)

1978

The ultrastructure of the sternal glands of the males ofThrips validus is consistent with the hypothesis that they are involved in pheromone production. The secretory cells, which are strongly modified epidermal cells, are characterized by the abundance of mitochondria and the presence of agranular, tubular endoplasmic reticulum (ATER) and microbodies. Each of the numerous apical microvilli encloses one or several tubular extensions of ATER. Some mitochondria are in close contact with ATER tubules. The mitochondrial matrix is probably involved in the elaboration of the secretory product, which is extruded and possibly modified by the agranular reticulum. The secretion is sudanophilic, but n…

Endoplasmic reticulumAnatomyMitochondrionBiologyCell biologyCytoplasmLipid dropletUltrastructureMicrobodyAnimal Science and ZoologySecretionAnatomyReticulumDevelopmental BiologyZoomorphologie
researchProduct

Dual Topology of the Hepatitis B Virus Large Envelope Protein

2001

The large (L) envelope protein of the hepatitis B virus (HBV) has the peculiar capacity to form two transmembrane topologies via an as yet uncharacterized process of partial post-translational translocation of its pre-S domain across membranes. In view of a current model that predicts an HBV-specific channel generated during virion envelope assembly to enable pre-S translocation, we have examined parameters influencing L topogenesis by using protease protection analysis of wild-type and mutant L proteins synthesized in transfected cells. We demonstrate that contrary to expectation, all determinants, thought to be responsible for channel formation, are dispensable for pre-S reorientation. In…

Endoplasmic reticulumCell BiologyBiologyMembrane transportTransloconBiochemistryTransmembrane proteinTransport proteinCell biologyTransmembrane domainDual topologyProtein structureBiochemistryMolecular BiologyJournal of Biological Chemistry
researchProduct

Chitosomes lack concanavalin-A-binding sites

1985

Whether intact or dissociated with digitonin, chitosomes isolated from the fungusMucor rouxii lack the ability to bind concanavalin A. The absence of external or internal concanavalin A-binding sites distinguishes the chitosome membrane no only from plasma membrane but also from membranes of other organelles (endoplasmic reticulum, mitochondrion, vacuole). This differential binding ability was used to partially separate chitosomal chitin synthetase from major membranes in a crude cell-free extract ofM. rouxii.

Endoplasmic reticulumGeneral MedicineVacuoleBiologyApplied Microbiology and BiotechnologyMicrobiologychemistry.chemical_compoundMembraneDigitoninBiochemistrychemistryConcanavalin AOrganellebiology.proteinBinding siteChitosome membraneCurrent Microbiology
researchProduct

Gibberellic acid stimulates lipid metabolism in barley aleurone protoplasts

1991

Abstract Changes in the lipid composition of barley aleurone protoplasts following incubation in the presence or absence of gibberellic acid (GA) were studied and correlated with cell development. Analysis of neutral lipids in protoplast extracts and purified lipid bodies provide evidence for the strong effect of GA on the mobilization of storage lipids. In vivo protoplast staining with the membrane marker N -phenyl-l-naphthylamine (NPN) and phospholipid determinations of protoplast extracts show an increase in membrane lipids during protoplast incubation. GA stimulates phospholipid metabolism by increasing the synthesis of phosphatidyl ethanolamine and phosphatidyl choline, the major phosp…

Endoplasmic reticulumMembrane lipidsfungiPhospholipidfood and beveragesLipid metabolismPlant ScienceGeneral Medicinebiochemical phenomena metabolism and nutritionBiologyProtoplastchemistry.chemical_compoundBiochemistrychemistryAleuroneGeneticsbacterialipids (amino acids peptides and proteins)Hordeum vulgareAgronomy and Crop ScienceGibberellic acidPlant Science
researchProduct

Effects of Ga3 and Ca2+ on barley aleurone protoplasts: a freeze-fracture study

1988

Freeze-fracture electron microscopy was used to study changes in the endomembrane system of barley (Hordeum vulgare L. cv. Himalaya) aleurone protoplasts. Protoplasts were used for this study because their response to calcium and the plant hormone gibberellic acid (Ga3) can be monitored prior to rapid freezing of cells for electron microscopy. Protoplasts incubated in Ga3 plus Ca2+ secrete elevated levels of a-amylase relative to cells incubated in Ga3 or Ca2+ alone. The endoplasmic reticulum (ER) and Golgi apparatus of protoplasts incubated in Ga3 plus Ca2+ undergo changes that are well correlated with the synthesis and secretion of a-amylase. The ER, which appears as short, single sheets …

Endoplasmic reticulumfungifood and beveragesCell BiologyPlant ScienceGeneral Medicinebiochemical phenomena metabolism and nutritionGolgi apparatusBiologyCell biologysymbols.namesakeBiochemistryAleuroneOrganelleGolgi cisternasymbolsSecretionEndomembrane systemHordeum vulgareProtoplasma
researchProduct

Lipase maturation factor 1 is required for endothelial lipase activity

2011

Lipase maturation factor 1 (Lmf1) is an endoplasmic reticulum (ER) membrane protein involved in the posttranslational folding and/or assembly of lipoprotein lipase (LPL) and hepatic lipase (HL) into active enzymes. Mutations in Lmf1 are associated with diminished LPL and HL activities ("combined lipase deficiency") and result in severe hypertriglyceridemia in mice as well as in human subjects. Here, we investigate whether endothelial lipase (EL) also requires Lmf1 to attain enzymatic activity. We demonstrate that cells harboring a (cld) loss-of-function mutation in the Lmf1 gene are unable to generate active EL, but they regain this capacity after reconstitution with the Lmf1 wild type. Fur…

Endothelial lipaseSettore MED/09 - Medicina InternaCombined Lipase DeficiencyQD415-436PhospholipaseTransfectionBiochemistryChromatography Affinityphospholipasescombined lipase deficiencyMiceEndocrinologyAnimalsHumansWithdrawals/RetractionsLipaseResearch ArticlesHypertriglyceridemiaLipoprotein lipasecombined lipase deficiency; endoplasmic reticulum; hepatic; metabolism; phospholipasesbiologyEndoplasmic reticulumWild typeMembrane ProteinsLipaseCell BiologyFibroblastsMolecular biologyLipoprotein Lipaseendoplasmic reticulumElectroporationHEK293 CellsMutationbiology.proteinHepatic lipasehepaticmetabolismPlasmidscombined lipase deficiencyJournal of Lipid Research
researchProduct

High levels of the molecular chaperone Mdg1/ERdj4 reflect the activation state of endothelial cells

2003

Mdg1/ERdj4, a mammalian chaperone that belongs to the HSP40 protein family, has been reported to be located in the endoplasmic reticulum (ER), is induced by ER stress, and protects ER stressed cells from apoptosis. Here we show that under normal physiological conditions, Mdg1/ERdj4 is expressed at various levels in the vasculature due to different activation states of the endothelium. To elucidate the stimuli that induce ER stress and thus upregulate Mdg1/ERdj4, we investigated the effect of several endothelium specific stressors on its expression. Mdg1/ERdj4 mRNA is induced by activated macrophages, by nitric oxide (NO) and heat shock, and during terminal cell differentiation, whereas shea…

EndotheliumCell SurvivalCellular differentiationApoptosisCell CommunicationEndoplasmic ReticulumNitric OxideMiceStress PhysiologicalmedicineAnimalsHumansRNA MessengerHeat shockEndoplasmic Reticulum Chaperone BiPbiologyMacrophagesEndoplasmic reticulumMembrane ProteinsProteinsCell BiologyHSP40 Heat-Shock ProteinsCoculture TechniquesUp-RegulationHsp70Cell biologyProtein Transportmedicine.anatomical_structureApoptosisChaperone (protein)biology.proteinUnfolded protein responseEndothelium VascularStress MechanicalCarrier ProteinsCell NucleolusHeat-Shock ResponseHeLa CellsMolecular ChaperonesExperimental Cell Research
researchProduct

Evidence for Several Hepatic Proteins Related to Microsomal Epoxide Hydrolase

1989

Epoxide hydrolases catalyze the conversion of epoxides, some of which have been shown to be carcinogenic, to dihydrodiols (Guenthner and Oesch 1981). At least three forms of epoxide hydrolases exist in rats, two of which, namely mEHb and mEHch, are associated mainly with the microsomal fraction (Oesch et al 1984; Levin et al 1983) whereas one form namely cEH is found to a large extent in the cytosolic fraction (Gill and Hammock 1981). These three forms differ in their immunological and catalytic properties quite considerably (Guenthner et al 1981). In the case of mEHb the existence of several closely related isoenzymes with an identical apparent subunit molecular weight (Mrs) of 50,000 was …

Epoxide hydrolase 2Epoxide hydrolase activityEndoplasmic reticulum membraneBiochemistryChemistryEndoplasmic reticulumMicrosomal epoxide hydrolaseEpoxide HydrolasesMicrosomeEpoxide hydrolase
researchProduct

The transmembrane Bax inhibitor motif (TMBIM) containing protein family: Tissue expression, intracellular localization and effects on the ER CA2+-fil…

2015

Abstract Bax inhibitor-1 (BI-1) is an evolutionarily conserved pH-dependent Ca2+ leak channel in the endoplasmic reticulum and the founding member of a family of six highly hydrophobic mammalian proteins named transmembrane BAX inhibitor motif containing (TMBIM) 1-6 with BI-1 being TMBIM6. Here we compared the structure, subcellular localization, tissue expression and the effect on the cellular Ca2+ homeostasis of all family members side by side. We found that all TMBIM proteins possess the di-aspartyl pH sensor responsible for pH sensing identified in TMBIM6 and its bacterial homologue BsYetJ. TMBIM1-3 and TMBIM4-6 represent two phylogenetically distinct groups that are localized in the Go…

GHITMGAAPProtein familyEndoplasmic reticulumCell BiologyBiologyGolgi apparatusSubcellular localizationFAIM2Transmembrane proteinGHITMCell biologyTransmembrane domainsymbols.namesakeMICS1BiochemistryMembrane proteinGRINAsymbolsRECS1Molecular BiologyBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
researchProduct