Search results for "Apical membrane"

showing 7 items of 17 documents

Characterization of the Apical Membrane Antigen-1 in Italian Strains of Babesia bigemina

2010

Summary Babesia bigemina is a parasite endemic in different parts of the world, including Europe and the Americas. One of the few genes characterized in this species codifies for the Apical Membrane Antigen 1 (AMA-1), a trans-membrane antigen recently identified. In this research, we characterized the ama-1 gene from three Italian B. bigemina strains, two B. bigemina strains obtained from Ragusa, Sicily (ITA1 and ITA3) and a third one obtained from Benevento, Campania (ITA2). Italian sequences were compared with those of the Australian strain obtained from the Sanger Institute web site and to strains from different parts of the world. The results obtained confirmed that this newly described…

General VeterinaryGeneral Immunology and MicrobiologyAntigenStrain (biology)Parasite hostingGeneral MedicineApical membrane antigen 1BiologyVirologyGeneBabesia bigeminaMicrobiologyWeb siteTransboundary and Emerging Diseases
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Histochemical localization of calcium ATPase in the cochlea of the guinea pig

1992

The activity of Ca(2+)-ATPase in the inner ear of the guinea pig was studied ultracytochemically by the lead citrate reaction. The electron-dense reaction products as an expression of Ca(2+)-ATPase activity were localized in endolymphatic cells of Reissner's membrane, in outer and inner hair cells and in some supporting cells. The main finding was the difference in the localization of Ca(2+)-ATPase in outer and inner hair cells. In the latter cells the activity sites were mainly intracellular and in apical membrane specializations, whereas in the outer hair cells the enzyme was localized in the apical membrane specializations and the basolateral plasma membrane.

MaleATPaseGuinea PigsCalcium-Transporting ATPasesGuinea pigEndolymphHair Cells AuditorymedicineAnimalsInner earOrgan of CortiCochleabiologyHistocytochemistryGeneral MedicineBasolateral plasma membraneApical membraneCochleaCalcium ATPasemedicine.anatomical_structureOtorhinolaryngologyBiochemistryBiophysicsbiology.proteinFemaleCalcium Channelssense organsIntracellularEuropean Archives of Oto-Rhino-Laryngology
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Lactaturia and loss of sodium-dependent lactate uptake in the colon of SLC5A8-deficient mice.

2008

SLC5A8 is a member of the sodium/glucose cotransporter family. It has been proposed that SLC5A8 might act as an apical iodide transporter in the thyroid follicular cells or as a transporter of short chain monocarboxylates. We have directly addressed the functional role of SLC5A8 in vivo by generation of SLC5A8 mutant mice. We found that SLC5A8 is responsible for the re-absorption of lactate at the apical membrane of the kidney proximal tubules and of serous salivary gland ducts. In addition, SLC5A8 mediated the uptake of lactate into colonocytes under physiological conditions. We did not find any evidence of SLC5A8 being essential for the apical iodide transport in the thyroid gland, even i…

Monocarboxylic Acid Transportersmedicine.medical_specialtyColonButyrateBiologyBiochemistryIntestinal absorptionMiceInternal medicinemedicineAnimalsIodide transportLactic AcidMolecular BiologyCation Transport ProteinsMice KnockoutThyroidSodiumTransporterCell BiologyNeoplasms ExperimentalApical membraneTransport proteinButyratesMembrane Transport Structure Function and BiogenesisEndocrinologymedicine.anatomical_structureCell Transformation NeoplasticIntestinal AbsorptionCarcinogensKidney DiseasesCotransporterThe Journal of biological chemistry
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OCTN2-Mediated Carnitine Uptake in a Newly Discovered Human Proximal Tubule Cell Line (Caki-1)

2006

The proximal tubular reabsorption of carnitine in the human kidney is significant because more than 95% of the carnitine filtered in the kidney is reabsorbed by the proximal tubules therefore maintaining the homeostatic balance of carnitine in the body. Objectives of this study include the characterization of OCTN2 function in the Caki-1 cell line and the potential interactions of carnitine uptake with renally secreted drugs, including drugs of quaternary ammonium structure. Caki-1 cells were additionally characterized to be of proximal tubule nature, and an apical membrane expression pattern of OCTN2 in Caki-1 cells was discovered. Uptake studies with radiolabeled L-carnitine in Caki-1 cel…

Organic Cation Transport ProteinsFluorescent Antibody TechniquePharmaceutical SciencePharmacologyKidney Tubules Proximalchemistry.chemical_compoundCarnitineDrug DiscoverymedicineHumansSecretionAmmoniumCarnitineSolute Carrier Family 22 Member 5KidneyChemistrySodiumTemperatureBiological TransportHydrogen-Ion ConcentrationApical membraneCadherinsmedicine.anatomical_structureGene Expression RegulationPharmaceutical PreparationsCell cultureRenal physiologyMolecular MedicineHomeostasismedicine.drugMolecular Pharmaceutics
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IRSp53 shapes the plasma membrane and controls polarized transport at the nascent lumen during epithelial morphogenesis

2019

AbstractEstablishment of apical–basal cell polarity is necessary for generation of luminal and tubular structures during epithelial morphogenesis. Molecules acting at the membrane/ actin interface are expected to be crucial in governing these processes. Here, we show that the I-BAR-containing IRSp53 protein is restricted to the luminal side of epithelial cells of various glandular organs, and is specifically enriched in renal tubules in human, mice, and zebrafish. Using three-dimensional cultures of renal MDCK and intestinal Caco-2 cysts, we show that IRSp53 is recruited early after the first cell division along the forming apical lumen, and is essential for formation of a single lumen and …

Settore MED/04 - Patologia GeneraleCell divisionbiologyChemistryCytoplasmCell polarityMorphogenesisApical membranebiology.organism_classificationZebrafishActinLumen (unit)Cell biology
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Follicle Cells of Styela plicata Eggs (Ascidiacea)

2001

Styela plicata eggs are surrounded by large follicle cells that at LM appear as highly vacuolated and columnar in shape; at the apical end of each cell lies a very large and clear vacuole, half of which extends inward. Electron microscope observations show a Single layer of largely spaced box-like follicle cells; the close cell-cell contact at their base is realized by interdigitations. The cell surface shows a peculiar structure, more developed in the latero-basal regions, consisting of a complex of membrane extensions, i.e. microvilli, filopodia and lamellipodia. Filopodia irradiate in all directions towards the adjacent cells and the outermost vitelline coat, thus creating a complex netw…

biologyChemistryVacuoleApical membranebiology.organism_classificationlaw.inventionCell biologyFollicleStyela plicatalawSecretionElectron microscopeLamellipodiumFilopodia
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The Follicle Cells of Styela Plicata (Ascidiacea, Tunicata): A Sem Study

2000

The morphological aspect of the follicle cells of Styela plicata eggs is described by means of scanning electron microscope investigations. The follicular layer is made of spaced, cylindrical box-like cells which are arranged hexagonally. They adhere to the egg through a complex network of membrane extensions making an overall thin layer on the vitelline coat. The walls of the follicle cells are plentifully provided with microvilli, filopodia and lamellipodia, which allow a connection among the cells. At their apical end lies a large vacuole containing a granule, probably involved in secretion. At insemination the majority of spermatozoa is distributed on the apical membrane of the follicle…

biologyGranule (cell biology)VacuoleAnatomyApical membranebiology.organism_classificationCell biologyFollicleStyela plicataembryonic structuresAnimal Science and ZoologyLamellipodiumFilopodiaAscidiaceaZoological Science
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