Search results for "Membrane Transport"

showing 10 items of 215 documents

Long-Term Potentiation in the Neonatal Rat Barrel Cortex In Vivo

2012

Long-term potentiation (LTP) is important for the activity-dependent formation of early cortical circuits. In the neonatal rodent barrel cortex, LTP has been studied only in vitro . We combined voltage-sensitive dye imaging with extracellular multielectrode recordings to study whisker stimulation-induced LTP in the whisker-to-barrel cortex pathway of the neonatal rat barrel cortex in vivo . Single whisker stimulation at 2 Hz for 10 min induced an age-dependent expression of LTP in postnatal day (P) 0 to P14 rats, with the strongest expression of LTP at P3–P5. The magnitude of LTP was largest in the activated barrel-related column, smaller in the surrounding septal region, and no LTP could b…

animal structuresPatch-Clamp TechniquesLong-Term PotentiationBiophysicsStimulationBiologyIn Vitro TechniquesStatistics NonparametricIn vivoCortex (anatomy)Evoked Potentials SomatosensoryExtracellularmedicineAnimalsNeuronsSerotonin Plasma Membrane Transport ProteinsCortical circuitsNeonatal ratAfferent PathwaysGeneral Neurosciencemusculoskeletal neural and ocular physiologyAge FactorsLong-term potentiationSomatosensory CortexBarrel cortexElectric StimulationVoltage-Sensitive Dye ImagingRatsmedicine.anatomical_structurenervous systemAnimals NewbornVibrissaeBiophysicsBrief CommunicationsNeuroscience
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Membrane transport in the endocytic pathway: Animal versus plant cells

2000

The endocytic pathway is a well established process in animal cells, but it is not well understood in plant cells. At the morphological level, all the compartments involved in endocytosis in animal cells seem to have counterparts in plant cells, and the organization of the pathway appears to share some striking similarities. Several Rab homologues have been found in plant cells, including homologues of Rab5, Rab7, and Rab11, markers of endocytic compartments in animal cells. Coat proteins are also present in plant cells, including clathrin, adaptins, and ADP ribosylation factor proteins. However, endocytic compartments in plant cells also exhibit specific features both in organization and f…

biologyADP ribosylation factorfungiEndocytic cyclefood and beveragesCell BiologyPlant ScienceGeneral MedicineMembrane transportPlant cellEndocytosisClathrinCell biologyBiochemistrybiology.proteinRabFunction (biology)Protoplasma
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Kinetic Characterization of Secretory Transport of a New Ciprofloxacin Derivative (CNV97100) across Caco-2 Cell Monolayers**This work has been submit…

2002

The kinetics of transport of a new fluoroquinolone antibiotic (CNV97100) and its analogs were characterized using the Caco-2 cell culture model. Unidirectional permeabilities of these analogs were greater (p < 0.05) than that of ciprofloxacin. The absorptive permeabilities (P(AB)) of 4'-N-substituted analogs (CNV97101-104) were 400-600% greater, whereas the secretory permeability (P(BA)) was 25-80% greater than unsubstituted analogs because CNV97101-104 were poor substrates for efflux transporters (efflux ratio approximately 1). The transport of compounds without 4'-N-substitution (i.e., ciprofloxacin and CNV97100) favored secretion (efflux ratio approximately 4). Further characterization o…

biologyLeukotriene C4ChemistryStereochemistryPharmaceutical ScienceMembrane transportMolecular biologychemistry.chemical_compoundCaco-2Cyclosporin amedicinebiology.proteinVerapamilEffluxAntibacterial agentmedicine.drugP-glycoproteinJournal of Pharmaceutical Sciences
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[9] Identification of carrier systems in plasma membranes of mammalian cells involved in transport of l-arginine

1999

Publisher Summary This chapter describes the transport systems and the corresponding carrier proteins involved in the L-arginine transport that have been described till date. The chapter also discusses the methods that have been used to characterize L-arginine transport in nitric oxide (NO) producing cells or tissues. L-arginine transport is mediated by multiple carrier systems, some of which have not yet been identified at a molecular level. It is conceivable that a modification of a carrier or an associated protein could alter its transport activity, resulting in the appearance of a carrier with altered transport characteristics. Considerable progress has been made in identifying cationic…

biologyMembrane transport proteinCaveolaeExtracellularbiology.proteinCompartmentalization (psychology)Membrane transportEndothelial NOSIntracellularTransport proteinCell biology
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Transport, stability, and biological activity of resveratrol

2011

Numerous studies have reported interesting properties of trans-resveratrol, a phytoalexin, as a preventive agent of several important pathologies: vascular diseases, cancers, viral infections, and neurodegenerative processes. These beneficial effects of resveratrol have been supported by observations at the cellular and molecular levels in both cellular and in vivo models, but the cellular fate of resveratrol remains unclear. We suggest here that resveratrol uptake, metabolism, and stability of the parent molecule could influence the biological effects of resveratrol. It appears that resveratrol stability involves redox reactions and biotransformation that influence its antioxidant properti…

chemistry.chemical_classificationAntioxidantendocrine system diseasesMembrane transport proteinorganic chemicalsGeneral NeurosciencePhytoalexinmedicine.medical_treatmentfood and beveragesBiological activityMetabolismBiologyResveratrolGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundHistory and Philosophy of SciencechemistryBiotransformationBiochemistryIn vivobiology.proteinmedicineskin and connective tissue diseaseshormones hormone substitutes and hormone antagonistsAnnals of the New York Academy of Sciences
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Membrane Transport of l-Arginine and Cationic Amino Acid Analogs

2000

Publisher Summary This chapter reviews the current knowledge of the mechanisms and regulation of cationic amino acids (CAA) carrier proteins and discusses the potential involvement of each transporter in supplying L-arginine for nitric oxide biosynthesis. The CAA L-arginine, the substrate for nitric oxide synthases (NOSs), is considered a semi-essential amino acid in most mammals. Consequently, mammalian cells must be capable of exchanging CAA with the environment. The bilayer of the plasma membrane is impermeable to polar molecules, and thus, specialized carrier proteins with distinct substrate specificity transport hydrophilic solutes such as amino acids. L-arginine shares the same transp…

chemistry.chemical_classificationArginineChemistryCationic polymerizationnutritional and metabolic diseasesSubstrate (chemistry)TransporterMembrane transportAmino acidNitric oxidechemistry.chemical_compoundMembraneBiochemistrymental disorderscardiovascular diseases
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CATs, a family of three distinct mammalian cationic amino acid transporters

1996

Three related mammalian carrier proteins that mediate the transport of cationic amino acids through the plasma membrane have been identified in murine and human cells (CAT for cationic amino acid transporter). Models of the CAT proteins in the membrane suggest they have 12 or 14 transmembrane domains connected by short hydrophilic loops and intracellular N- and C-termini. The transport activity of the CAT proteins is sensitive to trans-stimulation and independent of the presence of sodium ions. These features agree with the behaviour of carrier proteins mediating facilitated diffusion. The three CAT proteins, CAT-1, CAT-2A and CAT-2(B) are encoded by two different genes (CAT-1 and CAT-2). C…

chemistry.chemical_classificationFacilitated diffusionOrganic ChemistryClinical BiochemistryMembrane transportBiologyBiochemistryTransport proteinAmino acidTransmembrane domainchemistryBiochemistryAmino acid transporterReceptorIntracellularAmino Acids
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Comparative analysis of the coordinated motion of Hsp70s from different organelles observed by single-molecule three-color FRET.

2021

Cellular function depends on the correct folding of proteins inside the cell. Heat-shock proteins 70 (Hsp70s), being among the first molecular chaperones binding to nascently translated proteins, aid in protein folding and transport. They undergo large, coordinated intra- and interdomain structural rearrangements mediated by allosteric interactions. Here, we applied a three-color single-molecule Forster resonance energy transfer (FRET) combined with three-color photon distribution analysis to compare the conformational cycle of the Hsp70 chaperones DnaK, Ssc1, and BiP. By capturing three distances simultaneously, we can identify coordinated structural changes during the functional cycle. Be…

chemistry.chemical_classificationOrganellesMultidisciplinarySaccharomyces cerevisiae ProteinsAllosteric regulationPeptideSaccharomyces cerevisiaeBiological SciencesMitochondrial Membrane Transport ProteinsRecombinant ProteinsSingle Molecule ImagingFolding (chemistry)Förster resonance energy transferchemistryHeat shock proteinBiophysicsEscherichia coliFluorescence Resonance Energy TransferMoleculeProtein foldingNucleotideHSP70 Heat-Shock ProteinsMolecular ChaperonesProceedings of the National Academy of Sciences of the United States of America
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Proton-dependent kinetics of citrate uptake in growing cells ofLactococcus lactissubsp.lactisbv.diacetylactis

1995

The kinetic analysis of citrate uptake in growing cells of Lactococcus lactis subsp. lactis biovar. diacetylactis identified a proton-dependent transport and suggested the divalent anionic species as the form of citrate transported across cell membranes. The reaction followed Michaelis-Menten kinetics for a two-substrate reaction. The limiting steps were the formation of the ternary complex and the rate of transport. Temperature modified the activity of the permease, increasing the uptake rate.

chemistry.chemical_classificationPermeaseKineticsLactococcus lactisCitrate transportBiologyMembrane transportbiology.organism_classificationStreptococcaceaeMicrobiologyDivalentchemistryBiochemistryGeneticsMolecular BiologyTernary complexFEMS Microbiology Letters
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Role of P‐glycoprotein‐mediated secretion in absorptive drug permeabiity: An approach using passive membrane permeability and affinity to P‐glycoprot…

1999

Abstract It has been shown in vivo and in vitro that P‐glycoprotein (P‐gp) may be able to influence the permeability of its substrates across biological membranes. However, the quantitative contribution of the secretion process mediated by P‐gp on the overall permeability of membranes has not been determined yet. In particular, observations need to be clarified in which substrates showing high affinity to P‐glycoprotein, e.g., verapamil, apparently do not seem to be greatly influenced by P‐gp in their permeability and consequently also with respect to their extent of GI‐absorption after oral administration, whereas weaker substrates of P‐gp, e.g., talinolol, have clearly shown P‐gp‐related …

chemistry.chemical_compoundMembraneChromatographyMembrane permeabilityPassive transportChemistryPermeability (electromagnetism)BiophysicsPharmaceutical ScienceBiological membranePermeationMembrane transportTalinololJournal of Pharmaceutical Sciences
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