Search results for "1307 Cell Biology"

showing 10 items of 19 documents

Induction of the peroxisome proliferator activated receptor by fenofibrate in rat liver

1992

AbstractThe process of peroxisome proliferation in rodent liver by hypolipidemic compounds and related substances has recently been shown to be receptor-madiated. In the present study, we have examined the effect of oral administration of the strong peroxisome proliferator fenofibrate on the hepatic expression level of the peroxisome proliferator activated receptor (PPAR) in rats. Immunoblots of rat liver cytosols and nuclear extracs using antibodies raised against recombinant PPAR/β-galactosidase fusion proteins revealed a pronounced increase in the amount of PPAR protein in response to fenofibrate treatment. This induction could also be confirmed at the level or RNA by Northern blotting. …

Male1303 BiochemistryReceptors Cytoplasmic and Nuclear10050 Institute of Pharmacology and ToxicologyPeroxisome proliferator-activated receptorPPARMicrobodiesPolymerase Chain ReactionBiochemistryPPAR agonist1307 Cell BiologyMiceCytosol1315 Structural BiologyFenofibrateStructural Biologychemistry.chemical_classificationMice Inbred BALB CFenofibrateOligodeoxyribonucleotidesPeroxisome proliferator-activated receptor alphaFusion proteinmedicine.drugmedicine.medical_specialtyPeroxisome proliferator-activated receptor gammamRNAMolecular Sequence DataBiophysicsPeroxisome ProliferationReceptors Cell Surface610 Medicine & healthBiology1311 GeneticsInternal medicine1312 Molecular BiologyGeneticsmedicineAnimalsNorthern blotMolecular BiologyAntibodyHypolipidemic compoundCell NucleusMessenger RNABase SequenceImmune SeraCell BiologyBlotting NorthernRatsMice Inbred C57BLEndocrinologychemistry570 Life sciences; biologyTranscription Factors1304 BiophysicsFEBS Letters
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The membrane anchor of microsomal epoxide hydrolase from human, rat, and rabbit displays an unexpected membrane topology.

1997

The microsomal epoxide hydrolase (mEH) and cytochrome P450s catalyze the sequential formation of carcinogenic metabolites. According to one algorithm for predicting the membrane topology of proteins, the human, the rabbit, and the rat mEH should adopt a type II topology. The type II topology is also predicted by a recently established neuronal network which is trained to recognize signal peptides with very high accuracy. In contrast to these predictions we find, based on N-glycosylation analysis in a cell-free and in a cellular system, that the membrane anchor of human, rat, and rabbit mEH displays a type I topology. This result is correctly predicted by the positive inside rule in which ne…

Signal peptide1303 BiochemistryGlycosylationGlycosylationCytochromeStereochemistryRecombinant Fusion ProteinsImmunoblottingMolecular Sequence DataBiophysics10050 Institute of Pharmacology and Toxicology610 Medicine & healthProtein Sorting SignalsTransfectionBiochemistry1307 Cell BiologyCell membranechemistry.chemical_compoundSpecies Specificity1312 Molecular BiologymedicineElectrochemistryAnimalsHumansAmino Acid SequenceMolecular BiologyPeptide sequenceEpoxide HydrolasesbiologyCell MembraneCell BiologyRatsmedicine.anatomical_structurechemistryMutagenesisMicrosomal epoxide hydrolaseMembrane topologyEpoxide HydrolasesCOS Cellsbiology.protein570 Life sciences; biologyRabbits1304 BiophysicsBiochemical and biophysical research communications
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Does dietary salt induce autoimmunity?

2013

Two recent publications suggest that dietary salt may polarize TH17 cells and therefore increase the risk of developing autoimmune disease. Where low salt diets can readily be tested for their therapeutic effects in autoimmune disease, more work is needed to connect dietary salts with the development of immunopathology.

610 Medicine & healthBiology10263 Institute of Experimental Immunologymedicine.disease_causeImmediate early proteinAutoimmunity1307 Cell Biology03 medical and health sciences0302 clinical medicineLow-salt dietsImmunopathology1312 Molecular BiologymedicineMolecular Biology030304 developmental biologyAutoimmune disease0303 health sciencesCell Biologymedicine.diseaseResearch Highlight3. Good healthImmunology570 Life sciences; biologyInterleukin 17030215 immunologyDietary saltCell research
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Isolation and characterization of a cDNA encoding rat liver cytosolic epoxide hydrolase and its functional expression in Escherichia coli.

1993

A cDNA of 1992 base pairs encoding the complete rat liver cytosolic epoxide hydrolase has been isolated using a polymerase chain reaction-derived DNA fragment (Arand, M., Knehr, M., Thomas, H., Zeller, H. D., and Oesch, F. (1991) FEBS Lett. 294, 19-22) known to represent the 3'-end of the cytosolic epoxide hydrolase mRNA. Sequence analysis revealed an open reading frame of 1662 nucleotides corresponding to 554 amino acids (M(r) = 62,268). The DNA sequence obtained did not display significant homology to the sequences of microsomal epoxide hydrolase or leukotriene A4 hydrolase or to any other DNA included in the EMBL Data Bank (release 32). On Northern blotting of rat liver RNA, a single mRN…

Epoxide hydrolase 2Male1303 BiochemistryBase pairMolecular Sequence DataRestriction Mapping10050 Institute of Pharmacology and Toxicology610 Medicine & healthBiologyBiochemistryLeukotriene-A4 hydrolase1307 Cell BiologyRats Sprague-Dawleychemistry.chemical_compoundCytosolFenofibrateComplementary DNA1312 Molecular BiologyEscherichia coliAnimalsAmino Acid SequenceCloning MolecularEpoxide hydrolaseMolecular BiologyPeroxisomal targeting signalEpoxide HydrolasesBase SequenceCell BiologyDNABlotting NorthernMolecular biologyRatschemistryBiochemistryLiverMicrosomal epoxide hydrolase570 Life sciences; biologyDNAThe Journal of biological chemistry
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An impaired peroxisomal targeting sequence leading to an unusual bicompartmental distribution of cytosolic epoxide hydrolase

1991

AbstractTo gain an understanding of the mechanism by which the subcellular distribution of cytosolic epoxide hydrolase (cEH) is directed, we have analyzed the carboxy terminal region of rat liver cEH by means of cDNA cloning to define the structure of its possible peroxisomal targeting sequence (PTS). Purified cEH was subjected to peptide analysis following endoproteinase Glu-C digestion and HPLC-separation of the fragments. The obtained sequence information was used to perform PCR experiments resulting in the isolation of a 680 bp cDNA clone encoding the carboxy terminus of cEH. The deduced amino acid sequence displays a terminal tripeptide Ser-Lys-Ile which is highly homologous to the PTS…

MaleSignal peptidePTSanimal structures1303 BiochemistryMolecular Sequence DataBiophysics10050 Institute of Pharmacology and Toxicology610 Medicine & healthTripeptideProtein Sorting SignalsBiologyMicrobodiesBiochemistryAmino acid sequence1307 Cell BiologyCytosol1315 Structural Biology1311 GeneticsStructural BiologyComplementary DNAGenetics1312 Molecular BiologyAnimalsCloning MolecularEpoxide hydrolaseMolecular BiologyPeptide sequenceEpoxide Hydrolaseschemistry.chemical_classificationBase SequencecDNA sequenceDNACell BiologyPeroxisomeMolecular biologyRatsIsoenzymesCytosolPCREnzymeLiverchemistryBiochemistrycEH570 Life sciences; biologyPeptide analysis1304 Biophysics
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Degradation of phosphatidylethanol counteracts the apparent phospholipase D-mediated formation in heart and other organs.

2003

Phosphatidylalcohols, such as phosphatidylethanol (PEth), are formed from phosphatidylcholine in the presence of a primary alcohol (e.g., ethanol). This 'transphosphatidylation' reaction is used as specific phospholipase D (PLD) assay. Accumulation of PEth in tissues is recognized as a reliable measure of PLD activity, as PEth is allegedly metabolically stable. The general validity of this assumption was reinvestigated in isolated rat heart, small intestine and brain slices. The half-times of 3H-PEth degradation (labelled with 3H-myristic acid and preformed by ethanol exposure for 30 min) were about 1 h in heart and small intestine, but 17 h in brain. As the formation of PEth is superimpose…

Vasodilator AgentsIschemia610 Medicine & healthGlycerophospholipidsTritium1307 Cell BiologyRats Sprague-Dawleychemistry.chemical_compoundIschemiaPhosphatidylcholineIntestine Small1312 Molecular BiologyDiazoxidemedicinePhospholipase DAnimalsMolecular BiologyEthanolPhospholipase DMyocardiumDiazoxideBrainCell Biologymedicine.diseaseSmall intestineRatsPerfusionmedicine.anatomical_structurechemistryBiochemistry10054 Clinic for Psychiatry Psychotherapy and PsychosomaticsIschemic preconditioningPhosphatidylethanolmedicine.drugHalf-LifeBiochimica et biophysica acta
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Myoglobin, expressed in brown adipose tissue of mice, regulates the content and activity of mitochondria and lipid droplets

2021

Abstract The identification of novel physiological regulators that stimulate energy expenditure through brown adipose tissue (BAT) activity in substrate catalysis is of utmost importance to understand and treat metabolic diseases. Myoglobin (MB), known to store or transport oxygen in heart and skeletal muscles, has recently been found to bind fatty acids with physiological constants in its oxygenated form (i.e., MBO2). Here, we investigated the in vivo effect of MB expression on BAT activity. In particular, we studied mitochondrial function and lipid metabolism as essential determinants of energy expenditure in this tissue. We show in a MB-null (MBko) mouse model that MB expression in BAT i…

PalmitatesOxidative phosphorylationMitochondrion1307 Cell BiologyMiceAdipose Tissue BrownLipid dropletBrown adipose tissueRespiration1312 Molecular BiologymedicineAnimalsHumansPPAR alpha11434 Center for Clinical StudiesMuscle SkeletalMolecular BiologyUncoupling Protein 1Mice KnockoutMyoglobinChemistryProteinsThermogenesisLipid metabolismLipid DropletsCell BiologyMetabolism10081 Institute of Veterinary PhysiologyPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaMitochondriaCell biologyOxygenDisease Models AnimalAdipocytes Brownmedicine.anatomical_structure10076 Center for Integrative Human Physiology570 Life sciences; biologyApoptosis Regulatory ProteinsEnergy MetabolismThermogenesisBiochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
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NMR Investigation of Structures of G-Protein Coupled Receptor Folding Intermediates

2016

Folding of G-protein coupled receptors (GPCRs) according to the two-stage model (Popot, J. L., and Engelman, D. M. (1990) Biochemistry 29, 4031-4037) is postulated to proceed in 2 steps: partitioning of the polypeptide into the membrane followed by diffusion until native contacts are formed. Herein we investigate conformational preferences of fragments of the yeast Ste2p receptor using NMR. Constructs comprising the first, the first two, and the first three transmembrane (TM) segments, as well as a construct comprising TM1-TM2 covalently linked to TM7 were examined. We observed that the isolated TM1 does not form a stable helix nor does it integrate well into the micelle. TM1 is significant…

0301 basic medicine10120 Department of ChemistryBioquímicaSaccharomyces cerevisiae Proteins1303 BiochemistryProtein ConformationStereochemistrySaccharomyces cerevisiaeBiochemistryMicelleRessonància magnètica nuclear1307 Cell BiologyG03 medical and health sciencesprotein coupled receptorGPCRProtein Domains540 Chemistry1312 Molecular BiologyAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyMicellesG protein-coupled receptorSequence Homology Amino Acid030102 biochemistry & molecular biologyChemistryProteïnes de membranaFoldingCell BiologyTransloconPeptide FragmentsTransmembrane proteinNMRFolding (chemistry)Crystallography030104 developmental biologyStructural biology10036 Medical ClinicProtein Structure and FoldingReceptors Mating FactorHelixProtein folding
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Colorimetric quantitation of trace amounts of sodium lauryl sulfate in the presence of nucleic acids and proteins

1992

A fast and sensitive procedure for the colorimetric detection of sodium lauryl sulfate (SDS) is presented. The assay is based upon the formation of a chloroform-extractable ion pair between lauryl sulfate and methylene blue that is quantified spectrophotometrically with an estimated detection limit of 150 ng of SDS. The method is suitable for the monitoring of contaminating traces of SDS in protein or nucleic acid samples that have the potential to interfere with enzymatic manipulations such as proteolytic digest, restriction analysis, or reverse transcription. Since the procedure is extremely simple and no special equipment is required it is accessible to every researcher concerned with SD…

1303 BiochemistryTrace AmountsSodiumBiophysicschemistry.chemical_element10050 Institute of Pharmacology and Toxicology610 Medicine & healthBiochemistry1307 Cell Biologychemistry.chemical_compoundNucleic Acids1312 Molecular BiologyAnimalsSulfateColorimetryMolecular BiologyDetection limitChromatographyProteinsSodium Dodecyl SulfateCell BiologyDNAReference StandardsRatsMethylene BluechemistryNucleic acidRNA570 Life sciences; biologyCattleColorimetryQuantitative analysis (chemistry)Methylene blue1304 Biophysics
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Sequence of a novel cytochrome CYP2B cDNA coding for a protein which is expressed in a sebaceous gland, but not in the liver

1992

The major phenobarbital-inducible rat hepatic cytochromes P-450, CYP2B1 and CYP2B2, are the paradigmatic members of a cytochrome P-450 gene subfamily that contains at least seven additional members. Specific oligonucleotide probes for these genomic members of the CYP2B subfamily were used to assess their tissue-specific expression. In Northern-blot analysis a probe specific to gene 4 (which is designated now as CYP2B12) hybridized to a single mRNA present in the preputial gland, an organ which is used as a model for sebaceous glands, but did not hybridize to mRNA isolated from the liver or from five other tissues of untreated or Aroclor 1254-treated rats. The cDNA sequence for the CYP2B12 R…

MaleSubfamily1303 BiochemistryMolecular Sequence Data10050 Institute of Pharmacology and Toxicology610 Medicine & healthBiologyBiochemistryRats Sprague-Dawley1307 Cell BiologySebaceous GlandsRapid amplification of cDNA endsCytochrome P-450 Enzyme SystemComplementary DNAMicrosomes1312 Molecular BiologyCoding regionAnimalsAmino Acid SequenceMolecular BiologyBase SequencecDNA librarySingle-Strand Specific DNA and RNA EndonucleasesProtein primary structureNucleic acid sequenceCell BiologyDNARibonuclease PancreaticBlotting NorthernMolecular biologyRatsOpen reading frameBiochemistryLiverMultigene FamilyMicrosomes Liver570 Life sciences; biologyFemaleOligonucleotide ProbesResearch Article
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