Search results for "leucine"

showing 10 items of 191 documents

Impact of nutritional status on the oral bioavailability of leucine administered to rats as part of a standard enteral diet.

2010

Summary Background To investigate the absorption and relative bioavailability of leucine administered orally as part of an enteral diet in well and malnourished animals. Methods Two groups – RN (regular nutrition) and PCR (protein-calorie restricted) – were fed with different diets for 23–25 days. Rats from each group were assigned randomly to one of three treatments (water, T-Diet Plus Standard ® (problem) or Isosource ST ® (reference)) administered in single ( N  = 76) or multiple ( N  = 39) doses. Blood samples were assayed for leucine content. Area under the curve (AUC) was calculated by non-compartmental analysis. Log-transformed AUC(s) were statistically compared by analysis of varian…

MaleAdministration OralBiological AvailabilityNutritional StatusCritical Care and Intensive Care MedicineMultiple dosingEnteral administrationAbsorptionAnimal scienceEnteral NutritionLeucineDiet Protein-RestrictedMedicineAnimalsFood scienceRats WistarNutrition and DieteticsDose-Response Relationship Drugbusiness.industryArea under the curveNutritional statusConfidence intervalBioavailabilityDietRatsArea Under CurveAnalysis of varianceLeucinebusinessEnergy IntakeClinical nutrition (Edinburgh, Scotland)
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Elevation of hepatic epoxide hydratase activity by ethoxyquin is due to increased synthesis of the enzyme.

1980

Abstract Feeding of the antioxidant ethoxyquin to rats leads to an increase of epoxide hydratase activity in liver microsomes. The apparent half life of the increase is 3–4 days. Elevation of epoxide hydratase activity is also obtained by intraperitoneal treatment of mice with ethoxyquin. This elevation is prevented by concomitant treatment with cycloheximide. When radiolabelled leucine is incorporated into microsomal protein by liver cell fractions from either ethoxyquin-fed or untreated rats, gel electrophoresis reveals that ethoxyquin feeding increases incorporation into epoxide hydratase. These results suggest that the elevation of epoxide hydratase activity by ethoxyquin is due to incr…

MaleAntioxidantmedicine.medical_treatmentBiophysicsCycloheximideBiochemistrySubstrate Specificitychemistry.chemical_compoundEthoxyquinmedicineAnimalsEnzyme inducerBenzopyrenesCycloheximideMolecular Biologychemistry.chemical_classificationEpoxide HydrolasesEthoxyquinbiologyLiver cellCell BiologyRatsEnzymechemistryBiochemistryEnzyme Inductionbiology.proteinMicrosomeMicrosomes LiverQuinolinesLeucineBiochemical and biophysical research communications
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Activation of L-arginine transport by protein kinase C in rabbit, rat and mouse alveolar macrophages

1998

1 The role of protein kinase C in controlling L-arginine transport in alveolar macrophages was investigated. 2 L-[3H]Arginine uptake in rabbit alveolar macrophages declined by 80 % after 20 h in culture. 4β-Phorbol 12-myristate 13-acetate (PMA), but not 4α-phorbol 12-myristate 13-acetate (α-PMA), present during 20 h culture, enhanced L-[3H]arginine uptake more than 10-fold. Staurosporine and chelerythrine opposed this effect. 3 L-[3H]Arginine uptake was saturable and blockable by L-lysine. After PMA treatment Vmax was increased more than 5-fold and Km was reduced from 0.65 to 0.32 mM. 4 Time course experiments showed that PMA increased L-[3H]arginine uptake almost maximally within 2 h. This…

MaleArgininePhysiologyMice Inbred StrainsStimulationCycloheximideArginineTritiumL-arginine transportRats Sprague-DawleyMicechemistry.chemical_compoundSpecies SpecificityLeucineMacrophages AlveolarmedicineAnimalsStaurosporineRNA MessengerEnzyme InhibitorsProtein Kinase CProtein kinase CbiologySodiumMembrane ProteinsBiological TransportRabbit ratOriginal Articlesbiology.organism_classificationMolecular biologyRatsKineticsChelerythrinechemistryEthylmaleimideCarcinogensAmino Acid Transport Systems BasicTetradecanoylphorbol AcetateFemaleRabbitsCarrier Proteinsmedicine.drugThe Journal of Physiology
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Evolution of chromatin-remodeling complexes: comparative genomics reveals the ancient origin of "novel" compensasome genes.

2003

Dosage compensation in Drosophila is mediated by a complex, called compensasome, com- posed of at least five proteins and two noncoding RNAs. Genes encoding compensasome proteins have been collectively named male-specific lethals or msls. Recent work showed that three of the Drosophila msls (msl-3, mof, and mle) have an ancient origin. In this study, I describe likely orthologues of the two re- maining msls, msl-1 and msl-2, in several inverte- brates and vertebrates. The MSL-2 protein is the only one found in Drosophila and vertebrate genomes that contains both a RING finger and a peculiar type of CXC domain, related to the one present in Enhancer of Zeste proteins. MSL-1 also contains two…

MaleLeucine zipperAmino Acid MotifsMolecular Sequence DataBiologyGenomeChromatin remodelingEvolution MolecularDosage Compensation GeneticGeneticsRing fingermedicineAnimalsDrosophila ProteinsHumansAmino Acid SequenceEnhancerMolecular BiologyEcology Evolution Behavior and SystematicsCaenorhabditis elegansPhylogenyComparative genomicsGeneticsDosage compensationfungiNuclear ProteinsGenomicsbiology.organism_classificationChromatin Assembly and DisassemblyProtein Structure TertiaryDNA-Binding Proteinsmedicine.anatomical_structureVertebratesDrosophilaSequence AlignmentTranscription FactorsJournal of molecular evolution
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RADHA - a new male germ line-specific chromosomal protein of Drosophila

1999

A new chromosomal protein - RADHA - of Drosophila is described that is specific for the male germ line. It is encoded by a single-copy gene, located in the region 96C-D of D. melanogaster polytene chromosomes. Transcription of the radha gene is restricted to the primary spermatocyte stage. The protein initially accumulates in some of the Y-chromosomal lampbrush loops. After meiosis it is found in the nuclei of spermatids and might be involved in chromatin rearrangement processes in the male germ line. RADHA is a basic protein with a C-terminal leucine zipper region and several segments capable of forming coiled-coil structures.

MaleLeucine zipperTranscription GeneticMolecular Sequence DataBiologyLaboratorium voor ErfelijkheidsleerMeiosisSpermatocytesTestisGeneticsMelanogasterAnimalsDrosophila ProteinsLife ScienceAmino Acid SequenceGeneGenetics (clinical)GeneticsPolytene chromosomeBase SequenceDNAbiology.organism_classificationChromatinDrosophila melanogasterInsect ProteinsLaboratory of GeneticsDrosophila melanogasterEPSDrosophila Protein
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Polymorphisms cyclooxygenase-2 -765G>C and interleukin-6 -174G>C are associated with serum inflammation markers in a high cardiovascular risk populat…

2009

Inflammation is involved in cardiovascular diseases. Some studies have found that the Mediterranean diet (MD) can reduce serum concentrations of inflammation markers. However, none of these studies have analyzed the influence of genetic variability in such a response. Our objective was to study the effect of the -765G>C polymorphism in the cyclooxygenase-2 (COX-2) gene and the -174G>C polymorphism in the interleukin-6 (IL-6) gene on serum concentrations of IL-6, C-reactive protein, intercellular adhesion molecule 1 (ICAM-1) and vascular cell adhesion molecule-1 as well as their influence on the response to a nutritional intervention with MD. An intervention study in a high cardiovascular ri…

MaleMediterranean dietVascular cell adhesion molecule-1Suplements nutritiusMedicine (miscellaneous)InterleucinesDiet MediterraneanOlis vegetalsPolymorphism (computer science)Nutseducation.field_of_studyNutrition and DieteticsbiologyBiochemical markersPlant oilsMiddle AgedIntercellular Adhesion Molecule-1Dietary supplementsInflamacióOli d'olivaC-Reactive ProteinCardiovascular diseasesCardiovascular DiseasesMarcadors bioquímicsFemalemedicine.symptommedicine.medical_specialtyDiet therapyPopulationVascular Cell Adhesion Molecule-1InflammationDried fruitGenetic polymorphismsMediterranean cookingInternal medicineCuina mediterràniamedicineHumansPlant OilsGenetic variabilityInterleukin 6educationOlive OilAgedInflammationPolymorphism GeneticInterleukin-6Malalties cardiovascularsPolimorfisme genèticInterleukinsEndocrinologyGene Expression RegulationCyclooxygenase 2Immunologybiology.proteinCyclooxygenaseVegetable oilsFruita secaBiomarkersOlive oil
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A European family with histidine 58 transthyretin mutation in familial amyloid polyneuropathy

1997

1. IntroductionMore than 50 mutations of the transthyretin (TTR) [1]molecule resulting in different clinical forms of amyloidosisincluding familial amyloid polyneuropathy (FAP) havebeen reported to date. Within this FAP spectrum severaltransthyretin mutations are more frequent, others are rare.One mutation, the codon 58 histidine for leucine has pre-viously been recorded only in American subjects (Mary-land/German type), originally reported in a large kinship[2,3] and in another family from Ohio [4]. In the originaldescription of the Maryland/German type of amyloidosis[2], it was stated that the early immigrants in this pedigreewere from the Rhine river area, "nearly all of them from thelef…

MalePathologymedicine.medical_specialtyAtaxiaAmyloid Neuropathiesmedicine.disease_causeAtrophyLeucineGermanymedicineHumansPoint MutationPrealbuminHistidineCodonGenetics (clinical)Genes DominantMutationDysesthesiabiologybusiness.industryPoint mutationAmyloidosisMiddle Agedmedicine.diseaseUnited StatesTransthyretinNeurologyPediatrics Perinatology and Child Healthbiology.proteinNeurology (clinical)medicine.symptomRestriction fragment length polymorphismbusinessNeuromuscular Disorders
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A second family with familial AD and the V717L APP mutation has a later age at onset

2006

Four mutations have been reported at the 717 codon of the amyloid precursor protein (APP), with valine substituted by isoleucine, glycine, phenylalanine, and leucine. While several families with the isoleucine substitution have been described, the other substitutions have been reported in only one family each worldwide. A family with the V717L APP mutation has been previously reported,1 with a mean age at onset of 38 years (range 35 to 39), based on four affected family members, and a mean age at death of 46 years (range 40 to 50). We have identified a second family with a later mean age at onset of 50 years (range 48 to 57) and mean age at death of 61 years (range 57 to 68). Family 171 is …

MalePediatricsmedicine.medical_specialtyMutation Missensemedicine.disease_causeAmyloid beta-Protein PrecursorAlzheimer DiseaseValineInternal medicinemedicineAmyloid precursor proteinHumansAge of OnsetAgedAge of Onset Aged Alzheimer Disease/genetics Alzheimer Disease/physiopathology Amino Acid Substitution Amyloid beta-Protein Precursor/genetics Female Humans Malle Middle Aged Mutation Missense PedigreeMutationSettore M-PSI/02 - Psicobiologia E Psicologia FisiologicabiologyMean ageMiddle AgedPedigreeEndocrinologyAmino Acid Substitutionbiology.proteinFemaleNeurology (clinical)IsoleucineNeurology
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Identification and properties of the cell membrane bound leucine aminopeptidase interacting with the potential immunostimulant and chemotherapeutic a…

1983

Bestatin was found to be a competitive inhibitor (with respect to the Leu-NA substrate) not only of the isolated microsomal and cytosolic leucine aminopeptidases (Leu-APm and Leu-APc) but also of the aminopeptidases (APs) present in membrane preparations (from mouse liver) and on the cell surface of L5178Y cells. Kinetic parameters indicate that cellular AP is identical to Leu-APm. To rule out the possibility that AP-B is involved in the inhibition reactions, comparable studies with amastatin were performed. Electrophoretical studies revealed the solubilized cell membrane bound AP to co-migrate with Leu-APm in polyacrylamide gels. The activity of the separated membrane AP was inhibited by b…

MaleSurface PropertiesCellBiochemistryAminopeptidaseBinding CompetitiveCell membranechemistry.chemical_compoundLeucyl AminopeptidaseMiceAmastatinCytosolLeucinemedicineAnimalsCells CulturedPharmacologyBinding SitesChemistryCell CycleCell MembraneCell cycleCytosolmedicine.anatomical_structureBiochemistryMicrosomeMice Inbred CBALeucineProtein BindingBiochemical pharmacology
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Resistance to thyroid hormone in a family caused by a new point mutation L330S in the thyroid receptor (TR) beta gene.

1997

Resistance to thyroid hormone (RTH) is an inherited defect manifesting as variable tissue hyporesponsiveness to thyroid hormone, usually caused by mutations in the thyroid hormone receptor beta (TR beta) gene. Up to now 78 mutations in this gene have been identified, mostly clustered in two regions located in exon 9 and 10. We describe a new point mutation replacing the normal thymidine-1274 with a cytosine that results in the substitution of the normal leucine-330 with a serine (L330S) in the receptor protein. This mutation was identified in an 11-year-old boy who presented with symptoms and signs suggestive of both hyperthyroidism and hypothyroidism. Interestingly a mutation in the same c…

MaleThyroid Hormone Resistance Syndromeendocrine systemmedicine.medical_specialtyendocrine system diseasesEndocrinology Diabetes and MetabolismBiologyThyroid Function TestsThyroid hormone receptor betaEndocrinologyLeucineInternal medicinemedicineSerineHumansPoint MutationBeta (finance)ChildGeneThyroid hormone receptorReceptors Thyroid HormonePoint mutationdigestive oral and skin physiologyThyroidDNAExonsPedigreeEndocrinologymedicine.anatomical_structureMultigene FamilyCancer researchPAX8HormoneThyroid : official journal of the American Thyroid Association
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