Search results for "Dehydrogenases"

showing 10 items of 55 documents

17β-Hydroxysteroid dehydrogenase-3 deficiency: From pregnancy to adolescence

2009

OBJECTIVE: Aim of this study is to report on basal clinical phenotype and follow up after diagnosis, of patients with 17beta-hydroxysteroid-dehydrogenase type 3 (17beta-HSD3) deficiency in Italy. SETTING: Pediatric Endocrine Departments, University Hospitals. PATIENTS: The cases of 5 Italian subjects affected by 17beta-HSD3 deficiency are presented in this study. INTERVENTIONS: Laboratory and genetic assessment. Gonadectomy and female sex assignment (4 patients) or GnRH analog therapy to regress puberty and gender identity disorder (1 patient). RESULTS: Presentation lasted from pregnancy (pre-natal diagnosis of a 46,XY fetus with female external genitalia) to infancy (inguinal hernia contai…

MaleGender Identity DisorderPediatricsmedicine.medical_specialty17-Hydroxysteroid DehydrogenasesEndocrinology Diabetes and MetabolismSex assignmentPrenatal diagnosisGene mutationBiologyClitoromegalyAdolescence pregnancy 17beta-Hydroxysteroid dehydrogenase-3 deficiencySettore MED/38 - Pediatria Generale E SpecialisticaEndocrinologyPregnancyPrenatal DiagnosismedicineHumansDisorders of sex developmentDISORDERS OF SEX DEVELOPMENTTestosterone17-BETA-HYDROXYSTEROID DEHYDROGENASE TYPE 3 GENEGynecologyPregnancyPubertymedicine.diseaseFemaleMALE/FEMALE SEX REVERSALTESTOSTERONE/D4-ANDROSTENEDIONE RATIO17-BETA-HYDROXYSTEROID DEHYDROGENASE TYPE 3 DEFICIENCYmedicine.symptomJournal of Endocrinological Investigation
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Dihydrodiol dehydrogenase activities of rabbit liver are associated with hydroxysteroid dehydrogenases and aldo-keto reductases.

1992

1. Dihydrodiol dehydrogenase activities were investigated in rabbit liver. Using a five-step purification scheme, eight isoenzymes of dihydrodiol dehydrogenase with isoelectric points of 5.55-9.3 and promoter molecular masses of 34-35 kDa were purified to apparent homogeneity and designated CF-1 to CF-6, CM-1 and CM-2. 2. CF-1 and CF-2 had near-neutral isoelectric points of 7.4 and 6.8 and molecular masses of about 125 kDa in the native state. Both enzymes readily accepted NAD+ as well as NADP+ as coenzymes, had relatively low Km values of 0.33 mM and 0.47 mM for benzene dihydrodiol and resembled previously described carbonyl reductases in their substrate specificity towards ketones and qui…

MaleOxidoreductases Acting on CH-CH Group DonorsCarbonyl ReductaseStereochemistryAldo-Keto ReductasesDehydrogenaseReductaseBiochemistryCofactorCatalysisSubstrate SpecificityAldehyde Reductasepolycyclic compoundsAnimalsTissue DistributionIsoelectric PointAldehyde ReductaseAldo-keto reductasebiologyChemistryHydroxysteroid DehydrogenasesAntibodies MonoclonalHydroxysteroid DehydrogenasesIsoenzymesMolecular WeightAlcohol OxidoreductasesBiochemistryLiverbiology.proteinElectrophoresis Polyacrylamide GelNAD+ kinaseRabbitsOxidoreductasesEuropean journal of biochemistry
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Characteristics of the spermathecal contents of old and young honeybee queens.

2009

Sperm are often stored, for a long time after mating, in females of various animal species. In case of the queen honeybee (Apis mellifera), sperm remain fertile for several years in the spermatheca. Little information is available regarding the effect of long-term storage of sperm on its fertility. To evaluate this, enzymes and/or sperm have been analysed from the spermatheca of 75 queens of various ages (0 year Y0, n=14; one year Y1, n=14; two years Y2, n=7; virgin queen VQ, n=40) and semen samples have been taken from 46 drones. The sperm from the spermatheca of older queens move more slowly (F=11.45, P < 0.0001) and show different movement patterns (Chi2=90.0, P < 0.0001) from those of t…

Maleendocrine systemPhysiologyCell Survivalmedia_common.quotation_subjectSemenFertilityAndrologychemistry.chemical_compoundSpermathecaLactate dehydrogenaseBotanyCitrate synthaseAnimalsMatingAnimal speciesreproductive and urinary physiologymedia_commonAnalysis of VariancebiologyL-Lactate Dehydrogenaseurogenital systemAge FactorsGlyceraldehyde-3-Phosphate DehydrogenasesArginine KinaseGenitalia FemaleBeesSpermSpermatozoachemistryInsect Sciencebiology.proteinFemaleJournal of insect physiology
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17beta-hydroxysteroid dehydrogenase-3 deficiency: a rare endocrine cause of male-to-female sex reversal.

2006

Deficiency of 17beta-hydroxysteroid dehydrogenase type 3 (17beta-HSD3), due to mutations in the gene encoding the enzyme, results in a rare autosomal recessive form of male-to-female sex reversal. Mutated genes encode an abnormal enzyme with absent or reduced ability to convert Delta4-androstenedione to testosterone in the testis. Affected individuals are genetically males who developed internal male Wolffian structures but female external genitalia. Such individuals are usually raised as females and diagnosis is made at puberty, when they show virilization. Correct diagnosis is mandatory to optimize treatment and follow-up. In the present paper we report the clinical history, endocrine eva…

Malemedicine.medical_specialty17-Hydroxysteroid DehydrogenasesEndocrinology Diabetes and MetabolismDisorders of Sex Development17beta-hydroxysteroid dehydrogenaseBiologyEndocrine System Diseaseschemistry.chemical_compoundEndocrinologyMolecular geneticsInternal medicinemedicineEndocrine systemHumansGeneTestosteroneVirilizationObstetrics and GynecologySex reversalmedicine.diseaseEndocrinologychemistryChild PreschoolAndrogensAndrogen insensitivity syndromeFemalemedicine.symptomGynecological endocrinology : the official journal of the International Society of Gynecological Endocrinology
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Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: a severe fatty acid oxidation disorder

1994

3-Hydroxyacyl-CoA dehydrogenase deficiency is a newly recognised fatty acid oxidation disorder with a usually fatal outcome. We present a further patient who presented with hypoketotic hypoglycaemia, hepatopathy, secondary carnitine deficiency and increased plasma long-chain acylcarnitines. 3-Hydroxydicarboxylic aciduria was present and the diagnosis confirmed in cultured skin fibroblasts. Our patient is compared with those reported in the literature with respect to clinical symptoms, differential diagnosis and possible therapeutic regimens.

Malemedicine.medical_specialtyCardiomyopathyLipid Metabolism Inborn ErrorsFatal OutcomeInternal medicineCarnitineMedicineHumansBeta oxidationchemistry.chemical_classificationCultured skinbusiness.industryLiver DiseasesInfant Newborn3-Hydroxyacyl CoA DehydrogenasesMitochondrial MyopathiesClinical Enzyme Testsmedicine.diseaseDehydrogenase deficiencyHypoglycemiaEnzymeEndocrinologychemistrySecondary carnitine deficiencyPediatrics Perinatology and Child HealthDifferential diagnosisbusinessCardiomyopathiesLong-Chain-3-Hydroxyacyl-CoA DehydrogenaseEuropean journal of pediatrics
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Effect of endurance training on the capacity of red and white skeletal muscle of mouse to oxidize carboxyl-14C-labelled palmitate.

1977

Three groups of mice were trained for 1, 4 and 5 months according to different running programs on a motor driven treadmill and the fatty acid oxidation capacity (FAO) and the activities of some enzymes of energy metabolism (cytochrome c oxidase, malate dehydrogenase, triosephosphate dehydrogenase, and lactate dehydrogenase) were determined from m. quadriceps femoris (MQF). Endurance training increased the FAO [5-month training 4 days/week, 30 min/day 22% (p less than 0.05); 1-month training, 7 days/week, 150 min/day 37% (p less than 0.001); 4-month training, 5 days/week, 60 min/day 24% (p less than 0.05)]. The activities of cytochrome c oxidase and malate dehydrogenase increased approx. 30…

Malemedicine.medical_specialtyTime FactorsPhysiologyPhysical ExertionPalmitatesPalmitic AcidsBiologyMalate dehydrogenaseElectron Transport Complex IVchemistry.chemical_compoundMiceEndurance trainingMalate DehydrogenaseLactate dehydrogenaseInternal medicineOxidative enzymemedicineCytochrome c oxidaseAnimalsCarbon RadioisotopesBeta oxidationchemistry.chemical_classificationL-Lactate DehydrogenaseMusclesSkeletal muscleGlyceraldehyde-3-Phosphate DehydrogenasesEnzymeEndocrinologymedicine.anatomical_structurechemistrybiology.proteinOxidation-ReductionActa physiologica Scandinavica
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The Low Energy-Coupling Respiration in Zymomonas mobilis Accelerates Flux in the Entner-Doudoroff Pathway.

2015

Performing oxidative phosphorylation is the primary role of respiratory chain both in bacteria and eukaryotes. Yet, the branched respiratory chains of prokaryotes contain alternative, low energy-coupling electron pathways, which serve for functions other than oxidative ATP generation (like those of respiratory protection, adaptation to low-oxygen media, redox balancing, etc.), some of which are still poorly understood. We here demonstrate that withdrawal of reducing equivalents by the energetically uncoupled respiratory chain of the bacterium Zymomonas mobilis accelerates its fermentative catabolism, increasing the glucose consumption rate. This is in contrast to what has been observed in o…

Metabolic Processes0301 basic medicineRespiratory chainlcsh:MedicineBiochemistryOxidative PhosphorylationGlucose Metabolismlcsh:ScienceZymomonasMultidisciplinarybiologyOrganic CompoundsSimulation and ModelingMonosaccharidesChemical ReactionsCatabolismAerobiosisEnzymesChemistryBiochemistryPhysical SciencesCarbohydrate MetabolismOxidoreductasesOxidation-ReductionResearch Article030106 microbiologyCarbohydratesAcetaldehydeOxidative phosphorylationResearch and Analysis MethodsZymomonas mobilisElectron Transport03 medical and health sciencesOxidationEntner–Doudoroff pathwayDehydrogenasesOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesProteinsNADbiology.organism_classificationElectron transport chainKineticsGlucoseMetabolismFermentationEnzymologyFermentationlcsh:QFlux (metabolism)BacteriaPLoS ONE
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Clinical strains ofCandida albicansexpress the surface antigen glyceraldehyde 3-phosphate dehydrogenase in vitro and in infected tissues

1999

We have previously described the presence of an enzymatically active form of glyceraldehyde 3-phosphate-dehydrogenase (GAPDH) in the cell surface of Candida albicans ATCC 26555 which is also a fibronectin and laminin binding protein. Immunohistochemical analysis of tissue sections from patients with disseminated candidiasis with a polyclonal antiserum to GAPDH from C. albicans (PAb anti-CA-GAPDH) revealed that the enzyme is expressed at the surface of fungal cells in infected tissues. The same PAb detected the presence of GAPDH species, with a molecular mass of approximately 33 kDa, in cell wall extracts obtained from clinical isolates of the fungus. These cell surface-bound GAPDH moieties …

Microbiology (medical)Antigens FungalImmunologyMicrobiologyMicrobiologyImmunoenzyme Techniqueschemistry.chemical_compoundstomatognathic systemAntigenGlyceraldehydeCandida albicansHumansImmunology and AllergyCandida albicansGlyceraldehyde 3-phosphate dehydrogenaseAntiserumbiologyGlyceraldehyde-3-Phosphate DehydrogenasesGeneral Medicinebiology.organism_classificationMolecular biologyCorpus albicansInfectious DiseaseschemistryPolyclonal antibodiesAntigens Surfacebiology.proteinGlyceraldehyde 3-phosphateFEMS Immunology &amp; Medical Microbiology
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Active surfaces engineered by immobilizing protein-polymer nanoreactors for selectively detecting sugar alcohols.

2016

We introduce active surfaces generated by immobilizing protein-polymer nanoreactors on a solid support for sensitive sugar alcohols detection. First, such selective nanoreactors were engineered in solution by simultaneous encapsulation of specific enzymes in copolymer polymersomes, and insertion of membrane proteins for selective conduct of sugar alcohols. Despite the artificial surroundings, and the thickness of the copolymer membrane, functionality of reconstituted Escherichia coli glycerol facilitator (GlpF) was preserved, and allowed selective diffusion of sugar alcohols to the inner cavity of the polymersome, where encapsulated ribitol dehydrogenase (RDH) enzymes served as biosensing e…

Models MolecularMaterials scienceMembrane permeabilityPolymersSurface PropertiesBiophysicsBioengineering02 engineering and technologyNanoreactorBiosensing Techniques010402 general chemistryRibitolAquaporins01 natural sciencesPermeabilityBiomaterialschemistry.chemical_compoundSugar AlcoholsEscherichia coliOrganic chemistrySugar alcoholRibitolchemistry.chemical_classificationEscherichia coli Proteins021001 nanoscience & nanotechnology0104 chemical sciencesNanostructuresMembraneImmobilized ProteinschemistryMechanics of MaterialsPolymersomeCeramics and Composites0210 nano-technologyBiosensorSugar Alcohol DehydrogenasesSugar Alcohol DehydrogenasesBiomaterials
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The analysis of modified peroxisome proliferator responsive elements of the peroxisomal bifunctional enzyme in transfected HepG2 cells reveals two re…

1995

AbstractPeroxisome proliferators (PPs) are non-genotoxic carcinogens in rodents. They can induce the expression of numerous genes via the heterodimerization of two members of the steroid hormone receptor superfamily, called the peroxisome proliferator-activated receptor (PPAR) and the 9-cis retinoic acid receptor (RXR). Many of the PP responsive genes possess a peroxisome proliferator response element (PPRE) formed by two TGACCT-related motifs. The bifunctional enzyme (HD) PPRE contains 3 such motifs, creating DR1 and DR2 sequences. PPAR and RXR regulate transcription via the DR1 element while DR2 modulates the expression of the gene via auxiliary factors in HepG2 cells.

Peroxisome proliferator-activated receptor gammaReceptors Retinoic AcidSteroid hormone receptorMolecular Sequence DataResponse elementBiophysicsReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorchemical and pharmacologic phenomenaIn Vitro TechniquesRegulatory Sequences Nucleic AcidRetinoid X receptorBiologyPeroxisomal Bifunctional EnzymeTransfectionMicrobodiesBiochemistryGene Expression Regulation EnzymologicTranscriptional activationPeroxisomal Bifunctional EnzymeMultienzyme ComplexesStructural BiologyPeroxisome proliferator response element9-cis Retinoic acid receptor alphaTumor Cells CulturedGeneticsHumansRNA MessengerIsomerasesEnoyl-CoA HydrataseMolecular Biologychemistry.chemical_classificationBinding SitesBase Sequence3-Hydroxyacyl CoA DehydrogenasesPeroxisome proliferator-activated receptorCell BiologyDNA-Binding ProteinsRetinoic acid receptorRetinoid X ReceptorsLiverOligodeoxyribonucleotidesBiochemistrychemistryRat peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenaseEnzyme InductionPeroxisome proliferator-activated receptor alphaTranscription FactorsFEBS Letters
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