Search results for " Enzymologic"

showing 10 items of 187 documents

Targeted disruption of the peroxisomal thiolase B gene in mouse: a new model to study disorders related to peroxisomal lipid metabolism

2004

The peroxisomal beta-oxidation system consists of four steps catalysed by three enzymes: acyl-CoA oxidase, 3-hydroxyacyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (multifunctional enzyme) and thiolase. In humans, thiolase activity is encoded by one gene, whereas in rodents, three enzymes encoded by three distinct genes (i.e. thiolase A, thiolase B and SCP2/thiolase) catalyse the thiolase activity. So far, acyl-CoA oxidase- and multifunctional enzyme-deficient patients have been identified and knock-out mice for these genes have been produced. Conversely, no isolated thiolase-deficient patient has been found, and no thiolase (A or B)-deficient mice have been generated. Hence, to better u…

DehydrogenaseBiologymedicine.disease_causeBiochemistryGene Expression Regulation EnzymologicPeroxisomal DisordersMiceStructure-Activity RelationshipPeroxisomesmedicineAnimalsHumansRNA MessengerGeneHydro-LyasesSCP2chemistry.chemical_classificationMutationOxidase testThiolaseStem Cells3-Hydroxyacyl CoA DehydrogenasesGeneral MedicinePeroxisomeAcetyl-CoA C-AcyltransferaseEmbryo MammalianLipid MetabolismMolecular biologyMice Mutant StrainsMice Inbred C57BLDisease Models AnimalPhenotypeEnzymechemistryBiochemistryAcyl-CoA OxidaseBiochimie
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Unraveling the evolutionary history of the phosphoryl-transfer chain of the phosphoenolpyruvate:phosphotransferase system through phylogenetic analys…

2007

[Background] The phosphoenolpyruvate phosphotransferase system (PTS) plays a major role in sugar transport and in the regulation of essential physiological processes in many bacteria. The PTS couples solute transport to its phosphorylation at the expense of phosphoenolpyruvate (PEP) and it consists of general cytoplasmic phosphoryl transfer proteins and specific enzyme II complexes which catalyze the uptake and phosphorylation of solutes. Previous studies have suggested that the evolution of the constituents of the enzyme II complexes has been driven largely by horizontal gene transfer whereas vertical inheritance has been prevalent in the general phosphoryl transfer proteins in some bacter…

FirmicutesEvolutionContext (language use)macromolecular substancesGene Expression Regulation EnzymologicEvolution MolecularPTS phosphoryl transfer chain (PTS-ptc)Genome ArchaealPhylogeneticsQH359-425DeinococcusPhosphorylationPhosphoenolpyruvate Sugar Phosphotransferase SystemGenePhylogenyEcology Evolution Behavior and SystematicsGeneticsBacteriaSequence Homology Amino AcidbiologyPhylogenetic tree:CIENCIAS DE LA VIDA::Biología celular::Citogenética [UNESCO]Phosphoenolpyruvate phosphotransferase system (PTS)Computational BiologyGene Expression Regulation BacterialPEP group translocationPhosphoenolpyruvate phosphotransferase system (PTS); Cytoplasmic phosphoryl transfer proteins; PTS phosphoryl transfer chain (PTS-ptc)biology.organism_classificationArchaeaUNESCO::CIENCIAS DE LA VIDA::Biología celular::CitogenéticaMultigene FamilyHorizontal gene transferbacteriaCytoplasmic phosphoryl transfer proteinsSequence AlignmentGenome BacterialResearch Article
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Expression of the Anti-amyloidogenic Secretase ADAM10 Is Suppressed by Its 5′-Untranslated Region*

2010

Proteolytic processing of the amyloid precursor protein by alpha-secretase prevents formation of the amyloid beta-peptide (Abeta), which is the main constituent of amyloid plaques in brains of Alzheimer disease (AD) patients. alpha-Secretase activity is decreased in AD, and overexpression of the alpha-secretase ADAM10 (a disintegrin and metalloprotease 10) in an AD animal model prevents amyloid pathology. ADAM10 has a 444-nucleotide-long, very GC-rich 5'-untranslated region (5'-UTR) with two upstream open reading frames. Because similar properties of 5'-UTRs are found in transcripts of many genes, which are regulated by translational control mechanisms, we asked whether ADAM10 expression is…

Five prime untranslated regionenzymology [Brain]ADAM10ADAM10 protein humanBACE1-ASgenetics [Amyloid Precursor Protein Secretases]genetics [Alzheimer Disease]genetics [ADAM Proteins]BiochemistryGene Expression Regulation Enzymologicbiosynthesis [Membrane Proteins]ADAM10 ProteinAlzheimer DiseaseChlorocebus aethiopsAmyloid precursor proteinProtein biosynthesisbiosynthesis [Amyloid beta-Peptides]genetics [Amyloid beta-Peptides]AnimalsHumansGene RegulationMolecular BiologySequence Deletionbiosynthesis [ADAM Proteins]Amyloid beta-PeptidesbiologyBase SequenceP3 peptideenzymology [Alzheimer Disease]BrainMembrane ProteinsCell BiologyMolecular biologyBiochemistry of Alzheimer's diseasegenetics [Membrane Proteins]ADAM Proteinsbiosynthesis [Amyloid Precursor Protein Secretases]Protein Biosynthesisddc:540COS Cellsbiology.proteinAmyloid Precursor Protein Secretases5' Untranslated RegionsAmyloid precursor protein secretase
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Myocardial G Protein Receptor–Coupled Kinase Expression Correlates With Functional Parameters and Clinical Severity in Advanced Heart Failure

2010

In heart failure (HF), sympathetic hyperactivation induces deleterious effects in myocardial β-adrenergic signaling, with receptor down-regulation and desensitization mediated by G protein receptor-coupled kinases (GRKs). We hypothesised that changes in GRK isoforms may be associated with clinical status in advanced HF, using the Interagency Registry for Mechanically Assisted Circulatory Support (INTERMACS) scale.We included 31 patients with advanced HF undergoing transplantation. According to INTERMACS profiles, mRNA and protein levels of GRK isoforms in left ventricular (LV) myocardium were analyzed and compared with nonfailing LV samples.In failing LV myocardium, GRK2 and GRK5 (but not G…

G-Protein-Coupled Receptor Kinase 5Malemedicine.medical_specialtyG-Protein-Coupled Receptor Kinase 2Down-RegulationPolymerase Chain ReactionSeverity of Illness IndexGene Expression Regulation EnzymologicInternal medicinemedicineHumansRNA MessengerRegistriesReceptorG protein-coupled receptorHeart FailureG protein-coupled receptor kinasebiologybusiness.industryMyocardiumBeta adrenergic receptor kinaseStroke volumeMiddle AgedG-Protein-Coupled Receptor Kinasesmedicine.diseaseTransplantationEndocrinologySpainHeart failureCirculatory systembiology.proteinFemaleHeart-Assist DevicesCardiology and Cardiovascular MedicinebusinessJournal of Cardiac Failure
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Alternatively spliced transcripts of the thymus-specific protease PRSS16 are differentially expressed in human thymus.

2004

The putative serine protease PRSS16 is abundantly expressed in the thymic cortex and the gene is encoded within the HLA I complex. Although its function is not yet defined, the very restricted expression points to a role in T-cell development in the thymus. In this study, we show that the PRSS16 mRNA is alternatively spliced to generate at least five transcripts. Apart from the full-length sequence, we found two other isoforms with all putative active site residues of the serine protease, suggesting that those variants may also be functional. Semi-quantitative analysis of the splice variants in different tissue samples revealed a strong correlation between the specific formation of alternat…

Gene isoformAdultMaleThymomamedicine.medical_treatmentImmunologyMolecular Sequence DataMorphogenesisThymus GlandGene Expression Regulation EnzymologicMyasthenia GravisGeneticsmedicineMorphogenesisHumansGeneGenetics (clinical)Serine proteaseMessenger RNAProteasebiologyBase SequenceSerine EndopeptidasesMiddle Agedmedicine.diseaseMolecular biologyMyasthenia gravisIsoenzymesAlternative Splicingbiology.proteinFemaleGenes and immunity
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Neuronal-Type NO Synthase: Transcript Diversity and Expressional Regulation

1998

Of the three established isoforms of NO synthase, the gene for the neuronal-type enzyme (NOS I) is by far the largest and most complicated one. The genomic locus of the human NOS I gene is located on chromosome 12 and distributed over a region greater than 200 kb. The nucleotide sequence corresponding to the major neuronal mRNA transcript is encoded by 29 exons. The full-length open reading frame codes for a protein of 1434 amino acids with a predicted molecular weight of 160.8 kDa. However, both in rodents and in humans, multiple, tissue-specific or developmentally regulated NOS I mRNA transcripts have been reported. They arise from the initiation by different transcriptional units contain…

Gene isoformCancer ResearchTranscription GeneticPolyadenylationPhysiologyClinical BiochemistryNitric Oxide Synthase Type IILocus (genetics)BiologyBiochemistryGene Expression Regulation EnzymologicExonGene expressionTranscriptional regulationAnimalsHumansRNA MessengerPromoter Regions GeneticGeneSequence DeletionMammalsGeneticsChromosomes Human Pair 12Gene Expression Regulation DevelopmentalAlternative SplicingOpen reading frameNitric Oxide SynthaseNitric Oxide
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Comparative analysis of zebrafish nos2a and nos2b genes

2008

Abstract Nitric oxide synthase (NOS) produces nitric oxide (NO) from arginine. Three NOS isoforms have been identified in mammals, namely a neuronal (NOS1), an inducible (NOS2) and an endothelial (NOS3) enzyme. In zebrafish genome, one nos1 gene and two nos2 genes (nos2a and nos2b) were observed. We cloned zebrafish nos2a cDNA and compared nos2a and nos2b sequences, expression and inducibility. When analyzed by reverse transcription-PCR, the expression of nos2a remained very low during initial development, then increased at 96 hpf, while nos2b was expressed from 6 hpf and subsequently remained stable. Expression of nos2a is detected in the head, eye and gut regions by WISH experiments perfo…

Gene isoformEmbryo Nonmammaliananimal structuresNOS1Molecular Sequence DataNitric Oxide Synthase Type IISyntenyGene Expression Regulation EnzymologicGene DuplicationComplementary DNAparasitic diseasesGene duplicationGeneticsAnimalsAmino Acid SequenceCloning MolecularGeneZebrafishCells CulturedPhylogenyZebrafishSequence Homology Amino AcidbiologyRegeneration (biology)fungiGene Expression Regulation DevelopmentalGeneral Medicinebiology.organism_classificationMolecular biologyIsoenzymesNitric oxide synthasebiology.proteinGene
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Regulation of the expression of inducible nitric oxide synthase.

2003

Nitric oxide (NO), generated by the inducible isoform of nitric oxide synthase (iNOS), has been described to have beneficial microbicidal, antiviral, antiparasital, immunomodulatory, and antitumoral effects. However, aberrant iNOS induction at the wrong place or at the wrong time has detrimental consequences and seems to be involved in the pathophysiology of several human diseases. iNOS is primarily regulated at the expression level by transcriptional and post-transcriptional mechanisms. iNOS expression can be induced in many cell types with suitable agents such as bacterial lipopolysaccharides (LPS), cytokines, and other compounds. Pathways resulting in the induction of iNOS expression may…

Gene isoformLipopolysaccharidesCell typeTranscription GeneticClinical BiochemistryNitric Oxide Synthase Type IINitric OxideBiochemistryGene Expression Regulation EnzymologicNitric oxidechemistry.chemical_compoundAnimalsHumansRNA MessengerPromoter Regions GeneticMolecular BiologyTranscription factorRegulation of gene expressionbiologyChemistryNF-kappa BInterferon-Stimulated Gene Factor 3Cell biologyNitric oxide synthaseBiochemistryInterferon-Stimulated Gene Factor 3biology.proteinCytokinesSignal transductionNitric Oxide SynthaseSignal TransductionTranscription FactorsBiological chemistry
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Potential Functional Significance of Brain-Type and Muscle-Type Nitric Oxide Synthase I Expressed in Adventitia and Media of Rat Aorta

1999

Abstract —Skeletal muscle and myocardium express μNOS I, an elongated splice variant of neuronal-type nitric oxide (NO) synthase (NOS I), and NOS III, endothelial-type NO synthase, respectively. This study was designed to elucidate whether vascular smooth muscle also contains a constitutively expressed NO synthase isoform. In the rat, μNOS I contains an insert of 102 nucleotides after nucleotide 2865 of the cDNA, yielding a protein of 164 kd. Reverse transcription-polymerase chain reaction with primers flanking this insert and with insert-specific primers indicated that endothelium-denuded rat aorta expresses both brain-type NOS I and μNOS I. RNase protection analyses with an antisense RNA…

Gene isoformPathologymedicine.medical_specialtyDNA ComplementaryVascular smooth muscleNitric Oxide Synthase Type IIIBlotting WesternAorta ThoracicNitric Oxide Synthase Type INitroarginineGene Expression Regulation EnzymologicMuscle Smooth VascularMembrane PotentialsPotassium ChlorideNitric oxideImmunoenzyme TechniquesRats Sprague-DawleyNorepinephrinechemistry.chemical_compoundmedicine.arteryAdventitiamedicineAnimalsVasoconstrictor AgentsAorta AbdominalRNA MessengerMuscle SkeletalMessenger RNAAortabiologyBrainSkeletal muscleMolecular biologyRatsNitric oxide synthaseAntisense Elements (Genetics)medicine.anatomical_structurechemistryVasoconstrictionbiology.proteinCalciumFemaleNitric Oxide SynthaseTunica MediaCardiology and Cardiovascular MedicineArteriosclerosis, Thrombosis, and Vascular Biology
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Regulation of the expression of inducible nitric oxide synthase

2010

Nitric oxide (NO) generated by the inducible isoform of nitric oxide synthase (iNOS) is involved in complex immunomodulatory and antitumoral mechanisms and has been described to have multiple beneficial microbicidal, antiviral and antiparasital effects. However, dysfunctional induction of iNOS expression seems to be involved in the pathophysiology of several human diseases. Therefore iNOS has to be regulated very tightly. Modulation of expression, on both the transcriptional and post-transcriptional level, is the major regulation mechanism for iNOS. Pathways resulting in the induction of iNOS expression vary in different cells or species. Activation of the transcription factors NF-kappaB an…

Gene isoformRegulation of gene expressionCancer ResearchPhysiologyClinical BiochemistryNitric Oxide Synthase Type IIRNA-Binding ProteinsRNARNA-binding proteinBiologyBiochemistryGene Expression Regulation EnzymologicPathophysiologyNitric oxideCell biologyNitric oxide synthasechemistry.chemical_compoundBiochemistrychemistrybiology.proteinHumansRNA MessengerPromoter Regions GeneticTranscription factorTranscription FactorsNitric Oxide
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