Search results for "ACETYL-COA"

showing 10 items of 33 documents

Nucleotide Variability at the Acetyl Coenzyme A Carboxylase Gene and the Signature of Herbicide Selection in the Grass Weed Alopecurus myosuroides (H…

2004

Acetyl coenzyme A carboxylase (ACCase) is the target of highly effective herbicides. We investigated the nucleotide variability of the ACCase gene in a sample of 18 black-grass (Alopecurus myosuroides [Huds.]) populations to search for the signature of herbicide selection. Sequencing 3,396 bp encompassing ACCase herbicide-binding domain in 86 individuals revealed 92 polymorphisms, which formed 72 haplotypes. The ratio of nonsynonymous versus synonymous substitutions was very low, in agreement with ACCase being a vital metabolic enzyme. Within black grass, most nonsynonymous substitutions were related to resistance to ACCase-inhibiting herbicides. Differentiation between populations was stro…

0106 biological sciencesNonsynonymous substitutionMolecular Sequence DataStatistics as TopicBiologyGenes PlantPoaceae01 natural sciencesLinkage DisequilibriumNucleotide diversity03 medical and health sciences[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyGeneticsVULPIN[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMolecular BiologyGeneAllelesPhylogenyComputingMilieux_MISCELLANEOUSEcology Evolution Behavior and SystematicsSelection (genetic algorithm)030304 developmental biologychemistry.chemical_classificationGenetics0303 health sciencesPolymorphism GeneticBase SequenceModels GeneticHaplotypeAlopecurus myosuroidesGenetic VariationDNASequence Analysis DNAPesticidebiology.organism_classificationProtein Structure TertiaryEnzymeHaplotypeschemistrySoftwareAcetyl-CoA Carboxylase010606 plant biology & botanyMolecular Biology and Evolution
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An isoleucine residue within the carboxyl-transferase domain of multidomain acetyl-coenzyme A carboxylase is a major determinant of sensitivity to ar…

2003

Abstract A 3,300-bp DNA fragment encoding the carboxyl-transferase domain of the multidomain, chloroplastic acetyl-coenzyme A carboxylase (ACCase) was sequenced in aryloxyphenoxypropionate (APP)-resistant and -sensitive Alopecurus myosuroides (Huds.). No resistant plant contained an Ile-1,781-Leu substitution, previously shown to confer resistance to APPs and cyclohexanediones (CHDs). Instead, an Ile-2,041-Asn substitution was found in resistant plants. Phylogenetic analysis of the sequences revealed that Asn-2,041 ACCase alleles derived from several distinct origins. Allele-specific polymerase chain reaction associated the presence of Asn-2,041 with seedling resistance to APPs but not to C…

0106 biological sciencesPhysiologyMolecular Sequence DataSequence alignmentPlant ScienceBiology01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants geneticschemistry.chemical_compoundMagnoliopsida[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsmental disordersGeneticsTransferaseVULPINAmino Acid SequenceIsoleucinePeptide sequencePhylogenyComputingMilieux_MISCELLANEOUS2. Zero hungerchemistry.chemical_classificationPolymorphism GeneticCyclohexanonesHerbicidesAcetyl-CoA carboxylase04 agricultural and veterinary sciencesACETYL-COA CARBOXYLASEPyruvate carboxylaseProtein Structure TertiaryEnzymeBiochemistrychemistryMutation040103 agronomy & agriculture0401 agriculture forestry and fisheriesIsoleucinePropionatesSequence AlignmentDNA010606 plant biology & botanyResearch Article
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Universal primers for PCR-sequencing of grass chloroplastic acetyl-CoA carboxylase domains involved in resistance to herbicides

2005

Summary Primers were designed to amplify two regions involved in sensitivity to herbicides inhibiting the plastidic acetyl-CoA carboxylase (ACCase) from grasses (Poaceae). The first primer pair amplified a 551-bp amplicon containing a variable Ile/Leu codon at position 1781 in Alopecurus myosuroides sequence. The second primer pair amplified a 406-bp amplicon containing four variable codons (Trp/Cys, Ile/Asn, Asp/Gly, Gly/Ala) at positions 2027, 2041, 2078 and 2096, respectively, in A. myosuroides sequence. Both primer pairs amplified the targeted fragments from genes encoding plastidic ACCases, but not from the very similar genes encoding cytosolic ACCases. Clear DNA sequences were obtaine…

0106 biological sciencesPlant Science01 natural sciencesDNA sequencinglaw.inventionlaw[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyPoa annua[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyACETYL COENZYME-A CARBOXYLASEGeneEcology Evolution Behavior and SystematicsPolymerase chain reactionComputingMilieux_MISCELLANEOUSGeneticsbiologyAlopecurus myosuroidesAcetyl-CoA carboxylasefood and beverages04 agricultural and veterinary sciencesAmpliconbiology.organism_classificationBiochemistry040103 agronomy & agriculture0401 agriculture forestry and fisheriesPrimer (molecular biology)Agronomy and Crop Science010606 plant biology & botany
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An isoleucine-leucine substitution in chloroplastic acetyl-CoA carboxylase from green foxtail (Setaria viridis L. Beauv.) is responsible for resistan…

2002

The cDNAs encoding chloroplastic acetyl-CoA carboxylase (ACCase, EC 6.4.1.2) from three lines of Setaria viridis (L. Beauv.) resistant or sensitive to sethoxydim, and from one sethoxydim-sensitive line of Setaria italica (L. Beauv.) were cloned and sequenced. Sequence comparison revealed that a single isoleucine-leucine substitution discriminated ACCases from sensitive and resistant lines. Using near-isogenic lines of S. italica derived from interspecific hybridisation, we demonstrated that the transfer of the S. viridis mutant ACCase allele into a sethoxydim-sensitive S. italica line conferred resistance to this herbicide. We confirmed this result using allele-specific polymerase chain rea…

0106 biological sciencesSetariaChloroplastsMutantMolecular Sequence DataDrug ResistancePlant ScienceMolecular cloningPoaceae01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants geneticsLeucine[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsGeneticsPoint MutationAmino Acid SequenceIsoleucineComputingMilieux_MISCELLANEOUSAllelesPhylogenyGenes DominantbiologySequence Homology Amino AcidSetaria viridisCyclohexanonesHerbicidesAcetyl-CoA carboxylase04 agricultural and veterinary sciencesbiology.organism_classification3. Good healthPyruvate carboxylaseBiochemistryAmino Acid Substitution040103 agronomy & agriculture0401 agriculture forestry and fisheriesLeucineIsoleucineSequence Alignment010606 plant biology & botanyAcetyl-CoA CarboxylasePlanta
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Full-length sequencing and identification of novel polymorphisms in the ACACA gene of Valle del Belice sheep breed

2017

The essential role of the acetyl-CoA carboxylase (ACACA) enzyme in milk fatty acid (FA) synthesis suggests that it may be responsible for the phenotypic variability observed in milk. Before attempting association analyses between this gene and/or enzyme and phenotypic traits, a study on the genetic variability within this locus is required. The aim of this work was to sequence the entire coding region of ACACA gene in Valle del Belice sheep breed to identify polymorphic sites. A total of 51 coding exons of ACACA gene were sequenced in 32 individuals of Valle del Belice sheep breed. Sequencing analysis and alignment of obtained sequences showed the presence of 23 polymorphic sites. The most …

0301 basic medicineGenetic MarkerssheepSingle-nucleotide polymorphismLocus (genetics)BiologyBreedingPolymorphism Single Nucleotide03 medical and health sciencesExonSettore AGR/17 - Zootecnica Generale E Miglioramento Geneticosingle-nucleotide polymorphismsGeneticsAnimalsGenetic variabilityGeneACACA gene single-nucleotide polymorphisms sheep Valle del Belice breedGeneticsValle del Belice breedACACAHaplotype0402 animal and dairy science04 agricultural and veterinary sciencesExonsSequence Analysis DNAsingle-nucleotide polymorphism040201 dairy & animal scienceACACA gene; sheep; single-nucleotide polymorphisms; Valle del Belice breed030104 developmental biologyPhenotypeAmino Acid SubstitutionHaplotypesGenetic markerMutationACACA geneAcetyl-CoA Carboxylase
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Targeting cellular fatty acid synthesis limits T helper and innate lymphoid cell function during intestinal inflammation and infection

2019

CD4+ T cells contribute critically to a protective immune response during intestinal infections, but have also been implicated in the aggravation of intestinal inflammatory pathology. Previous studies suggested that T helper type (Th)1 and Th17 cells depend on de novo fatty acid (FA) synthesis for their development and effector function. Here, we report that T-cell-specific targeting of the enzyme acetyl-CoA carboxylase 1 (ACC1), a major checkpoint controlling FA synthesis, impaired intestinal Th1 and Th17 responses by limiting CD4+ T-cell expansion and infiltration into the lamina propria in murine models of colitis and infection-associated intestinal inflammation. Importantly, pharmacolog…

0301 basic medicineImmunologyBiologyMice03 medical and health scienceschemistry.chemical_compound0302 clinical medicineImmune systemRAR-related orphan receptor gammamedicineAnimalsImmunology and AllergyFatty acid synthesisBarrier functionLamina propriaEffectorFatty AcidsInnate lymphoid cellT-Lymphocytes Helper-InducerNuclear Receptor Subfamily 1 Group F Member 3ColitisInflammatory Bowel DiseasesImmunity InnateBiosynthetic PathwaysDisease Models Animal030104 developmental biologymedicine.anatomical_structurechemistryImmunologyLipogenesisBiomarkersAcetyl-CoA Carboxylase030215 immunologyMucosal Immunology
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Resveratrol shifts energy metabolism to increase lipid oxidation in healthy old mice.

2019

Abstract Objectives The objective of this work was to determine the specific mechanisms by which resveratrol inhibits lipogenesis and stimulates lipolysis. Methods Twelve male mice were individually introduced into a metabolic cage for 24 h to measure basal metabolic rate, prior to intervention. They were randomly divided into two groups, resveratrol (RSV) and control (C), and administered resveratrol intraperitoneally or vehicle, respectively, for two consecutive days. After 24 h, the metabolic energy expenditure was again determined for 24 h, before mice were sacrificed. Protein and gene expression of different enzymes related to metabolism in the hepatic tissue, adipose tissue and gastro…

0301 basic medicinePolyphenolMalemedicine.medical_specialtyAgingLipolysisAdipose tissueWhite adipose tissueRM1-950ResveratrolLipid catabolism03 medical and health scienceschemistry.chemical_compoundMice0302 clinical medicineInternal medicinemedicineAnimalsCarnitineBeta oxidationFatty acid synthesisRespiratory quotientPharmacologyLipogenesisFatty AcidsGeneral MedicineMice Inbred C57BL030104 developmental biologyEndocrinologyMalonyl-CoAchemistryAdipose TissueCarnitine AcyltransferasesLiverResveratrol030220 oncology & carcinogenesisLipogenesisTherapeutics. PharmacologyEnergy MetabolismOxidation-Reductionmedicine.drugAcetyl-CoA CarboxylaseBiomedicinepharmacotherapy = Biomedecinepharmacotherapie
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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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Modulation of the hepatic fatty acid pool in peroxisomal 3-ketoacyl-CoA thiolase B-null mice exposed to the selective PPARalpha agonist Wy14,643

2009

10 pages; International audience; The peroxisomal 3-ketoacyl-CoA thiolase B (Thb) gene was previously identified as a direct target gene of PPARalpha, a nuclear hormone receptor activated by hypolipidemic fibrate drugs. To better understand the role of ThB in hepatic lipid metabolism in mice, Sv129 wild-type and Thb null mice were fed or not the selective PPARalpha agonist Wy14,643 (Wy). Here, it is shown that in contrast to some other mouse models deficient for peroxisomal enzymes, the hepatic PPARalpha signaling cascade in Thb null mice was normal under regular conditions. It is of interest that the hypotriglyceridemic action of Wy was reduced in Thb null mice underlining the conclusion t…

MESH : RNA MessengerMESH: Microsomes LiverMESH : PyrimidinesMono-unsaturated fatty acids n-7 and n-9MESH : Hepatocytes[SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyMESH: Mice KnockoutPPARαBiochemistryMESH: Acetyl-CoA C-AcetyltransferaseStearoyl-CoA desaturase-1MESH: HepatocytesMicechemistry.chemical_compoundMESH : Lipid MetabolismWy14MESH: AnimalsPeroxisomal 3-ketoacyl-CoA thiolase BAcetyl-CoA C-AcetyltransferaseMESH: PPAR alphaMESH : Fatty AcidsMESH: Lipid MetabolismMice Knockoutchemistry.chemical_classificationThiolaseFatty Acids643General MedicinePeroxisomeMESH : Stearoyl-CoA DesaturaseMESH: Fatty AcidsMESH : Microsomes LiverMESH : Acetyl-CoA C-AcetyltransferaseMicrosomes LiverMono-unsaturated fatty acids n-7 and n-9; Peroxisomal 3-ketoacyl-CoA thiolase B; PPARα; Stearoyl-CoA desaturase-1; Wy14643lipids (amino acids peptides and proteins)Stearoyl-CoA DesaturasePolyunsaturated fatty acidmedicine.medical_specialtyMESH : PPAR alphaMESH : Mice Inbred C57BL[ SDV.BBM.BM ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyBiologyMESH: Mice Inbred C57BLInternal medicineMESH : MicePeroxisomesmedicineAnimalsHumansPPAR alphaRNA MessengerMESH: MiceMESH: RNA MessengerSCP2MESH: HumansMESH : HumansFatty acid[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyStearoyl-CoALipid MetabolismMESH: PeroxisomesSterol regulatory element-binding proteinMice Inbred C57BLPyrimidinesEndocrinologychemistryMESH: PyrimidinesMESH: Stearoyl-CoA DesaturaseHepatocytesMESH : Mice KnockoutMESH : AnimalsStearoyl-CoA desaturase-1MESH : PeroxisomesBiochimie
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Pre-imaginal exposure to Oberon® disrupts fatty acid composition, cuticular hydrocarbon profile and sexual behavior in Drosophila melanogaster adults

2021

International audience; Oberon® is a commercial formulation of spiromesifen, a pesticide inhibitor of lipid biosynthesis via acetyl CoA carboxylase, widely used in agricultural crop protection. However, its mode of action requires further analysis. We currently examined the effect of this product on Drosophila melanogaster as a non-target and model organism. Different concentrations of spiromesifen were administered by ingestion (and contact) during pre-imaginal development, and we evaluated its delayed action on adults. Our results suggest that spiromesifen induced insecticidal activity on D. melanogaster. Moreover, spiromesifen treatment significantly increased the duration of larval and …

Male0106 biological sciencesInsecticidesmedicine.medical_specialtyPhysiologyHealth Toxicology and MutagenesisAnimal ScalesBiologyToxicology01 natural sciencesBiochemistrySexual Behavior Animal03 medical and health sciencessexual behaviorInternal medicineLipid biosynthesisMelanogastermedicineAnimalsSpiro CompoundsMode of action030304 developmental biology0303 health sciencesLarvacuticular hydrocarbonsFatty AcidsfungiAcetyl-CoA carboxylasetoxicityLipid metabolismCell BiologyGeneral Medicinebiology.organism_classificationspiromesifenHydrocarbons[SDV.BA.ZI]Life Sciences [q-bio]/Animal biology/Invertebrate Zoology010602 entomologyDrosophila melanogasterEndocrinologyToxicityFemaleDrosophila melanogasterComparative Biochemistry and Physiology Part C: Toxicology & Pharmacology
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