Search results for "complementary DNA"

showing 10 items of 243 documents

Selective detection of mRNA forms encoding the major phenobarbital inducible cytochromes P450 and other members of the P450IIB family by the RNAse A …

1990

Abstract The identification of P450 mRNAs in a tissue poses the problem that members of the same P450 gene family share a high sequence homology. Studies based on oligomer probes rely on a probe covering only a few base pairs. In contrast in our study on the expression of the P450IIB gene family we used in vitro-generated antisense transcripts, covering several hundred base pairs, of the hypervariable and constant regions of the P450IIB1 and P450IIB2 cDNA, in the RNAse A protection assay of mRNA isolated from various tissues. RNAse A concentrations were adjusted to a level where this enzyme still yielded distinct fragments for a defined P450IIB1 antisense/P450IIB2 sense heteroduplex, which …

MaleRNase PBiophysicsGene ExpressionBiologyBiochemistryPeptide MappingCytochrome P-450 Enzyme SystemComplementary DNASense (molecular biology)Gene expressionGene familyAnimalsRNA MessengerMolecular BiologyGeneNucleaseRats Inbred StrainsRNA ProbesRibonuclease PancreaticMolecular biologyRatsBiochemistryGenesbiology.proteinHeteroduplexArchives of biochemistry and biophysics
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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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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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Long-term therapeutic levels of human alpha-1 antitrypsin in plasma after hydrodynamic injection of nonviral DNA

2003

The transfection efficacy of several vectors containing the full genomic hAAT gene with its natural promoter (pTG7101) and others containing the cDNA of hAAT gene driven by cytomegalovirus immediate-early promoter or the 0.5 kb upstream of hAAT gene sequence has been studied by hydrodynamic tail-vein injection (20 microg/mouse). pTG7101 (but not the other plasmids) results in therapeutic and stable concentration of hAAT in plasma. A dose-response study with this plasmid (0.3-320 microg/mouse) confirms that hAAT remains long-term stable in plasma, with therapeutic concentrations of hAAT (>0.9 mg/ml). The parameters of the dose-response curve were: R: 0.98, E(max) 3449.0+/- 279.7 microg/ml an…

MaleTime FactorsTransgeneGenetic enhancementMolecular Sequence DataGene ExpressionBiologyGene deliveryTransfectionInjectionsMicePlasmidComplementary DNAGene expressionGeneticsAnimalsHumansTransgenesMolecular BiologyGeneBase SequenceReverse Transcriptase Polymerase Chain ReactionDNAGenetic TherapyTransfectionImmunohistochemistryMolecular biologyMice Inbred C57BLLiveralpha 1-AntitrypsinMolecular MedicineGene Therapy
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Gene diagnosis and carrier detection in Hunter syndrome by the iduronate-2-sulphatase cDNA probe.

1992

Hunter disease (McKusick 309900) is an X-chromosomal mucopolysaccharidosis due to deficiency of the lysosomal enzyme iduronate-2-sulphatase (IDS; EC 3.1.6.13). Diagnosis is based on both the typical clinical features of patients and the lack/reduction of IDS activity. Female carriers show no symptoms of the disease. In the past, several different assays were elaborated for measuring enzyme activity in carriers but none of them proved to be suitable for detecting heterozygotes reliably (Zlotogora and Bach 1984)

MaleX ChromosomeMucopolysaccharidosisIduronate SulfataseBiologyGene mappingComplementary DNAGenotypeGeneticsmedicineHumansAlleleChildDeoxyribonucleases Type II Site-SpecificGenetics (clinical)Mucopolysaccharidosis IIGeneticsGenetic Carrier ScreeningHunter syndromeHeterozygote advantagemedicine.diseaseMolecular biologyEnzyme assayPedigreeBlotting Southernbiology.proteinDNA ProbesPolymorphism Restriction Fragment LengthJournal of inherited metabolic disease
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Molecular Cloning and mRNA Expression of Heat Shock Protein Genes and Their Response to Cadmium Stress in the Grasshopper Oxya chinensis

2015

Heat shock proteins (Hsps) are highly conserved molecular chaperones that are synthesized in response to stress. In this study, we cloned the full-length sequences of the Grp78 (glucose-regulated protein 78), Hsp70, Hsp90, and Hsp40 genes from the Chinese rice grasshopper Oxya chinensis. The full-length cDNA sequences of OcGrp78, OcHsp70, OcHsp90, and OcHsp40 contain open reading frames of 1947, 1920, 2172, and 1042 bp that encode proteins of 649, 640, 724, and 347 amino acids, respectively. Fluorescent real-time quantitative PCR (RT-qPCR) was performed to quantify the relative transcript levels of these Hsp genes in different tissues and developmental stages. The mRNAs encoding these four …

MaleZygotelcsh:MedicineGrasshoppersOpen Reading FramesStress PhysiologicalComplementary DNAHeat shock proteinGene expressionAnimalsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsRNA MessengerCloning Molecularlcsh:ScienceEndoplasmic Reticulum Chaperone BiPGeneHeat-Shock ProteinsRegulation of gene expressionMultidisciplinarybiologylcsh:RHSP40 Heat-Shock ProteinsHsp90Molecular biologyHsp70Real-time polymerase chain reactionGene Expression RegulationLarvabiology.proteinInsect ProteinsFemalelcsh:QResearch ArticleCadmiumSignal TransductionPLOS ONE
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Molecular characterization of a new adult male putative calycin specific to tergal aphrodisiac secretion in the cockroach Leucophaea maderae

2001

0014-5793 (Print) Journal Article Research Support, Non-U.S. Gov't; Lma-p18 is an epicuticular surface protein specific to the tergal gland aphrodisiac secretion of Leucophaea maderae adult males. Native Lma-p18 was purified and the complete cDNA sequence was determined by RT-PCR using primers based on Edman degradation fragments. Northern blot and in situ hybridization analyses showed that Lma-p18 is expressed exclusively in the anterior part of male tergal gland, which is exposed only during sexual behavior. Sequence analysis indicated that Lma-p18 belongs to the calycin superfamily and is very similar to Lma-p22, the first known male-specific tergal protein in L. maderae. Lma-p18 and Lma…

Maleendocrine systemendocrine system diseasesSequence analysisMolecular Sequence DataBiophysicsSequence HomologyCockroachesIn situ hybridizationBiochemistryExocrine GlandsCockroachStructural Biologybiology.animalComplementary DNAGeneticsAnimalsDevelopmentalSex behaviorAphrodisiacNorthern blotAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceSecretionCockroachSequence Homology Amino AcidbiologyEdman degradationBase SequenceGene Expression Regulation DevelopmentalMolecularCell BiologyTergal glandMolecular biologyCalycinAmino AcidGene Expression RegulationLarvaExocrine Glands/metabolismInsect Proteins/*genetics/*metabolismCockroaches/*physiologyInsect ProteinsFemaleCloning
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Cloning of Two Putative Ecdysteroid Receptor Isoforms from Tenebrio Molitor and their Developmental Expression in the Epidermis during Metamorphosis

1997

Using the Drosophila EcR-B1 cDNA as a probe, we have cloned the putative ecdysteroid receptor from the mealworm Tenebrio molitor. We have isolated two cDNAs with different 5' termini that contain a complete open reading frame. These two cDNAs encode two proteins with distinct N-terminal regions corresponding to two isoforms. The coleopteran receptor is obviously related to the ecdysteroid receptor of other insects, but shares only 89% and 61% amino acid identities with the DNA-binding and ligand-binding domains of the Drosophila receptor, respectively. Its expression pattern has been examined in the epidermis during the last larval instar and pupal stage of T. molitor, in correlation with t…

MealwormGene isoformReceptors SteroidDNA Complementaryanimal structuresInvertebrate Hormonesmedia_common.quotation_subjectMolecular Sequence DataBiochemistrychemistry.chemical_compoundHemolymphComplementary DNABotanyHemolymphAnimalsAmino Acid SequenceRNA MessengerCloning MolecularMetamorphosisTenebriomedia_commonEcdysteroidBase SequenceSequence Homology Amino AcidbiologyfungiMetamorphosis BiologicalPupaGene Expression Regulation DevelopmentalSequence Analysis DNABlotting Northernbiology.organism_classificationCell biologyOpen reading frameDrosophila melanogasterEcdysteronechemistryLarvaEpidermisEcdysone receptorEuropean Journal of Biochemistry
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Expression and distribution of the glucocorticoid receptor DlGR1 in the teleost Dicentrarchus labrax brain

2009

Cortisol is the main corticosteroid secreted by the interrenal cells of the head kidney and it exerts a role in mantaining the omeostatic status in fish. In teleosts its effects are mediated through intracellular receptors expressed in several tissues, that are ligand-dependent transcription factors by binding to specific tissue DNA sequences. In Dicentrarchus labrax we previously cloned and sequenced a glucocorticoid receptor, DlGR1, isolated from leukocytes of peritoneal cavity. In this work we showed mRNA expression and tissue immunohistochemical localization of brain DlGR1 by in situ hybridization assays, with a riboprobe with DlGR1 cDNA trascriptional activation domain, and by immunohi…

Messenger RNAD. labraxSettore BIO/05 - ZoologiaRiboprobeIn situ hybridizationBiologyD. labrax Immunohistochemistry In situ hybridization Glucocorticoid receptorMolecular biologyGlucocorticoid receptorHormone receptorComplementary DNAimmunohistochemistryglucocorticoid receptorglucocorticoidAnimal Science and Zoologyin situ hybridizationlcsh:Animal cultureReceptorTranscription factorlcsh:SF1-1100
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Isolation and characterization of a Paracentrotus lividus cDNA encoding a stress-inducible chaperonin

2001

Chaperonins are ubiquitous proteins that facilitate protein folding in an adenosine triphosphate–dependent manner. Here we report the isolation of a sea urchin cDNA (Plhsp60) coding for mitochondrial chaperonin (Cpn60), whose basal expression is further enhanced by heat shock. The described cDNA corresponds to a full-length mRNA encoding a protein of 582 amino acids, the first 32 of which constitute a putative mitochondrial targeting leader sequence. Comparative analysis has demonstrated that this protein is highly conserved in evolution.

Messenger RNADNA ComplementaryEmbryo NonmammalianbiologyShort CommunicationMolecular Sequence DataChaperonin 60Cell Biologybiology.organism_classificationBiochemistryMolecular biologyParacentrotus lividusMitochondriaChaperoninCell biologySea UrchinsComplementary DNAAnimalsProtein foldingHSP60Amino Acid SequenceRNA MessengerHeat shockPeptide sequenceHeat-Shock Response
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