Search results for "Molecular sequence"

showing 10 items of 1972 documents

A pheromone-binding protein from the cockroach Leucophaea maderae: cloning, expression and pheromone binding

2003

0264-6021 (Print) Journal Article; Odorant-binding proteins (OBPs) are thought to transport volatile compounds from air to their receptors through the sensillary lymph. In this protein family, the subgroup of pheromone-binding proteins (PBPs) is specifically tuned to the perception of the sexual pheromone. To date, the description of OBPs has been restricted to Endopterygota and Paraneoptera. Their expression in Orthopteroid has been hypothesized, but no evidence of OBP has been produced in this assemblage to date. In the present study, we describe the first OBP from a Dictyopteran insect that belongs to the cockroach Leucophaea maderae. The PBP of L. maderae (PBPLma) shares all the hallmar…

Carrier Proteins/*genetics/*metabolismProtein familymedia_common.quotation_subjectMolecular Sequence DataCockroachesEndopterygotaInsectBiochemistryPolymerase Chain ReactionPheromonesbiology.animalPheromones/*metabolismAnimalsPheromone bindingAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceIn Situ Hybridizationmedia_commonCockroachbiologyBase SequenceMolecularCell Biologybiology.organism_classificationRecombinant ProteinsBiochemistryCockroaches/*physiologyInsect ProteinsPheromoneCarrier ProteinsPheromone binding proteinInsect Proteins/genetics/metabolismRecombinant Proteins/chemistry/metabolismResearch ArticleCloning
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Complexity of IL-1β induced gene expression pattern in human articular chondrocytes

1997

The mRNA fingerprinting technique, differential display reverse transcription polymerase chain (DDRT-PCR), was used to detect changes in the overall pattern of gene expression in human articular knee chondrocytes-induced by interleukin-1 beta (IL-1 beta), the prototypical inducer of catabolic responses in degenerate joint diseases. One hundred different primer combinations generated approximately 10,000 different PCR fragments for IL-1 beta treated, as well as for untreated human chondrocytes, cultivated in alginate beads. This represented 53% of all expressed chondrocyte genes as based on statistical considerations. Side by side comparisons of differential display patterns originating from…

Cartilage ArticularDNA ComplementaryMolecular Sequence DataCell Culture TechniquesBiomedical EngineeringBiologyPolymerase Chain ReactionChondrocyteChondrocytesRheumatologyComplementary DNAGene expressionOsteoarthritismedicineHumansOrthopedics and Sports MedicineRNA MessengerGeneAgedDifferential displayDifferential displayIL-1Middle AgedBlotting NorthernMolecular biologyReverse transcriptaseReal-time polymerase chain reactionmedicine.anatomical_structureGene Expression RegulationFemalePrimer (molecular biology)Interleukin-1Osteoarthritis and Cartilage
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Identification and characterisation of the dopamine receptor II from the cat flea Ctenocephalides felis (CfDopRII)

2006

International audience; G protein-coupled receptors (GPCRs) represent a protein family with a wide range of functions. Approximately 30% of human drug targets are GPCRs, illustrating their pharmaceutical relevance. In contrast, the knowledge about invertebrate GPCRs is limited and is mainly restricted to model organisms like Drosophila melanogaster and Caenorhabditis elegans. Especially in ectoparasites like ticks and fleas, only few GPCRs are characterised. From the cat flea Ctenocephalides felis, a relevant parasite of cats and dogs, no GPCRs are known so far. Thus, we performed a bioinformatic analysis of available insect GPCR sequences from the honeybee Apis mellifera, the mosquito Anop…

Cat fleaAnopheles gambiaeMolecular Sequence Dataved/biology.organism_classification_rank.speciesBiochemistryCell LineReceptors DopamineAnimals Genetically ModifiedXenopus laevisAnimalsHumansAmino Acid SequenceCloning MolecularModel organismMolecular BiologyPhylogenyCaenorhabditis elegansCtenocephalides[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]G protein-coupled receptorGeneticsbiologyved/biologyEcologyFelisComputational Biologybiology.organism_classificationDrosophila melanogasterMultigene FamilyInsect ScienceOocytesInsect ProteinsSiphonapteraFemaleRNA Interference[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Drosophila melanogasterSequence Alignment[CHIM.CHEM]Chemical Sciences/Cheminformaticshormones hormone substitutes and hormone antagonistsInsect Biochemistry and Molecular Biology
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Silicateins, the major biosilica forming enzymes present in demosponges: protein analysis and phylogenetic relationship.

2007

Silicateins are enzymes, which are restricted to sponges (phylum Porifera), that mediate the catalytic formation of biosilica from monomeric silicon compounds. The silicatein protein is compartmented in the sponges in the axial filaments which reside in the axial canals of the siliceous spicules. In the present study silicatein has been isolated from the freshwater sponge Lubomirskia baicalensis where it occurs in isoforms with sizes of 23 kDa, 24 kDa and 26 kDa. Since the larger protein is glycosylated we posit that it is a processed form of one of the smaller size forms. The silicatein isoforms are post-translationally modified by phosphorylation; at least four isoforms exist with pI's of…

Cathepsin LMolecular Sequence DataCathepsin LDemospongeCatalytic triadGeneticsAnimalsAmino Acid SequenceGenePeptide sequencePhylogenyCathepsinbiologySequence Homology Amino AcidGeneral MedicineExonsbiology.organism_classificationSilicon DioxideCathepsinsIntronsPoriferaSuberites domunculaSpongeCysteine EndopeptidasesMicroscopy ElectronBiochemistrybiology.proteinGene
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Expression of M-cadherin protein in myogenic cells during prenatal mouse development and differentiation of embryonic stem cells in culture.

1994

Molecules regulating morphogenesis by cell-cell interactions are the cadherins, a class of calcium-dependent adhesion molecules. One of its members, M-cadherin, has been isolated from a myoblast cell line (Donalies et al. [1991] Proc. Natl. Acad. Sci. U.S.A. 88:8024—8028). In mouse development, expression of M-cadherin mRNA first appears at day 8.5 of gestation (E8.5) in somites and has been postulated to be down-regulated in developing muscle masses (Moore and Walsh [1993] Development 117:1409—1420). Affinity-purified polyclonal M-cadherin antibodies, detecting a protein of approximately 120 kDa, were used to study the cell expression pattern of M-cadherin protein. It was first visualized …

Cell Adhesion Molecules NeuronalRecombinant Fusion ProteinsMolecular Sequence DataMorphogenesisFluorescent Antibody TechniqueGestational AgeBiologyEmbryonic and Fetal DevelopmentMiceLamininPregnancyMyocyteAnimalsAmino Acid SequenceRNA MessengerMuscle SkeletalCells CulturedDNA PrimersMice Inbred BALB CBase SequenceCadherinCell adhesion moleculeStem CellsCell MembraneGene Expression Regulation DevelopmentalCadherinsEmbryonic stem cellMolecular biologyCell culturebiology.proteinDesminFemaleDevelopmental BiologyDevelopmental dynamics : an official publication of the American Association of Anatomists
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Cloning of a rat-specific long PCP4/PEP19 isoform

2007

We report the identification of a cDNA that encodes a putative protein of 94 amino acids and expected molecular weight of 10.7 kDa, the C-terminal half of which is identical to that of PEP19, a small, brain-specific protein involved in Ca++/calmodulin signaling. The novel rat-specific protein, tentatively named long PEP19 isoform (LPI), is the product of alternative splicing of the rat PCP4 gene encoding PEP19. We found that antibodies raised against the first 13 N-terminal amino acids of LPI, not present in PEP19, recognize a protein enriched in the developing rat brain.

Cell ExtractsGene isoformProtein isoformDNA ComplementaryCalmodulinMolecular Sequence DataNerve Tissue ProteinsAntibodiesRats Sprague-DawleyMiceExonComplementary DNAGeneticsAnimalsHumansProtein IsoformsAmino Acid SequenceRNA MessengerCloning MolecularPeptide sequencechemistry.chemical_classificationBase SequencebiologyGene Expression ProfilingAlternative splicingBrainGene Expression Regulation DevelopmentalRNA-Binding ProteinsExonsGeneral MedicineMolecular biologyIntronsRatsAmino acidchemistryBiochemistrybiology.proteinCalmodulin-Binding ProteinsPeptidesInternational Journal of Molecular Medicine
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Termination of transcription in an ‘in vitro’ system is dependent on a polyadenylation sequence

1991

Using HeLa cell nuclear extract as a source of the different transcription and polyadenylation factors and reverse transcription to analyze the levels of RNA 5' and 3' to the cleavage-polyadenylation site, an in vitro assay has been established to study polyadenylation coupled to transcription directed by different adenovirus promoters. The levels of transcription 5' and 3' to the cleavage site in the L3 polyadenylation region are practically the same as described previously, however, the level of transcription 3' to the cleavage site in the SV40 early polyadenylation region decreases immediately after the cleavage site indicating a termination of the transcription.

Cell ExtractsTranscription GeneticPolyadenylationMolecular Sequence DataRNA polymerase IISimian virus 40BiologyCleavage (embryo)AdenoviridaeTranscription (biology)GeneticsRNA MessengerPromoter Regions GeneticBase SequenceRNARNA-Directed DNA PolymerasePromoterMolecular biologyReverse transcriptasebiology.proteinRNA Polymerase IIChromosome DeletionPoly ACytokinesisHeLa CellsPlasmidsNucleic Acids Research
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Down-regulation of nuclear binding activities of OXBOX-REBOX transcription factors during cellular senescence.

1996

Functional capacity of mitochondria declines during aging and this impairment may have a major role in aging process. Several observations indicate that transcriptional efficiency is reduced during aging. Our purpose was to find out whether aging and cellular senescence affect the nuclear binding activities of transcription factors which bind to OXBOX-REBOX sequence present in promoter regions of numerous nuclear genes encoding mitochondrial proteins. These factors regulate and coordinate the expression of mitochondrial proteins. We observed a strong down-regulation in the nuclear binding activities of OXBOX-REBOX factors in replicatively senesced human WI-38 and IMR-90 fibroblasts. On the …

Cell cycle checkpointNuclear genePhotoagingMolecular Sequence DataBiophysicsDown-RegulationPlasma protein bindingBiologyMitochondrionBiochemistryDownregulation and upregulationmedicineAnimalsHumansRats WistarMolecular BiologyTranscription factorCellular SenescenceCell Line TransformedBase SequenceNuclear ProteinsCell BiologyDNAmedicine.diseaseCell biologyRatsCell cultureProtein BindingTranscription FactorsBiochemical and biophysical research communications
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Molecular evolution of the metazoan extracellular matrix: cloning and expression of structural proteins from the demosponges Suberites domuncula and …

2000

One crucial event during evolution to multicellularity was the development of either direct cell–cell contact or indirect interaction via extracellular matrix (ECM) molecules. The identification of those polypeptides provides conclusive data on the phylogenetic relationship of metazoan phyla and helps us to understand the position of the Metazoa among the other kingdoms. Recently it became evident that the ECM of sponges is amazingly complex; it is composed of fibrous molecules, e.g., collagen, and their corresponding receptors, which are highly similar to those existing in other metazoan phyla. While these data already support the view of monophyly of Metazoa, additional studies are requir…

Cell signalingDNA ComplementaryDermatopontinMolecular Sequence DataGene ExpressionBiologyBioinformaticsTransplantation AutologousExtracellular matrixEvolution MolecularMyotrophinGeneticsAnimalsAmino Acid SequenceCloning MoleculareducationGrowth SubstancesMolecular BiologyPeptide sequenceEcology Evolution Behavior and SystematicsPhylogenyCell Aggregationeducation.field_of_studyExtracellular Matrix ProteinsBase SequenceSequence Homology Amino AcidReceptor Protein-Tyrosine Kinasesbiology.organism_classificationRecombinant ProteinsCell biologyPoriferaSuberites domunculaTransplantationChondroitin Sulfate ProteoglycansIntercellular Signaling Peptides and ProteinsCollagenCarrier ProteinsCell Adhesion MoleculesFunction (biology)Journal of molecular evolution
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α-Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure

2001

Disintegrin metalloproteases from different organisms form the ADAM (a disintegrin and metalloprotease) family. All members display a common domain organization and possess four potential functions: proteolysis, cell adhesion, cell fusion, and cell signaling. Members of the ADAM family are responsible for the proteolytic cleavage of transmembrane proteins and release of their extracellular domain. The proteolytic process is referred to as ectodomain shedding, which is activated by phorbol esters and inhibited by hydroxamic acid-based inhibitors. We have shown that the disintegrin metalloprotease ADAM 10 has both constitutive and regulated alpha-secretase activity. Expression of a dominant n…

Cell signalingDisintegrinsMolecular Sequence DataProtein domainBiologyGeneral Biochemistry Genetics and Molecular BiologyADAM10 ProteinAmyloid beta-Protein PrecursorHistory and Philosophy of ScienceEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansProtease InhibitorsAmino Acid SequenceCell adhesionMetalloproteinaseGeneral NeuroscienceHEK 293 cellsMembrane ProteinsMetalloendopeptidasesRecombinant ProteinsTransmembrane proteincarbohydrates (lipids)ADAM ProteinsBiochemistryEctodomainbiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAnnals of the New York Academy of Sciences
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