Search results for "complementary DNA"

showing 10 items of 243 documents

Hamster Bcl-2 Protein Is Cleaved in Vitro and in Cells by Caspase-9 and Caspase-3

2001

Full-length cDNA of hamster bcl-2 (771 nt) was cloned by RT-PCR and inserted into pGEX-4T-1 to produce the recombinant hamster Bcl-2 protein. The purified recombinant Bcl-2 protein (26.4 kDa) was used as a substrate for the active human caspase-3 and caspase-9 in vitro. It is shown here that Bcl-2 is efficiently cleaved by caspase-3 to a 23 kDa fragment. Although not possessing a putative caspase-9 cleavage site in its sequence, hamster Bcl-2 was also cleaved by caspase-9 into exactly the same 23 kDa cleavage product, indicating that cleavage occurred at the same site. Caspase-3- and caspase-9-mediated cleavage of Bcl-2 was efficiently blocked by caspase-3 (zDEVD) and caspase-9 (zLEHD) inhi…

Recombinant Fusion ProteinsBlotting WesternBiophysicsHamsterCaspase 3CHO CellsCysteine Proteinase InhibitorsCleavage (embryo)Biochemistrylaw.inventionlawCricetinaeComplementary DNAAnimalsHumansMolecular BiologyCaspaseGlutathione TransferaseCleavage stimulation factorbiologyCaspase 3Chinese hamster ovary cellThrombinCell BiologyCaspase InhibitorsMolecular biologyCaspase 9Proto-Oncogene Proteins c-bcl-2Caspasesbiology.proteinRecombinant DNAOligopeptidesBiochemical and Biophysical Research Communications
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Cloning and analysis of cDNA for rat histone H1°

1993

Regulation of gene expressionCloningbiologyCellular differentiationMolecular cloningMolecular biologychemistry.chemical_compoundHistonechemistryHistone H1Complementary DNAGeneticsbiology.proteinDNANucleic Acids Research
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Mapping and structure of DMXL1, a human homologue of the DmX gene from Drosophila melanogaster coding for a WD repeat protein.

2000

The DmX gene was recently isolated from the X chromosome of Drosophila melanogaster. TBLASTN searches of the dbEST databases revealed sequences with a high level of similarity to DmX in a variety of different species, including insects, nematodes, and mammals showing that DmX is an evolutionarily highly conserved gene. Here we describe the cloning of the cDNA and the chromosomal localization of one of the human homologues of DmX, Dmx-like 1 (DMXL1). The human DMXL1 gene codes for a large mRNA of 11 kb with an open reading frame of 3027 amino acids. The putative protein belongs to the superfamily of WD repeat proteins, which have mostly regulatory functions. The DMXL1 protein contains an exc…

Repetitive Sequences Amino AcidDNA ComplementaryMolecular Sequence DataBiologyConserved sequenceMiceGene mappingComplementary DNAGeneticsAnimalsDrosophila ProteinsHumansRadiation hybrid mappingAmino Acid SequenceDinucleotide RepeatsGeneIn Situ Hybridization FluorescenceGeneticsBase SequenceChromosome MappingProteinsbiology.organism_classificationOpen reading frameDrosophila melanogasterChromosomes Human Pair 5Insect ProteinsDrosophila melanogasterDrosophila ProteinGenomics
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Stimulation of protein (collagen) synthesis in sponge cells by a cardiac myotrophin‐related molecule from Suberites domuncula

2000

The body wall of sponges (Porifera), the lowest metazoan phylum, is formed by two epithelial cell layers of exopinacocytes and endopinacocytes, both of which are associated with collagen fibrils. Here we show that a myotrophin-like polypeptide from the sponge Suberites domuncula causes the expression of collagen in cells from the same sponge in vitro. The cDNA of the sponge myotrophin was isolated; the potential open reading frame of 360 nt encodes a 120 aa long protein (Mr of 12,837). The sequence SUBDOMYOL shares high similarity with the known metazoan myotrophin sequences. The expression of SUBDOMYOL is low in single cells but high after formation of primmorph aggregates as well as in in…

Repetitive Sequences Amino AcidMolecular Sequence DataLysinePolymerase Chain ReactionBiochemistryMyotrophinComplementary DNAGeneticsProtein biosynthesisAnimalsAmino Acid SequenceCloning MolecularGrowth SubstanceseducationMolecular BiologyPhylogenyCell Sizeeducation.field_of_studyDose-Response Relationship DrugSequence Homology Amino AcidbiologySequence Analysis DNAbiology.organism_classificationRecombinant ProteinsIn vitroPoriferaUp-RegulationCell biologySuberites domunculaOpen reading frameSpongeIntercellular Signaling Peptides and ProteinsCollagenBiotechnologyThe FASEB Journal
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The putative sponge aggregation receptor. Isolation and characterization of a molecule composed of scavenger receptor cysteine-rich domains and short…

1998

Porifera (sponges) are the oldest extant metazoan phylum. Dissociated sponge cells serve as a classic system to study processes of cell reaggregation. The reaggregation of dissociated cells is mediated by an extracellularly localized aggregation factor (AF), based on heterophilic interactions of the third order; the AF bridges two cells by ligating a cell-surface-bound aggregation receptor (AR). In the present study we report cloning, expression and immunohistochemical localization of a polypeptide from the marine sponge Geodia cydonium, which very likely represents the AR. The presumed AR gene gives rise to at least three forms of alternatively spliced transcripts of 6.5, 4.9 and 3.9 kb, a…

Repetitive Sequences Amino Acidmedicine.drug_classMolecular Sequence DataReceptors Cell SurfaceCell CommunicationMonoclonal antibodyPolymerase Chain Reactionlaw.inventionAntigenlawComplementary DNAConsensus SequencemedicineAnimalsAmino Acid SequenceCloning MolecularReceptors ImmunologicReceptorCell AggregationReceptors LipoproteinRepetitive Sequences Nucleic AcidReceptors ScavengerbiologyMolecular massBase SequenceSequence Homology Amino AcidMembrane ProteinsCell BiologySequence Analysis DNAScavenger Receptors Class BMolecular biologyRecombinant ProteinsPoriferaTransmembrane domainBiochemistrybiology.proteinRecombinant DNAAntibodyProtein Binding
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Cloning of a novel putative G-protein-coupled receptor (NLR) which is expressed in neuronal and lymphatic tissue.

1993

AbstractA novel G-protein-coupled receptor was isolated from mouse and rat neuronal and lymphatic tissues. The amino acid sequence of the rat receptor (rNLR) shows an overall homology of 80% to a recently cloned receptor from Burkitt's lymphoma cells (BLR1) which is exclusively expressed in lymphatic tissues [(1992) Eur. J. Immunol. 22, 2795]. Much less homology between rNLR and BLR1 was observed at the N-terminus (about 40%), whereas rNLR and the mouse homologue mNLR show 92% amino acid identity. Northern blot analysis of NLR revealed a predominant 5.5 kb mRNA species in various brain regions and neuronal cell lines, whereas in the spleen a 3 kb transcript is predominant. This distribution…

Restriction MappingInterleukin 8BiochemistryReceptors G-Protein-CoupledMiceStructural BiologyTumor Cells CulturedLymphocytesCloning MolecularReceptorPeptide sequencechemistry.chemical_classificationNeuronsGenomic LibraryBurkitt's lymphomaBrainBurkitt LymphomaPolymerase chain reactionAmino acidOligodeoxyribonucleotidesOrgan SpecificityG-protein-coupled receptorBLR1Molecular Sequence DataBiophysicsReceptors Cell SurfaceBiologyNLRGTP-Binding ProteinsComplementary DNAGeneticsmedicineAnimalsHumansNorthern blotAmino Acid SequenceRNA MessengerMolecular BiologyG protein-coupled receptorMessenger RNABase SequenceSequence Homology Amino AcidCell Biologymedicine.diseaseMolecular biologyIntronsRatsNG108-15 cellchemistryBurkitt's lymphomaFEBS letters
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A Candida albicans 37 kDa polypeptide with homology to the laminin receptor is a component of the translational machinery.

1998

A cDNA encoding a 37 kDa protein was isolated from an expression library using antibodies raised against mycelial cell walls fromCandida albicans.The 37 kDa protein has over 60% sequence identity with the 37 kDa laminin-binding protein (LBP) from humans and over 80% identity with the Yst proteins ofSaccharomyces cerevisiae. TheC. albicansprotein was named CaYst1. It was found in membrane and ribosome fractions but surprisingly, was not found in cell walls. Unlike the human LBP, CaYst1p does not bind laminin. These data indicate that CaYst1p is not a cell-surface receptor for laminin as has been proposed for the human LBP. Instead, like theS. cerevisiaeYst proteins, it appears to be a riboso…

Ribosomal ProteinsSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeBlotting WesternMolecular Sequence DataMicrobiologyFungal ProteinsReceptors LamininRibosomal proteinComplementary DNACandida albicansAnimalsHumansCandida albicansAntibodies Fungalchemistry.chemical_classificationFungal proteinbiologyBase SequenceBinding proteinMembrane Proteinsbiology.organism_classificationBlotting NorthernMolecular biologyBlotting SouthernCytoskeletal ProteinsBiochemistrychemistryMembrane proteinProtein BiosynthesisRabbitsGlycoproteinSequence AlignmentMicrobiology (Reading, England)
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Increased serum miR-193a-5p during non-alcoholic fatty liver disease progression: Diagnostic and mechanistic relevance

2022

Background & Aims Serum microRNA (miRNA) levels are known to change in non-alcoholic fatty liver disease (NAFLD) and may serve as useful biomarkers. This study aimed to profile miRNAs comprehensively at all NAFLD stages. Methods We profiled 2,083 serum miRNAs in a discovery cohort (183 cases with NAFLD representing the complete NAFLD spectrum and 10 population controls). miRNA libraries generated by HTG EdgeSeq were sequenced by Illumina NextSeq. Selected serum miRNAs were profiled in 372 additional cases with NAFLD and 15 population controls by quantitative reverse transcriptase PCR. Results Levels of 275 miRNAs differed between cases and population controls. Fewer differences were seen wi…

SCORING SYSTEMCPM counts per millionAUROC area under the receiver operating characteristicRC799-869AST aspartate aminotransferaseMicroRNA; Non-alcoholic fatty liver disease; Biomarker; SequencingTGF-β transforming growth factor-betaGastroenterologySTEATOHEPATITISLiver disease0302 clinical medicineFibrosismiRNA microRNAlogFC log2 fold changeFIBROSISImmunology and AllergySequencing0303 health scienceseducation.field_of_studyNAS NAFLD activity scoremedicine.diagnostic_testFatty liverGastroenterologyGTEx Genotype-Tissue ExpressionMicroRNADiseases of the digestive system. Gastroenterology3. Good healthReal-time polymerase chain reactionBiomarker MicroRNA Non-alcoholic fatty liver disease SequencingLiver biopsyACIDBiomarker (medicine)030211 gastroenterology & hepatologyLife Sciences & BiomedicineResearch ArticleEXPRESSIONmedicine.medical_specialtyNAFLD non-alcoholic fatty liver diseaseNASH non-alcoholic steatohepatitisPopulationGastroenterology and HepatologySAF steatosis–activity–fibrosisVALIDATIONER endoplasmic reticulum03 medical and health sciencescDNA complementary DNAInternal medicineALT alanine aminotransferaseGastroenterologiInternal MedicinemedicineNAFL non-alcoholic fatty liverALGORITHMFIB-4 fibrosis-4education030304 developmental biologyPCA principal component analysisScience & TechnologyGastroenterology & HepatologyHepatologybusiness.industryBiomarkerFC fold changemedicine.diseaseBiomarker; MicroRNA; Non-alcoholic fatty liver disease; Sequencingdigestive system diseasesFLIP fatty liver inhibition of progressionCt cycle thresholdSteatosisqPCR quantitative PCRbusinessNon-alcoholic fatty liver disease
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The nucleotide and partial amino acid sequences of rat fetuin. Identity with the natural tyrosine kinase inhibitor of the rat insulin receptor.

1992

Fetuins are among the major plasma proteins, yet their biological role has remained elusive. Here we report the molecular cloning of rat fetuin and the sequence analysis of a full-length clone, RF619 of 1456 bp with an open reading frame of 1056 bp encoding 352 amino acid residues. The coding part of RF619 was identical with the cDNA sequence of the natural inhibitor of the insulin receptor tyrosine kinase from rat (pp63) except for four substitutions and a single base insertion causing divergence of the predicted protein sequences. Partial amino acid sequences of rat plasma fetuin were in agreement with the predictions based on the RF619 cDNA. Purified rat fetuin inhibited the insulin rece…

Sequence analysisMolecular Sequence DataBiochemistryTropomyosin receptor kinase CReceptor tyrosine kinaseSubstrate SpecificityComplementary DNASequence Homology Nucleic AcidAnimalsAmino Acid SequencePhosphorylationchemistry.chemical_classificationbiologyBase SequenceDNAProtein-Tyrosine KinasesFetuinMolecular biologyReceptor InsulinAmino acidRatsInsulin receptorBiochemistrychemistryROR1biology.proteinalpha-FetoproteinsEuropean journal of biochemistry
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Isolation, sequence analysis and characterization of cDNA clones coding for the C chain of mouse C1q. Sequence similarity of complement subcomponent …

1992

A mouse macrophage lambda gt11 cDNA library was screened using a genomic DNA clone coding for the C-chain gene of human C1q. Approximately 600,000 recombinant phage plaques were hybridized with peroxidase-labeled human C-chain probe and detected by enhanced chemiluminescence. Five positive clones were obtained. The size of the full-length cDNA is 1019 bp. The sequence identity of the nucleotide sequence with human C1q C chain is 79%, the identity of the deduced amino acid sequences is 73%. The mouse C1q C chain exhibits the same structural features as the human C chain, e.g. conservation of the cysteine residues. Like the mouse A chain, the mouse C chain has an RGD sequence that may be reco…

Sequence analysisMolecular Sequence DataNerve Tissue ProteinsSequence alignmentBiologyBiochemistrylaw.inventionMicelawComplementary DNAAnimalsHumansTissue DistributionAmino Acid SequenceRNA MessengerProtein PrecursorsGeneComplement C1qConserved SequenceBase SequenceSequence Homology Amino AcidcDNA libraryComplement C1qMacrophagesNucleic acid sequenceNucleic Acid HybridizationDNABlotting NorthernMolecular biologyRecombinant DNACollagenEuropean Journal of Biochemistry
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