Search results for "isoforms"

showing 10 items of 185 documents

Expression of fibronectin splice variants and oncofetal glycosylated fibronectin in the synovial membranes of patients with rheumatoid arthritis and …

2002

The aim of this study was to define and compare the expression of fibronectin (Fn) isoforms in synovial tissue of patients with rheumatoid arthritis (RA) and osteoarthritis (OA).Using monoclonal antibodies specific for total Fn, extra domain (ED)-A Fn, ED-B Fn, and oncofetal glycosylated Fn, we studied the expression of the Fn isoforms in synovium. Furthermore, in situ hybridization for the detection of ED-B Fn mRNA including a double labeling technique for the detection of cell type was applied.Strong expression of total Fn, ED-A Fn, oncofetal glycosylated Fn and, to a lesser extent, ED-B Fn could be demonstrated in the synovial lining layer in both RA and OA. Stromal and vessel expression…

Gene isoformmedicine.medical_specialtyPathologyImmunologyOsteoarthritisArthritis RheumatoidRheumatologyInternal medicineImmunopathologyOsteoarthritismedicineHumansProtein IsoformsImmunology and AllergyRNA MessengerAutoimmune diseasebiologybusiness.industrySynovial MembraneAntibodies Monoclonalmedicine.diseaseImmunohistochemistryRheumatologyFibronectinsFibronectinAlternative Splicingmedicine.anatomical_structureRheumatoid arthritisbiology.proteinSynovial membranebusinessRheumatology International
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Influence of muscle strength and total work on exercise-induced plasma growth hormone isoforms in women

2003

The purpose of this investigation was to determine the influence of physical strength and the ability to do more total work on human growth hormone (GH) variants to a heavy resistance exercise protocol in untrained women. From a distribution of 100 healthy, untrained women, the strongest 10 women (S) and the weakest 10 women (W) were compared for GH responses pre- and post an acute heavy resistance exercise test (AHRET, 6 sets of 10 RM squats, 2 minutes rest between sets). Blood samples were obtained pre-exercise and immediately post-exercise and subsequently analysed in total as well as fractionated by Sephacryl S-100R column chromatography into three molecular weight size classes: fractio…

Gene isoformmedicine.medical_specialtyTotal workWeight LiftingPhysical Therapy Sports Therapy and RehabilitationFraction (chemistry)Physical strengthRats Sprague-DawleyPlasma growth hormoneInternal medicinemedicineAnimalsHumansProtein IsoformsBioassayOrthopedics and Sports MedicineExercise physiologyMuscle SkeletalExerciseTibiaChemistryRatsEndocrinologyGrowth HormonePhysical EnduranceBiological AssayFemaleMass fractionJournal of Science and Medicine in Sport
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Expression of retinoic acid nuclear receptors in the mouse embryonal carcinoma cell line PCC7-Mz1

1992

Mouse embryonal carcinoma cell line PCC7-Mz1 can serve as a model of mammalian neural development [1989, J. Cell. Biol. 109, 2481-2493]. Upon exposure to all-trans retinoic acid (RA), Mz1 cells differentiate into a stable pattern of neurons, astroglia and fibroblasts whereas variants of the parental cell line either are restricted in their patterns of derivatives or do not respond at all to RA. Using gene probes specific for the alpha 1, alpha 2 and beta 2 isoforms of the retinoic acid nuclear receptor, we have studied by Northern blot analysis the expression of these transcription factors in uninduced and induced cells of clone Mz1 and in variants with different developmental potential. al…

Gene isoformmedicine.medical_specialtyTranscription GeneticReceptors Retinoic AcidCellular differentiationBiophysicsRetinoic acidTretinoinExpressionBiologyEmbryonic carcinoma cell line PCC7-MzBiochemistryEmbryonal carcinomaMicechemistry.chemical_compoundStructural BiologyInternal medicineTumor Cells CulturedGeneticsmedicineAnimalsRNA MessengerNorthern blotMolecular BiologyCell NucleusdbcAMPTeratomaRetinoic acid receptorCell DifferentiationCell BiologyBlotting Northernmedicine.diseaseCell biologyRetinoic acid receptorEndocrinologyBucladesineNuclear receptorchemistryCell cultureRNACarrier ProteinsPoly AIsoformsFEBS Letters
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Claudin-18 gene structure, regulation, and expression is evolutionary conserved in mammals

2011

Claudin-18 isoform 2 (CLDN18.2) is one of the few members of the human claudin family of tight junction molecules with strict restriction to one cell lineage. The objective of the current study was to compare molecular structure and tissue distribution of this gastrocyte specific molecule in mammals. We show here that the CLDN18.2 protein sequence is highly conserved, in particular with regard to functionally relevant domains in mouse, rat, rabbit, dog, monkey and human and also in lizards. Moreover, promoter regions of orthologs are highly homologous, including the binding site of the transcription factor cyclic AMP-responsive element binding protein (CREB), which is known to regulate acti…

Gene isoformmiceMolecular Sequence DataGene Expressionmolecular structureMammals/geneticsBiologyphylogenyRATSConserved sequenceEvolution MolecularDogsProtein Isoforms/geneticsSequence Homology Nucleic AcidGene expressionGeneticsProtein IsoformsAnimalsTissue DistributionAmino Acid SequenceMembrane Proteins/geneticsBinding sitePromoter Regions GeneticClaudinGeneTranscription factorConserved SequenceGastric Mucosa/metabolismMammalsRegulation of gene expressionGeneticsBinding SitesBase SequenceStomachStomach/cytologyMembrane ProteinsCREB-Binding Protein/metabolismHaplorhiniGeneral MedicineCREB-Binding ProteinGene Expression RegulationGastric MucosaOrgan SpecificityMultigene FamilyClaudinsRabbitsGene
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Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform enc…

2004

The conversion into abnormally folded prion protein (PrP) plays a key role in prion diseases. PrP(C) carries two N-linked glycan chains at amino acid residues 180 and 196 (mouse). Previous in vitro data indicated that the conversion process may not require glycosylation of PrP. However, it is conceivable that these glycans function as intermolecular binding sites during the de novo infection of cells on susceptible organisms and/or play a role for the interaction of both PrP isoforms. Such receptor-like properties could contribute to the formation of specific prion strains. However, in earlier studies, mutations at the glycosylation sites of PrP led to intracellular trafficking abnormalitie…

Genetically modified mouseGlycanGlycosylationGlycosylationPrionsanimal diseasesBovine spongiform encephalopathyMutantBlotting WesternScrapieMice TransgenicCHO CellsCell SeparationBiologyBiochemistryCell LinePrion Diseaseschemistry.chemical_compoundMicePolysaccharidesCell Line TumorCricetinaemedicineAnimalsImmunoprecipitationProtein IsoformsBiotinylationDisulfidesTransgenesCloning MolecularMolecular BiologyBinding SitesWild typeBrainCell Biologymedicine.diseaseFlow CytometryVirologyMolecular biologyIn vitronervous system diseasesEncephalopathy Bovine SpongiformMice Inbred C57BLchemistryMutationbiology.proteinCattleScrapieThe Journal of biological chemistry
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Usher syndrome: molecular links of pathogenesis, proteins and pathways.

2006

Contains fulltext : 50437.pdf (Publisher’s version ) (Closed access) Usher syndrome is the most common form of deaf-blindness. The syndrome is both clinically and genetically heterogeneous, and to date, eight causative genes have been identified. The proteins encoded by these genes are part of a dynamic protein complex that is present in hair cells of the inner ear and in photoreceptor cells of the retina. The localization of the Usher proteins and the phenotype in animal models indicate that the Usher protein complex is essential in the morphogenesis of the stereocilia bundle in hair cells and in the calycal processes of photoreceptor cells. In addition, the Usher proteins are important in…

Genetics and epigenetic pathways of disease [NCMLS 6]Usher syndromeCell Cycle ProteinsNerve Tissue ProteinsBiologyRetinaAdherens junctionMiceHair Cells AuditoryCell polarityGeneticsmedicineotorhinolaryngologic diseasesNeurosensory disorders [UMCN 3.3]AnimalsHumansProtein IsoformsCell Cycle ProteinMolecular BiologyGenetics (clinical)Renal disorder [IGMD 9]Adaptor Proteins Signal TransducingStereociliumMembrane ProteinsSignal transducing adaptor proteinGeneral MedicineActin cytoskeletonmedicine.diseaseeye diseasesCell biologyCytoskeletal ProteinsGenetic defects of metabolism [UMCN 5.1]Ear InnerMultiprotein ComplexesCateninSynapsessense organsUsher SyndromesPhotoreceptor Cells Vertebrate
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Hepatitis B subviral envelope particles use the COPII machinery for intracellular transport via selective exploitation of Sec24A and Sec23B

2020

Hepatitis B virus (HBV) is a leading cause of liver disease. Its success as a human pathogen is related to the immense production of subviral envelope particles (SVPs) contributing to viral persistence by interfering with immune functions. To explore cellular pathways involved in SVP formation and egress, we investigated host-pathogen interactions. Yeast-based proteomics revealed Sec24A, a component of the coat protein complex II (COPII), as an interaction partner of the HBV envelope S domain. To understand how HBV co-opts COPII as a proviral machinery, we studied roles of key Sec proteins in HBV-expressing liver cells. Silencing of Sar1, Sec23, and Sec24, which promote COPII assembly conco…

Hepatitis B virusImmunology610 MedizinVesicular Transport ProteinsBiologymedicine.disease_causeProteomicsEndoplasmic ReticulumMicrobiologyCell Line03 medical and health sciencesDownregulation and upregulationTranscription (biology)610 Medical sciencesVirologyddc:570medicineGene silencingHumansProtein IsoformsSecretionRNA Small InterferingCOPII030304 developmental biologyHepatitis B virus0303 health sciences030306 microbiologyEndoplasmic reticulumBiological TransportHepatitis Bdiseases infection microbe–cell interaction proteomics virusesCell biologyHost-Pathogen InteractionsHepatocytesCOP-Coated Vesicles
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Post-translational modifications in the survival motor neuron protein

2004

Spinal muscular atrophy (SMA) is an autosomal recessive disease characterized by a progressive loss of the spinal motoneurons. The SMA-determining gene has been termed survival motor neuron (SMN) and is deleted or mutated in over 98% of patients. The encoded gene product is a protein expressed as different isoforms. In particular, we showed that the rat SMN cDNA produces two isoforms with Mr of 32 and 35 kDa, both localized in nuclear coiled bodies, but the 32 kDa form is also cytoplasmic, whereas the 35 kDa form is also microsomal. To determine the molecular relationship between these two isoforms and potential post-translational modifications, we performed transfection experiments with a …

INVOLVEMENTFORMSPRODUCTBiochemistryMiceChlorocebus aethiopsProtein IsoformsPhosphorylationCyclic AMP Response Element-Binding ProteinSMN PROTEINCells CulturedMotor NeuronsSPINAL MUSCULAR-ATROPHYRNA-Binding ProteinsSMN Complex Proteins3T3 CellsTransfectionmedicine.anatomical_structureSpinal CordCOS CellsSUBCELLULAR-LOCALIZATIONEXPRESSIONGene isoformRecombinant Fusion ProteinsBiophysicsNerve Tissue ProteinsBiologyMuscular Atrophy SpinalGene productSMN Complex ProteinsComplementary DNAmedicineAnimalsHumansMolecular BiologyCell BiologySpinal muscular atrophyMotor neuronmedicine.diseaseSurvival of Motor Neuron 1 ProteinMolecular biologyRatsnervous system diseasesMolecular WeightSEVERITYnervous systemBODIESProtein Processing Post-TranslationalDETERMINING GENEImmunostainingBiochemical and Biophysical Research Communications
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β1D Integrin Inhibits Cell Cycle Progression in Normal Myoblasts and Fibroblasts

1998

Integrins are alphabeta heterodimeric transmembrane receptors involved in the regulation of cell growth and differentiation. The beta1 integrin subunit is widely expressed in vivo and is represented by four alternatively spliced cytoplasmic domain isoforms. beta1D is a muscle-specific variant of beta1 integrin and a predominant beta1 isoform in striated muscles. In the present study we showed that expression of the exogenous beta1D integrin in C2C12 myoblasts and NIH 3T3 or REF 52 fibroblasts inhibited cell proliferation. Unlike the case of the common beta1A isoform, adhesion of beta1D-transfected C2C12 myoblasts specifically via the expressed integrin did not activate mitogen-activated pro…

IntegrinsRecombinant Fusion ProteinsMolecular Sequence DataIntegrinSignal transductionTransfectionCell adhesion; Integrins; Signal transduction; Alternative splicing isoforms; Cell proliferation; MyodifferentiationBiochemistryCD49cCell LineCollagen receptorMiceAlternative splicing isoformsCell surface receptorAnimalsAmino Acid SequenceMuscle SkeletalMolecular BiologyCell proliferationMyodifferentiationbiologyCell growthIntegrin beta1Cell CycleCell adhesionCell DifferentiationReceptors Interleukin-2Cell BiologyImmunohistochemistryMolecular biologyCell biologyEnzyme ActivationProto-Oncogene Proteins c-rafAlternative SplicingGenes rasIntegrin alpha MCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinIntegrin beta 6C2C12Journal of Biological Chemistry
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Maturation of epidermal Langerhans cells: increased expression of beta- and gamma-actin isoforms as a basis of specialized cell functions.

1999

Epidermal Langerhans cells (LC) represent immature dendritic cells. During in vitro culture in the presence of keratinocytes they mature into potent immunostimulatory cells for naive T cells. This process is thought to simulate in vivo maturation of LC following activation by antigen contact. Maturation of LC is accompanied by morphological alterations. Applying a differential screening procedure we isolated differentially expressed cDNAs involved in the maturation events including cDNAs of the cytoskeletal actin isoforms beta- and gamma-actin. Stronger signals with hybridization probes derived from cultured LC compared with probes derived from freshly isolated LC indicate upregulation of a…

Langerhans cellDNA ComplementaryPhalloidinmacromolecular substancesDermatologyBiologyIn Vitro TechniquesBiochemistrychemistry.chemical_compoundMiceWestern blotmedicineAnimalsProtein IsoformsNorthern blotRNA MessengerCytoskeletonMolecular BiologyActinDNA PrimersMice Inbred BALB Cmedicine.diagnostic_testEpidermis (botany)Base SequenceReverse Transcriptase Polymerase Chain ReactionCell DifferentiationDendritic cellDendritic CellsActinsCell biologyUp-Regulationmedicine.anatomical_structurechemistryLangerhans CellsExperimental dermatology
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