Search results for "Splicing"

showing 10 items of 235 documents

Receptor for advanced glycation end products is subjected to protein ectodomain shedding by metalloproteinases.

2008

The receptor for advanced glycation end products (RAGE) is a 55-kDa type I membrane glycoprotein of the immunoglobulin superfamily. Ligand-induced up-regulation of RAGE is involved in various pathophysiological processes, including late diabetic complications and Alzheimer disease. Application of recombinant soluble RAGE has been shown to block RAGE-mediated pathophysiological conditions. After expression of full-length RAGE in HEK cells we identified a 48-kDa soluble RAGE form (sRAGE) in the culture medium. This variant of RAGE is smaller than a 51-kDa soluble version derived from alternative splicing. The release of sRAGE can be induced by the phorbol ester PMA and the calcium ionophore c…

endocrine system diseasesADAM10Receptor for Advanced Glycation End ProductsMatrix Metalloproteinase InhibitorsHydroxamic AcidsBiochemistryProtein biotinylationCell LineDiabetes ComplicationsADAM10 ProteinGlycationAlzheimer DiseaseHumansProtein IsoformsProtease Inhibitorscardiovascular diseasesRNA Small InterferingReceptors ImmunologicReceptorMolecular BiologyProtein kinase CCalcimycinIonophoresChemistryHEK 293 cellsCell Membranenutritional and metabolic diseasesMembrane ProteinsCell BiologyProtein Structure TertiaryADAM ProteinsAlternative SplicingEctodomainBiochemistryMatrix Metalloproteinase 9cardiovascular systemCarcinogensImmunoglobulin superfamilyTetradecanoylphorbol AcetateAmyloid Precursor Protein Secretaseshuman activitiesThe Journal of biological chemistry
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A novel splice acceptor site mutation in the ATP2A2 gene in a family with Darier disease

2016

This study identifies a novel spice site mutation in the ATP2A gene in a family with the Darier disease

gene ATP2A2 splicing site mutation Darier
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The Interaction Mechanism of Intrinsically Disordered PP2A Inhibitor Proteins ARPP-16 and ARPP-19 With PP2A

2021

Protein phosphatase 2A (PP2A) activity is critical for maintaining normal physiological cellular functions. PP2A is inhibited by endogenous inhibitor proteins in several pathological conditions including cancer. A PP2A inhibitor protein, ARPP-19, has recently been connected to several human cancer types. Accordingly, the knowledge about ARPP-19—PP2A inhibition mechanism is crucial for the understanding the disease development and the therapeutic targeting of ARPP-19—PP2A. Here, we show the first structural characterization of ARPP-19, and its splice variant ARPP-16 using NMR spectroscopy, and SAXS. The results reveal that both ARPP proteins are intrinsically disordered but contain transient…

macromolecular substancesIntrinsically disordered proteinsBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistryenvironment and public healthProtein–protein interactionprotein-protein interaction03 medical and health sciences0302 clinical medicineNMR spectroscopyIDPSARPP-16Molecular BiosciencesARPP-19NMR-spektroskopialcsh:QH301-705.5Molecular BiologyProtein secondary structure030304 developmental biologyOriginal Researchsoluviestintä0303 health sciencesMicroscale thermophoresisChemistryAlternative splicingInhibitor proteinProtein phosphatase 2Nuclear magnetic resonance spectroscopySAXS3. Good healthPP2APP2A inhibitor proteinssyöpäsolutlcsh:Biology (General)Biophysicsintrinsically disordered proteinsproteiinit030217 neurology & neurosurgery
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Expression of Wild-Type and Variant Estrogen Receptor Alpha in Liver Carcinogenesis and Tumor Progression.

2011

Although estrogen receptors (ERs) are expressed in human hepatocellular carcinoma (HCC), several clinical trials have failed to demonstrate the efficacy of antiestrogen treatment in HCC patients. Recently, the identification of several ER splicing variants has enlightened the complex nature of estrogen signaling in peripheral tissues; this may help understanding estrogen role in either nontumoral or malignant nonclassical target organs, including liver. In this work we have investigated mRNA expression of wild-type and splice variants of ERα in nontumoral, cirrhotic, and malignant human liver, as well as in HCC cell lines, using an exon-specific reverse transcription polymerase chain reacti…

medicine.medical_specialtyCarcinoma Hepatocellularmedicine.drug_classEstrogen receptorBiologyBiochemistryAromataseCell Line TumorInternal medicineGene OrderGeneticsmedicineHumansRNA MessengerneoplasmsMolecular BiologyLiver NeoplasmsEstrogen Receptor alphaWild typeExonsHep G2 Cellsmedicine.diseaseAntiestrogenGene Expression Regulation NeoplasticReverse transcription polymerase chain reactionAlternative SplicingCell Transformation NeoplasticEndocrinologyLiverEstrogenTumor progressionHepatocellular carcinomaCancer researchMolecular MedicineEstrogen receptor alphaLiver carcinogenesis Estrogen receptors tumor progressionBiotechnology
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Expression and cellular localization of kininogens in the human kidney

1996

Expression and cellular localization of kininogens in the human kidney. Human high (H) and low (L) molecular weight kininogens are encoded by distinct mRNAs derived by alternative splicing from a single kininogen gene. Previous studies have demonstrated the presence of L-kininogen but not of H-kininogen in the distal nephron structures of the kidney. Using the highly sensitive reverse trancriptase-polymerase chain reaction (RT-PCR) we have been able to demonstrate the expression of both H-kininogen mRNA and L-kininogen mRNA in kidney and liver. The presence of H- and L-kininogen antigen was shown immunohistochemically by applying specific antibodies that discriminate between the two types o…

medicine.medical_specialtyMolecular Sequence DataBiologyKidneyPolymerase Chain ReactionInternal medicinemedicineHumansAmino Acid SequenceRNA MessengerCellular localizationKidneyMessenger RNAKininogenKininogensurogenital systemAlternative splicingKidney metabolismKallikreinImmunohistochemistryCell biologymedicine.anatomical_structureEndocrinologyNephrologyImmunohistochemistrycirculatory and respiratory physiologyKidney International
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Regulation of PTHrP and PTH/PTHrP receptor by extracellular Ca2+ concentration and hormones in the breast cancer cell line 8701-BC.

2000

AbstractIt was previously reported that 8701-BC breast tumour cells express the gene for parathyroid hormonerelated peptide (PTHrP) and PTH/PTHrP receptor (PTHrPR) and release immunoreactive PTHrP (iPTHrP) into the extracellular medium. Since the regulation of PTHrP and PTHrPR by breast cancer cells has been poorly investigated so far, we have chosen the 8701- BC cell line as a model system to investigate whether alterations in the extracellular Ca[2+] concentration ([Ca[2+]]) and treatment with some wellknown differentiation agents for breast cells, such as dimethyl sulfoxide, hydrocortisone, progesterone, prolactin, alltrans retinoic acid and transforming growth factorβ1 might (i) modulat…

medicine.medical_specialtyTranscription GeneticRNA SplicingClinical BiochemistryRetinoic acidCodon InitiatorBreast NeoplasmsTretinoinBiochemistrychemistry.chemical_compoundTranscription (biology)Transforming Growth Factor betaInternal medicinemedicineExtracellularTumor Cells CulturedHumansProtein IsoformsRNA MessengerPromoter Regions GeneticMolecular BiologyGeneChemistryParathyroid Hormone-Related ProteinProteinsProlactinHormonesNeoplasm ProteinsEndocrinologyGene Expression RegulationCell cultureRNA splicingReceptors Parathyroid HormoneCalciumExtracellular Spacehormones hormone substitutes and hormone antagonistsHormoneBiological chemistry
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Descubrimiento y caracterización de la estefenantrina como fármaco para la Distrofia Miotónica Tipo 1

2015

La Distrofia Miotónica tipo 1 (DM1) es una enfermedad autosómica dominante cuyos principales síntomas incluyen miotonía (incapacidad para relajar el músculo tras una contracción voluntaria), degeneración muscular, cataratas, diabetes, arritmias cardiacas y déficit cognitivo entre otros. La causa genética de la enfermedad radica en la expansión del trinucleótido CTG en el extremo 3’ no traducido del gen proteina kinasa de la distrofia miotónica (DMPK). La expansión de este trinucleótido provoca la ganancia de función tóxica del RNA al transcribirse la región expandida. El RNA portador de las expansiones tóxicas de CTG se pliega sobre sí mismo formando una horquilla de doble cadena que queda …

muscleblindsplicingrastreo químicoUNESCO::CIENCIAS DE LA VIDAdrosophila:CIENCIAS DE LA VIDA [UNESCO]
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Expanded CCUG repeat RNA expression in Drosophila heart and muscle trigger Myotonic Dystrophy type 1-like phenotypes and activate autophagocytosis ge…

2016

AbstractMyotonic dystrophies (DM1–2) are neuromuscular genetic disorders caused by the pathological expansion of untranslated microsatellites. DM1 and DM2, are caused by expanded CTG repeats in the 3′UTR of the DMPK gene and CCTG repeats in the first intron of the CNBP gene, respectively. Mutant RNAs containing expanded repeats are retained in the cell nucleus, where they sequester nuclear factors and cause alterations in RNA metabolism. However, for unknown reasons, DM1 is more severe than DM2. To study the differences and similarities in the pathogenesis of DM1 and DM2, we generated model flies by expressing pure expanded CUG ([250]×) or CCUG ([1100]×) repeats, respectively, and compared …

musculoskeletal diseases0301 basic medicinecongenital hereditary and neonatal diseases and abnormalitiesRNA SplicingScienceGene ExpressionBiologyMyotonic dystrophyMyotonin-Protein KinaseArticle03 medical and health sciencesGene expressionAutophagymedicineAnimalsMyotonic DystrophyMuscle SkeletalGeneDNA Repeat ExpansionMultidisciplinaryMyocardiumQRIntronRNAArrhythmias CardiacDNA Repeat Expansionmedicine.diseaseMolecular biologyDisease Models AnimalCell nucleus030104 developmental biologymedicine.anatomical_structureRNA splicingMedicineDrosophilaLocomotionScientific Reports
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Sense and Antisense DMPK RNA Foci Accumulate in DM1 Tissues during Development.

2015

International audience; Myotonic dystrophy type 1 (DM1) is caused by an unstable expanded CTG repeat located within the DMPK gene 3'UTR. The nature, severity and age at onset of DM1 symptoms are very variable in patients. Different forms of the disease are described, among which the congenital form (CDM) is the most severe. Molecular mechanisms of DM1 are well characterized for the adult form and involve accumulation of mutant DMPK RNA forming foci in the nucleus. These RNA foci sequester proteins from the MBNL family and deregulate CELF proteins. These proteins are involved in many cellular mechanisms such as alternative splicing, transcriptional, translational and post-translational regul…

musculoskeletal diseasesCCAAT-Enhancer-Binding Protein-deltacongenital hereditary and neonatal diseases and abnormalities[SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiologylcsh:MedicineMice Transgenic[SDV.GEN.GH] Life Sciences [q-bio]/Genetics/Human genetics[SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyMyotonin-Protein KinaseMice[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]AnimalsHumansMyotonic DystrophyRNA AntisenseRNA Messengerlcsh:ScienceMuscle SkeletalCell NucleusMyocardiumlcsh:R[SDV.NEU.NB] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/NeurobiologyBrainGene Expression Regulation DevelopmentalRNA-Binding Proteins[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyEmbryo MammalianAlternative SplicingDisease Models Animal[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human geneticsAnimals Newborn[SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]lcsh:QTrinucleotide Repeat ExpansionSignal TransductionResearch ArticlePloS one
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Muscleblind, BSF and TBPH are mislocalized in the muscle sarcomere of a Drosophila myotonic dystrophy model

2012

SummaryMyotonic dystrophy type 1 (DM1) is a genetic disease caused by the pathological expansion of a CTG trinucleotide repeat in the 3' UTR of the DMPK gene. In the DMPK transcripts, the CUG expansions sequester RNA-binding proteins into nuclear foci, including transcription factors and alternative splicing regulators such as MBNL1. MBNL1 sequestration has been associated with key features of DM1. However, the basis behind a number of molecular and histological alterations in DM1 remain unclear. To help identify new pathogenic components of the disease, we carried out a genetic screen using a Drosophila model of DM1 that expresses 480 interrupted CTG repeats, i(CTG)480, and a collection of…

musculoskeletal diseasesSarcomerescongenital hereditary and neonatal diseases and abnormalitiesNeuroscience (miscellaneous)lcsh:MedicineMedicine (miscellaneous)RNA-binding proteinGenes InsectBiologyMyotonic dystrophyGeneral Biochemistry Genetics and Molecular BiologyAnimals Genetically Modifiedchemistry.chemical_compoundImmunology and Microbiology (miscellaneous)RNA interferencelcsh:PathologymedicineMBNL1AnimalsDrosophila ProteinsHumansMyotonic DystrophyGeneticsMuscleslcsh:RAlternative splicingNuclear ProteinsRNA-Binding ProteinsEpistasis Geneticmedicine.diseaseDisease Models AnimalchemistryGene Knockdown TechniquesDrosophilaFemaleRNA InterferenceTrinucleotide repeat expansionTrinucleotide Repeat ExpansionDrosophila Proteinlcsh:RB1-214Genetic screenResearch ArticleDisease Models & Mechanisms
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