Search results for "messenger"

showing 10 items of 1493 documents

Expression of Transketolase-like 1 and Activation of Akt in Grade IV Glioblastomas Compared With Grades II and III Astrocytic Gliomas

2008

Transketolases link the Embden-Meyerhof pathway to the pentose phosphate pathway. An influence of p-Akt on this metabolism was described. This study was performed to compare the expression of transketolase-like 1 (TKTL1) and p-Akt in glioblastoma multiforme (GBM) and other astrocytic gliomas (AGs, grades II and III). We analyzed 15 GBMs, 15 AGs (grade II), and 3 normal brain samples for TKTL1 expression by semiquantitative reverse transcription–polymerase chain reaction and Western blotting and 23 GBMs, 9 grade III AGs, and 7 grade II AGs immunohistochemically (TKTL1 and p-Akt). On the protein level, TKTL1 was significantly overexpressed in tumors. Immunohistochemically, the tumor grade sig…

Pathologymedicine.medical_specialtyAstrocytomaGeneral MedicineMetabolismAstrocytomaPentose phosphate pathwayTransketolaseBiologymedicine.diseaseEnzyme assayUp-RegulationEnzyme ActivationGene Expression Regulation NeoplasticBlotmedicinebiology.proteinCancer researchHumansGlycolysisRNA MessengerTransketolaseGlioblastomaProto-Oncogene Proteins c-aktProtein kinase BAmerican Journal of Clinical Pathology
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Expression of HIP/PAP mRNA in Human Hepatoma Cell Lines

2002

The present study attempts to shed more light on the role of hepatocarcinoma-intestine-pancreas/pancreatic associated protein (HIP/PAP) in hepatoma cells. We initially examined, by reverse transcription-polymerase chain reaction (RT-PCR), the HIP/PAP transcripts present in human hepatoma cell lines of different origins and with different grades of differentiation and genetic profiles. We also used DNA sequencing analysis to investigate the structure of the HIP/PAP gene. Further investigation is necessary to define the role of HIP/PAP during the development of human hepatocellular carcinoma and to ascertain whether the use of different transcripts is helpful in regulating HIP/PAP expression …

Pathologymedicine.medical_specialtyCarcinoma HepatocellularSettore MED/09 - Medicina InternaPancreatitis-Associated ProteinscarcinomaGeneral Biochemistry Genetics and Molecular BiologyHistory and Philosophy of ScienceAntigenAntigens NeoplasmHIP/PAPBiomarkers TumorTumor Cells CulturedmedicineCarcinomaHumansNeoplasmLectins C-TypeRNA MessengerPancreatitis-Associated ProteinsN-Glycosyl HydrolasesGenePlant ProteinsMessenger RNAbusiness.industryGeneral NeuroscienceLiver NeoplasmsAcute-phase proteinpancreatitihepatomamedicine.diseasePancreatitisHepatocellular carcinomaRibosome Inactivating Proteins Type 1Cancer researchproteinbusinessAcute-Phase ProteinsAnnals of the New York Academy of Sciences
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Coexpression of extracellular matrix glycoproteins undulin and tenascin in human autosomal dominant polycystic kidney disease.

1993

Autosomal dominant polycystic kidney disease (ADPKD) is the most common entity of cystic diseases of the kidney leading to end-stage renal insufficiency. Changes in extracellular matrix (ECM) are regarded to be an important pathogenic factor connected with the genes assumed to be responsible for human ADPKD. In order to assess the biological significance of altered expression and deposition of ECM glycoproteins for human ADPKD at molecular levels fresh-frozen tissue from ADPKD kidneys, fetal kidneys and normal adult kidneys were comparatively tested by immunohistochemistry for the presence of multifunctional ECM glycoproteins undulin, tenascin and fibronectin, interstitial collagen types I,…

Pathologymedicine.medical_specialtyCell Adhesion Molecules NeuronalAutosomal dominant polycystic kidney diseaseTenascinGene ExpressionKidneyExtracellular matrixFetusLamininTransforming Growth Factor betamedicineHumansRNA MessengerCells CulturedGlycoproteinsBasement membraneKidneyExtracellular Matrix Proteinsbiologyurogenital systemTenascinmedicine.diseasePolycystic Kidney Autosomal DominantImmunohistochemistryEpitheliumCell biologyFibronectinsFibronectinmedicine.anatomical_structurebiology.proteinCollagenLamininNephron
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Metalloprotease meprin beta in rat kidney: glomerular localization and differential expression in glomerulonephritis

2008

Meprin (EC 3.4.24.18) is an oligomeric metalloendopeptidase found in microvillar membranes of kidney proximal tubular epithelial cells. Here, we present the first report on the expression of meprin beta in rat glomerular epithelial cells and suggest a potential involvement in experimental glomerular disease. We detected meprin beta in glomeruli of immunostained rat kidney sections on the protein level and by quantitative RT-PCR of laser-capture microdissected glomeruli on the mRNA level. Using immuno-gold staining we identified the membrane of podocyte foot processes as the main site of meprin beta expression. The glomerular meprin beta expression pattern was altered in anti-Thy 1.1 and pas…

Pathologymedicine.medical_specialtyNephrology/Acute Renal Failure10039 Institute of Medical GeneticsKidney GlomerulusFluorescent Antibody Techniquelcsh:MedicinePodocyte foot610 Medicine & health1100 General Agricultural and Biological SciencesBiologyurologic and male genital diseasesHeymann NephritisGlomerulonephritisWestern blot1300 General Biochemistry Genetics and Molecular BiologymedicineAnimalsRNA MessengerMicroscopy Immunoelectronlcsh:ScienceKidneyMetalloproteinase1000 MultidisciplinaryMultidisciplinarymedicine.diagnostic_testPodocytesReverse Transcriptase Polymerase Chain Reactionurogenital systemImmune Seralcsh:RNephrology/Chronic Kidney DiseaseMetalloendopeptidasesGlomerulonephritismedicine.diseaseMolecular biologyRats Inbred F344Ratsmedicine.anatomical_structureRats Inbred Lew570 Life sciences; biologylcsh:QNephritisImmunostainingResearch Article
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Prognostic significance of c-erB-2 mRNA in ovarian carcinoma.

1996

The oncogene specific mRNA of c-erbB-2 was detected by the S1 nuclease protection assay in 95 ovarian cancer specimens. In 79 primary carcinomas, we found 16 (20%) with strong expression, 13 (17%) with weak expression, 4 (5%) with very weak expression, and 46 (58%) with no expression. In 3 of 16 recurrencies (19%) a strong expression of c-erbB-2 mRNA was detected, in 2 (12%) weak expression was detected, and in 11 (69%) no expression of c-erbB-2 mRNA was detected. Kaplan-Meier analysis revealed no significant association between strong expression of c-erbB-2 mRNA and survival of the 79 patients with primary cancer. However, in the subgroup of patients with FIGO (International Federation of …

Pathologymedicine.medical_specialtySerous carcinomaReceptor ErbB-2OvaryAndrologyPredictive Value of TestsOvarian carcinomamedicineCarcinomaHumansRNA MessengerRNA NeoplasmStage (cooking)neoplasmsNeoplasm StagingOvarian NeoplasmsMessenger RNAOncogenebusiness.industryObstetrics and Gynecologymedicine.diseasePrognosisSurvival AnalysisUp-RegulationGene Expression Regulation Neoplasticmedicine.anatomical_structureOncologyFemaleOvarian cancerbusinessGynecologic oncology
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KLEIP Deficiency in Mice Causes Progressive Corneal Neovascular Dystrophy

2012

PURPOSE. The BTB-kelch protein KLEIP/KLHL20 is an actin binding protein that regulates cell-cell contact formation and cell migration. The aim of our study was to characterize KLEIP’s function in ocular health and disease in mice. METHODS. KLEIP -/- mice were generated, and corneas were examined histologically and stained for keratin-1, loricrin, keratin-12, keratin-14, CD31, LYVE-1, F4/80, E-cadherin, and Ki67. Corneal abrasions were performed after eyelid opening. RESULTS. Corneas of KLEIP þ/þ and KLEIP -/- mice were indistinguishable at birth. After eyelid opening corneal epithelial hyperplasia started to manifest in KLEIP -/- mice, showing a progressive epithelial metaplasia leading to …

Pathologymedicine.medical_specialtyStromal cellGenotypeMice TransgenicCorneal dystrophyReal-Time Polymerase Chain ReactionCorneaMiceCorneal OpacityCorneamedicineAnimalsCorneal NeovascularizationRNA MessengerAdaptor Proteins Signal TransducingCorneal epitheliumintegumentary systembusiness.industryDystrophymedicine.diseaseeye diseasesEpitheliumMice Inbred C57BLDisease Models Animalmedicine.anatomical_structureGene Expression RegulationDisease ProgressionEpithelial MetaplasiaLoricrinsense organsCarrier ProteinsbusinessInvestigative Opthalmology & Visual Science
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C-myc mRNA Expression in Epithelial Ovarian Carcinomas in Relation to Estrogen Receptor Status, Metastatic Spread, Survival Time, FIGO Stage, and His…

1998

Recently, it has been suggested that c-myc expression might correlate with estrogen receptor (ER) status and metastatic spread in ovarian cancer. In this study, expression of c-myc mRNA in 90 epithelial ovarian carcinomas was determined using the S1 nuclease protection assay. Expression of c-myc mRNA was detectable in 27 of 90 tumors. There was no significant association between c-myc mRNA expression and metastatic spread, survival time, FIGO stage, or histologic grade and type. C-myc mRNA was expressed in 45% of ER-positive tumors but only 24% of ER-negative tumors (p = 0.094; Fisher's exact test). Similarly, 44% of progesterone receptor (PR)-positive and 23% of PR-negative tumors expresse…

Pathologymedicine.medical_specialtymedicine.drug_class10050 Institute of Pharmacology and ToxicologyEstrogen receptor610 Medicine & healthOvaryBiologyPathology and Forensic MedicineMetastasisProto-Oncogene Proteins c-mycProgesterone receptormedicineHumansRNA MessengerRNA NeoplasmSurvival rateEstrogen Receptor StatusOvarian NeoplasmsCarcinomaObstetrics and Gynecology2729 Obstetrics and Gynecologymedicine.diseaseSurvival Rate2734 Pathology and Forensic Medicinemedicine.anatomical_structureReceptors EstrogenEstrogen570 Life sciences; biologyFemaleReceptors ProgesteroneOvarian cancerInternational Journal of Gynecological Pathology
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Primary structure and unusual carbohydrate moiety of functional unit 2-c of keyhole limpet hemocyanin (KLH)

1999

Abstract The complete amino acid sequence of the Megathura crenulata hemocyanin functional unit KLH2-c was determined by direct sequencing and matrix-assisted laser desorption ionization mass spectrometry of the protein, and of peptides obtained by cleavage with EndoLysC proteinase, chymotrypsin and cyanogen bromide. This is the first complete primary structure of a functional unit c from a gastropod hemocyanin. KLH2-c consists of 420 amino acid residues. Circular dichroism spectra indicated approx. 31% β-sheet and 29% α-helix contents. A multiple sequence alignment with other molluscan hemocyanin functional units revealed average identities between 41 and 49%, but 55% in case of Octopus he…

Peanut agglutininmedicine.medical_treatmentMolecular Sequence DataCarbohydratesBiophysicschemical and pharmacologic phenomenaMegathura crenulataBiochemistrychemistry.chemical_compoundStructural BiologymedicineAnimalsChymotrypsinAmino Acid SequenceRNA MessengerMolecular BiologyPeptide sequenceChromatography High Pressure LiquidbiologyMolecular massCircular DichroismProtein primary structureHemocyaninbiology.organism_classificationMolecular WeightBiochemistrychemistryMolluscaSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationHemocyaninsbiology.proteinElectrophoresis Polyacrylamide GelCyanogen bromideSequence AlignmentKeyhole limpet hemocyaninBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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A FRET-based assay for characterization of alternative splicing events using peptide nucleic acid fluorescence in situ hybridization

2009

We describe a quantitative method for detecting RNA alternative splicing variants that combines in situ hybridization of fluorescently labeled peptide nucleic acid (PNA) probes with confocal microscopy Förster resonance energy transfer (FRET). The use of PNA probes complementary to sequences flanking a given splice junction allows to specifically quantify, within the cell, the RNA isoform generating such splice junction by FRET measure. As a proof of concept we analyzed two alternative splicing events originating from lymphocyte antigen 6 (LY6) complex, locus G5B (LY6G5B) pre-mRNA. These are characterized by the removal of the first intron (Fully Spliced Isoform, FSI) or by retention of suc…

Peptide Nucleic AcidsGene isoformCytoplasmIn situ hybridizationBiologychemistry.chemical_compoundFluorescence Resonance Energy TransferGeneticsmedicineHumansProtein IsoformsspliceRNA MessengerIn Situ Hybridization FluorescenceMicroscopy ConfocalPeptide nucleic acidmedicine.diagnostic_testAlternative splicingIntronPepsin AAlternative SplicingNucleic Acid ProbesFörster resonance energy transferBiochemistrychemistryBiophysicsMethods OnlineCell NucleolusHeLa CellsFluorescence in situ hybridizationNucleic Acids Research
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The analysis of modified peroxisome proliferator responsive elements of the peroxisomal bifunctional enzyme in transfected HepG2 cells reveals two re…

1995

AbstractPeroxisome proliferators (PPs) are non-genotoxic carcinogens in rodents. They can induce the expression of numerous genes via the heterodimerization of two members of the steroid hormone receptor superfamily, called the peroxisome proliferator-activated receptor (PPAR) and the 9-cis retinoic acid receptor (RXR). Many of the PP responsive genes possess a peroxisome proliferator response element (PPRE) formed by two TGACCT-related motifs. The bifunctional enzyme (HD) PPRE contains 3 such motifs, creating DR1 and DR2 sequences. PPAR and RXR regulate transcription via the DR1 element while DR2 modulates the expression of the gene via auxiliary factors in HepG2 cells.

Peroxisome proliferator-activated receptor gammaReceptors Retinoic AcidSteroid hormone receptorMolecular Sequence DataResponse elementBiophysicsReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorchemical and pharmacologic phenomenaIn Vitro TechniquesRegulatory Sequences Nucleic AcidRetinoid X receptorBiologyPeroxisomal Bifunctional EnzymeTransfectionMicrobodiesBiochemistryGene Expression Regulation EnzymologicTranscriptional activationPeroxisomal Bifunctional EnzymeMultienzyme ComplexesStructural BiologyPeroxisome proliferator response element9-cis Retinoic acid receptor alphaTumor Cells CulturedGeneticsHumansRNA MessengerIsomerasesEnoyl-CoA HydrataseMolecular Biologychemistry.chemical_classificationBinding SitesBase Sequence3-Hydroxyacyl CoA DehydrogenasesPeroxisome proliferator-activated receptorCell BiologyDNA-Binding ProteinsRetinoic acid receptorRetinoid X ReceptorsLiverOligodeoxyribonucleotidesBiochemistrychemistryRat peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenaseEnzyme InductionPeroxisome proliferator-activated receptor alphaTranscription FactorsFEBS Letters
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