Search results for "RNase"

showing 10 items of 49 documents

Studies of the expression of the cytochrome P450IA, P450IIB, and P450IIC gene family in extrahepatic and hepatic tissues.

1990

We have studied the expression of three P-450 gene subfamilies in hepatic and extrahepatic tissues using the sensitive RNAse A protection assay. Members of the P450IA subfamily, which encodes the major methylcholanthrene-inducible cytochromes P-450, were found to be not expressed in extrahepatic tissues of untreated animals, raising the question whether these P-450 play a role in the metabolism of carcinogens in unexposed individuals. In contrast, members of the P450IIB family, some of which encode the major phenobarbital-inducible cytochromes P-450, were found to be expressed in some extrahepatic tissues of untreated rats and here most notably in the lung and in sebaceous glands. Members o…

MaleSubfamilyCytochromeRNase PHealth Toxicology and MutagenesisCytochrome P-450 Enzyme SystemCytochrome P-450 CYP1A2Gene familyCytochrome c oxidaseAnimalsTissue DistributionGeneRegulation of gene expressionMessenger RNAbiologyPublic Health Environmental and Occupational HealthRNA ProbesMolecular biologyRatsBiochemistryLiverMultigene Familybiology.proteinFemaleOxidoreductasesResearch ArticleEnvironmental Health Perspectives
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Glutamate cysteine ligase up-regulation fails in necrotizing pancreatitis

2007

Glutathione depletion is a key factor in the development of acute pancreatitis. Our aim was to study the regulation of glutamate cysteine ligase, the rate-limiting enzyme in glutathione synthesis, in edematous or necrotizing pancreatitis in rats. Glutathione levels were kept low in necrotizing pancreatitis for several hours, with no increase in protein or mRNA levels of glutamate cysteine ligase subunits, despite binding of RNA polymerase II to their promoters and coding regions. The survival signal pathway mediated by ERK and c-MYC was activated, and c-MYC was recruited to the promoters. The failure in gene up-regulation seems to be due to a marked increase in cytosolic ribonuclease activi…

MaleTaurocholic AcidMAPK/ERK pathwayRNase PGlutamate-Cysteine LigaseRNA StabilityRNA polymerase IIBiochemistryGene Expression Regulation Enzymologicchemistry.chemical_compoundRibonucleasesTranscription (biology)Physiology (medical)medicineAnimalsEdemaRNA MessengerRibonucleaseRats WistarbiologyPancreatitis Acute NecrotizingNF-κBGlutathionemedicine.diseaseGlutathioneMolecular biologyRatsUp-RegulationPancreatitischemistrybiology.proteinPancreatitisRNA Polymerase IICeruletideTranscription FactorsFree Radical Biology and Medicine
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Inflammation events occurring upon bacterial infection in Mytilus galloprovincialis

2022

Bivalves, and in particular the Mediterranean Mytilus galloprovincialis are important sources of food in several countries in the world. Because of that, mussels farming has a strong economic impact. Due to their status as sessile and filter-feeding animals, bivalves accumulate in their tissues environmental pollutants and a larger amount of microorganisms and between these, a multitude of infective bacteria for higher vertebrates and humans, such as Vibrio species. Several immunological responses of M. galloprovincialis were investigated and described after Vibrio infection both, in vitro and in vivo conditions, such as hemocytes count and different cellular subpopulations. Particularly, i…

Mytilus TLR4 MYD88 AIF1 RNASET2 Vibrio infection
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AIF-1 and RNASET2 are involved in the inflammatory response in the Mediterranean mussel Mytilus galloprovincialis following Vibrio infection

2022

Filter-feeding bivalves, such as the Mytilus species, are exposed to different types of bacteria in the surrounding waters, in particular of the Vibrio genus. Mussels lack an adaptive immune system and hemocytes can recognize pathogen-associated molecular patterns (PAMPs) via pattern recognition receptors (PRRs) to activate intracellular signaling pathways to trigger the antimicrobial effectors synthesis. Among the areas of bivalve immunity that deserve study include the role of hemocyte subpopulations. Since little information are available on immune responses at the tissue level to human pathogenic vibrios commonly detected in coastal waters involved in seafood-borne diseases, in this wor…

MytilusHemocytesTumor Suppressor ProteinsAIF-1 Bacterial challenge Cellular immunity Immunohistochemistrym M. galloprovincialis Myd88 RNASET2 TLR4RNASET2General MedicineAquatic ScienceAIF-1; Bacterial challenge; Cellular immunity; Immunohistochemistry; M. galloprovincialis; Myd88; RNASET2; TLR4Myd88ImmunohistochemistryCellular immunityToll-Like Receptor 4Bacterial challengeRibonucleasesSeafoodVibrio InfectionsMyeloid Differentiation Factor 88Environmental ChemistryAnimalsHumansTLR4M. galloprovincialisAIF-1Vibrio
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(2'-5')Oligoadenylate and intracellular immunity against retrovirus infection.

1992

1. 1. The double-stranded RNA-dependent 2′,5′-oligoadenylate (2–5A) synthetase/ribonuclease L (RNase L) system plays an essential role in the establishment of the antiviral state of a cell exposed to virus infection. 2. 2. Until recently, the application of 2–5A derivatives to reinforce this system seemed to be limited mainly due to the low specificity of RNase L for viral RNA. 3. 3. Two new strategies have been developed which yield a selective antiviral effect of 2–5As at least against human immunodeficiency virus-1 (HIV-1) infection: (i) an “intracellular immunization” appproach using 2-5A synthetase cDNA linked to HIV trans -acting response element (TAR) and (ii) inhibition of retrovira…

OligoribonucleotidesbiologyRNase P2'-5'-OligoadenylateAdenine NucleotidesHIVbiology.organism_classificationVirus ReplicationBiochemistryVirologyMolecular biologyAntiviral AgentsVirusRetrovirusBiochemistryImmunityComplementary DNAbiology.protein2'5'-Oligoadenylate SynthetaseReverse Transcriptase InhibitorsRibonuclease LIntracellularHIV Long Terminal RepeatRetroviridae InfectionsThe International journal of biochemistry
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Real-time Fluorescence Measurement of Enterovirus Uncoating

2019

Viruses need to open, i.e., uncoat, in order to release their genomes for efficient replication and translation. Especially for non-enveloped viruses, such as enteroviruses, the cues leading to uncoating are less well known. The status of the virus has previously been observed mainly by transmission electron microscopy using negative staining, cryo electron microscopy, X-ray crystallography or gradient separation (reviewed in Tuthill et al., 2010, Myllynen et al., 2016, Ruokolainen et al., 2019). However, monitoring of uncoating has been limited by the lack of methods detecting dynamic changes of the virions. Here, we present a real-time fluorescence based protocol, which detects the viral …

PicornavirusRNase PCryo-electron microscopyStrategy and ManagementvirusesspektroskopiainfektiotIndustrial and Manufacturing EngineeringVirusMethods ArticletutkimusmenetelmätRNaseNucleic acid structuregenomeEnterovirusbiologyChemistryMechanical EngineeringSYBR Green IIVirus UncoatingPicornavirusMetals and AlloysfluoresenssiRNAfluorescence spectroscopybiology.organism_classificationNegative stainCell biologyenteroviruksetRNAuncoating
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Identification of disulphide bonds in the refolding of bovine pancreatic RNase A

1996

Background: Comprehension of the rules that govern the folding process is still far from satisfactory, though it is nevertheless clear that all the information required to define the folding is encoded in the amino acid sequence. In proteins that contain disulphide bonds, folding is associated with disulphide bond formation. Protein species with different numbers of disulphides tend to accumulate during the process; these species can be trapped in a stable form, by quenching any remaining free SH groups, and then characterized in order to identify the disulphide bonds formed. Results The refolding pathway of reduced and denatured RNase A has been studied using mass spectrometric strategies …

Protein FoldingSh groupsRNase P010402 general chemistryPeptide Mapping01 natural sciencesBiochemistryrefolding03 medical and health sciencesRNase AAnimalsDisulfidesES-MSPeptide sequencedisulphide bonds030304 developmental biology0303 health sciencesQuenching (fluorescence)ChemistryFAB-MSRibonuclease Pancreatic0104 chemical sciencesFolding (chemistry)CrystallographyMolecular MedicineCattlePancreatic RNaseDisulphide bondsCysteineFolding and Design
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Physicochemical compatibility of mixtures of dornase alfa and tobramycin containing nebulizer solutions

2008

Patients suffering from cystic fibrosis (CF) often need to inhale multiple doses of different nebulizable drugs per day. Patients attempt to shorten the time consuming administration procedure by mixing drug solutions/suspensions for simultaneous inhalation. The objective of this experimental study was to determine whether mixtures of the nebulizer solution dornase alfa (Pulmozyme) with tobramycin nebulizer solutions (TOBI and GERNEBCIN 80 mg) are physico-chemically compatible. Drug combinations were prepared by mixing the content of one respule Pulmozyme with either one respule TOBI or one ampoule GERNEBCIN 80 mg. Test solutions were stored at room temperature and exposed to light. Dornase…

Pulmonary and Respiratory MedicineChemical PhenomenaCystic FibrosisExcipientAmpouleDrug Incompatibilitychemistry.chemical_compoundAdministration InhalationTobramycinDeoxyribonuclease IHumansMedicinePotencyChromatographyInhalationbusiness.industryNebulizers and VaporizersDornase alfaSodium metabisulfiteAnti-Bacterial AgentsDrug CombinationsPharmaceutical SolutionsNebulizerchemistryAnesthesiaPediatrics Perinatology and Child HealthTobramycinbusinessmedicine.drugPediatric Pulmonology
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Physicochemical compatibility and stability of nebulizable drug admixtures containing Dornase alfa and tobramycin.

2012

The objective of this in-vitro study was to determine whether admixtures of the inhalation solutions Pulmozyme(®) (Dornase alfa) and either Bramitob(®) or Tobi(®) (both containing Tobramycin) are physicochemically compatible and to analyze the aerodynamic parameters of these admixtures. After mixing, test solutions were stored at room temperature and under ambient light conditions over a period of 24 h. Tobramycin concentrations were determined by using a fluorescence immunoassay. Stability of dornase alfa was determined by size-exclusion high performance liquid chromatography, ultraviolet spectroscopy, sodium dodecyl sulfate polyacrylamide gel electrophoresis and tentacle strong cation-exc…

Pulmonary and Respiratory MedicineTime FactorsDrug StorageHigh-performance liquid chromatographyDrug Incompatibilitychemistry.chemical_compoundDrug StabilityAdministration InhalationmedicineTobramycinGeometric standard deviationDeoxyribonuclease IPharmacology (medical)Sodium dodecyl sulfateParticle SizeAerosolsChromatographyInhalationNebulizers and VaporizersBiochemistry (medical)Osmolar ConcentrationDornase alfaHydrogen-Ion ConcentrationRecombinant ProteinsAnti-Bacterial AgentsDrug CombinationsPharmaceutical SolutionschemistryCompatibility (mechanics)TobramycinFeasibility StudiesParticle fractionmedicine.drugPulmonary pharmacologytherapeutics
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Rev protein suppression of complex formation between nuclear proteins and rev-responsive element-containing RNA of human immunodeficiency virus-1

1995

The Rev protein from human immunodeficiency virus type 1 (HIV-1) is known to bind Rev responsive element (RRE) sequence of HIV-1 mRNA. This interaction is thought to enhance expression of viral structural proteins but the mechanism for this effect is uncertain. The aim of this study was to investigate (i) whether other cellular proteins also bind to the RRE sequence and (ii) whether binding of cellular proteins to RRE RNA is influenced by Rev protein. Our results revealed that a variety of RNA-protein complexes are formed when in vitro transcribed RRE-containing RNA is incubated with proteins present in HeLa nuclear extracts. The molecular masses of the most prominent bands in RNase protect…

RNase PvirusesBiologyGenes envBiochemistrylaw.inventionchemistry.chemical_compoundBiopolymerslawHumansRNA MessengerNuclear proteinRibonucleoproteinMessenger RNANuclear ProteinsRNArev Gene Products Human Immunodeficiency VirusCell BiologyMolecular biologyCell biologyGene Products revRibonucleoproteinschemistryCytoplasmHIV-1Recombinant DNARNA ViralPMSFHeLa CellsThe International Journal of Biochemistry & Cell Biology
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