Search results for "MUCOSA"

showing 10 items of 1066 documents

Indirect Osteotome Maxillary Sinus Floor Elevation: An Update

2012

The objective was to review publications on indirect osteotome maxillary sinus floor elevation (OMSFE) procedures. Studies published between 1999 and 2010 on patients with a minimum of 1 year of follow-up were analyzed. Fourteen studies were included. Indirect OMSFE is indicated for a bone height of 6–8 mm. More bone height was gained when graft material was used. Schneiderian membrane perforation was the most frequent complication. Survival rates varied between 93.5% and 100%. Osteotome sinus membrane elevation is a predictable and effective procedure for placing implants in areas of the posterior maxilla with low bone height.

Bone TransplantationMaxillary sinusbusiness.industryDental Implantation EndosseousAlveolar Bone LossElevationSinus Floor AugmentationDentistryOsteotomyNasal Mucosamedicine.anatomical_structureBone transplantationmedicineHumansOsteotomeOral SurgerybusinessJournal of Oral Implantology
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Acute Laryngitis in the Rat Induced by Moraxella catarrhalis and Bordetella pertussis: Number of Neutrophils, Dendritic Cells, and T and B Lymphocyte…

1999

Infectious laryngotracheitis results in fulminant respiratory distress. During the disease, the subglottic mucosa is selectively infected and swollen, the reason for this preference being unknown. Therefore, in the present study the immunoreaction of the laryngeal mucosa was studied in the rat after inhalation of either heat-killed Moraxella catarrhalis (PVG rats) or application of viable Bordetella pertussis (BN rats). The number of neutrophils, macrophages, dendritic cells, and T and B lymphocytes was determined in the mucosa of the supraglottic, glottic, and subglottic area of the larynx as well as in the trachea. After application of the pathogens, the mucosa of the subglottic area was …

Bordetella pertussisPathologymedicine.medical_specialtyNeutrophilsWhooping CoughNeisseriaceae InfectionsT-LymphocytesInflammationGranulocyteBordetella pertussisMoraxella catarrhalisLaryngitismedicineAnimalsImmunity MucosalB-Lymphocytesbiologybusiness.industryRespiratory diseaseDendritic CellsT lymphocyteDendritic cellbiology.organism_classificationmedicine.diseaseEpitheliumBlood Cell CountRatsmedicine.anatomical_structureLaryngeal MucosaOrgan SpecificityPediatrics Perinatology and Child HealthImmunologymedicine.symptombusinessMoraxella catarrhalisPediatric Research
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Cigarette smoke alters IL-33 expression and release in airway epithelial cells

2014

AbstractAirway epithelium is a regulator of innate immune responses to a variety of insults including cigarette smoke. Cigarette smoke alters the expression and the activation of Toll Like Receptor 4 (TLR4), an innate immunity receptor. IL-33, an alarmin, increases innate immunity Th2 responses. The aims of this study were to explore whether mini-bronchoalveolar lavage (mini-BAL) or sera from smokers have altered concentrations of IL-33 and whether cigarette smoke extracts (CSE) alter both intracellular expression (mRNA and protein) and release of IL-33 in bronchial epithelial cells. The role of TLR4 in the expression of IL-33 was also explored.Mini-BALs, but not sera, from smokers show red…

Bronchial epithelial cellLipopolysaccharidesBlotting WesternBronchiInflammationRespiratory MucosaBiologyReal-Time Polymerase Chain ReactionBronchoalveolar LavageImmunoenzyme TechniquesBronchial epithelial cell; COPD; Cigarette smoke; IL-33; InflammationSmokeacute lung injury cigarette smokeinterleukin 33medicineCOPDHumansRNA MessengerReceptorMolecular BiologyCells CulturedCell ProliferationInflammationToll-like receptorInnate immune systemReverse Transcriptase Polymerase Chain ReactionInterleukinsCigarette smokeFlow CytometryInterleukin-33Immunity Innaterespiratory tract diseasesCell biologyToll-Like Receptor 4Interleukin 33ImmunologyIL-33TLR4Molecular MedicineRespiratory epitheliummedicine.symptomIntracellularBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
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Selective inhibition of binding of Bacillus thuringiensis Cry1Ab toxin to cadherin-like and aminopeptidase proteins in brush-border membranes and dis…

2007

Binding analyses with denatured epithelial membrane proteins from Bt (Bacillus thuringiensis) demonstrated at least two kinds of proteins, APNs (aminopeptidases N) and cadherin-like proteins, as possible receptors for the Cry1A class of Bt toxins. Two alternative models have been proposed, both based on initial toxin binding to a cadherin-like protein, but one involving APN and the other not. We have used two Bombyx mori strains (J65 and Kin), which are highly susceptible to Cry1Ab, to study the role of these two types of receptors on Cry1Ab toxin binding and cytotoxicity by means of the inhibitory effect of antibodies. BBMVs (brush-border membrane vesicles) of strain J65 incubated with lab…

Brush borderBacterial ToxinsBacillus thuringiensisCD13 Antigensmedicine.disease_causeBiochemistryAminopeptidaseAminopeptidasesAntibodiesHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineAnimalsIntestinal MucosaReceptorMolecular BiologyMembranesbiologyBacillus thuringiensis ToxinsMicrovilliCadherinToxinfungiEpithelial CellsCell Biologybiology.organism_classificationBombyxMolecular biologyEndotoxinsMembrane proteinBiochemistrybiology.proteinBiological AssayAntibodyProtein BindingThe Biochemical journal
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The CFTR associated protein CAP70 interacts with the apical Cl-/HCO3- exchanger DRA in rabbit small intestinal mucosa.

2005

DRA (down regulated in adenoma) is an intestinal anion exchanger, acting in parallel with NHE3 to facilitate ileal and colonic NaCl absorption. Furthermore it is involved in small intestinal bicarbonate secretion. Because DRA has a PDZ interaction motif, which may influence its properties, we searched for DRA-interacting PDZ adapter proteins in the small intestine. Using an overlay assay with the recombinant DRA C-terminus as a ligand, a 70 kDa protein was labeled, which was restricted to the brush border membrane in rabbit duodenal and ileal mucosa and was not detected in the colon. Destruction of the C-terminal PDZ interaction motif abolished this band, suggesting a specific protein-prote…

Brush borderColonPDZ domainAmino Acid MotifsMolecular Sequence DataCystic Fibrosis Transmembrane Conductance RegulatorIleumBiologyBiochemistryAntiportersCell LineIntestine SmallmedicineAnimalsHumansSecretionAmino Acid SequenceChloride-Bicarbonate AntiportersRNA MessengerIntestinal MucosaMessenger RNAHEK 293 cellsSignal transducing adaptor proteinMembrane ProteinsMolecular biologySmall intestinePeptide Fragmentsmedicine.anatomical_structureSulfate TransportersRabbitsCarrier ProteinsBiochemistry
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Efficacy of 5-FU topically applied on a buccal mucosal model resembling human tissue. A new chance for OSCC chemotherapy.

2008

Buccal mucosa modelOSCC chemotherapy5-FU
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Biotransformation in vitro of the 22R and 22S epimers of budesonide by human liver, bronchus, colonic mucosa and skin.

2001

The pharmacological effects of glucocorticoids are greatly influenced by their pharmacokinetic properties. In the present report, the in vitro biotransformation of the 22R and 22S epimers of the topical steroid budesonide was studied in the S-9 fraction of human liver, bronchus, skin and colonic mucosa. The disappearance of unchanged epimers of budesonide was measured during 90 min of incubation by high performance liquid chromatography. The rate of disappearance was high in human liver while little biotransformation occurred in bronchial tissue and colonic mucosa, and none was detected in the skin. A marked decay of the initial concentration of unchanged budesonide epimers was noticed afte…

Budesonidemedicine.medical_specialtyColonAdministration TopicalAnti-Inflammatory AgentsBronchiCell LineTherapeutic indexPharmacokineticsBiotransformationInternal medicineCulture TechniquesmedicineHumansPharmacology (medical)Intestinal MucosaBudesonideIncubationGlucocorticoidsBiotransformationCells CulturedSkinPharmacologyBronchusChemistryStereoisomerismIn vitroEndocrinologymedicine.anatomical_structureLiverHepatocytesEpimermedicine.drugFundamentalclinical pharmacology
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Pyostomatitis vegetans und Morbus Crohn: Eine spezifische Assoziation zweier Krankheiten

2008

HISTORY AND CLINICAL FINDINGS A 27-year-old man was referred to the dermatological out-patient clinic because of inflammatory changes in the oral mucosa of unknown cause. 5 months earlier he had been diagnosed as having Crohn's disease of the terminal ileum. On both sides of the buccal mucosa there were rough erythematous vegetations and disseminated miliary abscesses, which extended to the labial gingiva and the soft palate. Further physical examination was unremarkable. INVESTIGATIONS Several inflammatory parameters were increased: C-reactive protein 100 mg/l, erythrocyte sedimentation rate 55/88 mm, eosinophilic cationic protein 35.8 ng/ml (normal range 2.3-16 ng/ml). White cell count wa…

Budesonidemedicine.medical_specialtymedicine.diagnostic_testbusiness.industryGeneral Medicinemedicine.diseaseUlcerative colitisGastroenterologymedicine.anatomical_structureGastrointestinal diseaseErythrocyte sedimentation rateInternal medicineBiopsymedicineEosinophiliamedicine.symptomOral mucosabusinessPyostomatitis vegetansmedicine.drugDMW - Deutsche Medizinische Wochenschrift
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Induction of CD36 and thrombospondin-1 in macrophages by hypoxia-inducible factor 1 and its relevance in the inflammatory process.

2012

Inflammation is part of a complex biological response of vascular tissue to pathogens or damaged cells. First inflammatory cells attempt to remove the injurious stimuli and this is followed by a healing process mediated principally by phagocytosis of senescent cells. Hypoxia and p38-MAPK are associated with inflammation, and hypoxia inducible factor 1 (HIF-1) has been detected in inflamed tissues. We aimed to analyse the role of p38-MAPK and HIF-1 in the transcriptional regulation of CD36, a class B scavenger receptor, and its ligand thrombospondin (TSP-1) in macrophages and to evaluate the involvement of this pathway in phagocytosis of apoptotic neutrophils. We have also assessed HIF-1α, p…

CD36 AntigensMaleAnatomy and PhysiologyNeutrophilsCD36Digestive Physiologylcsh:MedicineApoptosisp38 Mitogen-Activated Protein KinasesBiochemistryMonocytesThrombospondin 1Intestinal mucosaCrohn DiseaseIntestinal Mucosalcsh:ScienceHypoxiaPromoter Regions GeneticMultidisciplinaryProtein StabilityMiddle AgedOxygen Metabolismmedicine.anatomical_structureMedicineFemaleHypoxia-Inducible Factor 1medicine.symptomProtein BindingSignal TransductionResearch ArticleAdultCell PhysiologyAdolescentPhagocytosisImmune CellsImmunologyInflammationGastroenterology and HepatologyBiologyCell LineYoung AdultPhagocytosismedicineHumansUlcerative ColitisScavenger receptorBiologyInflammationLamina propriaDigestive RegulationMacrophageslcsh:RInflammatory Bowel DiseaseHypoxia (medical)Hypoxia-Inducible Factor 1 alpha SubunitMetabolismApoptosisImmunologyCancer researchbiology.proteinlcsh:QColitis UlcerativeDigestive SystemPloS one
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Luminal Lipid Regulates CD36 Levels and Downstream Signaling to Stimulate Chylomicron Synthesis

2011

International audience; The membrane glycoprotein CD36 binds nanomolar concentrations of long chain fatty acids (LCFA) and is highly expressed on the luminal surface of enterocytes. CD36 deficiency reduces chylomicron production through unknown mechanisms. In this report, we provide novel insights into some of the underlying mechanisms. Our in vivo data demonstrate that CD36 gene deletion in mice does not affect LCFA uptake and subsequent esterification into triglycerides by the intestinal mucosa exposed to the micellar LCFA concentrations prevailing in the intestine. In rodents, the CD36 protein disappears early from the luminal side of intestinal villi during the postprandial period, but …

CD36 AntigensMaleMTPCD36[SDV]Life Sciences [q-bio]BiochemistryMicrosomal triglyceride transfer proteinMice0302 clinical medicineIntestinal mucosaCricetinaeChylomicronsLipoproteinHypertriglyceridemiaMice Knockout0303 health sciencesMitogen-Activated Protein Kinase 3biologyPostprandial PeriodLipid-binding ProteinIntestineApoB48ERKmedicine.anatomical_structurePostprandialBiochemistrylipids (amino acids peptides and proteins)Apolipoprotein B-48MAP Kinase Signaling SystemEnterocyteCHO CellsChylomicron03 medical and health sciencesCricetulusparasitic diseasesmedicineAnimalsRats WistarMolecular Biology030304 developmental biologyUbiquitinationLipid absorptionLipid metabolismCell BiologyLipid MetabolismRatsEnterocytesMetabolismbiology.proteinApolipoprotein B-48CD36[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition030217 neurology & neurosurgeryChylomicron
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