Search results for "Pseudomembranous colitis"

showing 7 items of 7 documents

Clostridium difficile Toxins Disrupt Epithelial Barrier Function by Altering Membrane Microdomain Localization of Tight Junction Proteins

2001

ABSTRACT The anaerobic bacterium Clostridium difficile is the etiologic agent of pseudomembranous colitis. C. difficile toxins TcdA and TcdB are UDP-glucosyltransferases that monoglucosylate and thereby inactivate the Rho family of GTPases (W. P. Ciesla, Jr., and D. A. Bobak, J. Biol. Chem. 273:16021–16026, 1998). We utilized purified reference toxins of C. difficile , TcdA-10463 (TcdA) and TcdB-10463 (TcdB), and a model intestinal epithelial cell line to characterize their influence on tight-junction (TJ) organization and hence to analyze the mechanisms by which they contribute to the enhanced paracellular permeability and disease pathophysiology of pseudomembranous colitis. The increase i…

Bacterial ToxinsImmunologyClostridium difficile toxin ABiologyZonula Occludens-2 ProteinOccludinMicrobiologyCell junctionPermeabilityTight JunctionsMicrobiologyAdherens junctionEnterotoxinsMembrane MicrodomainsBacterial ProteinsIntestinal MucosaClostridioides difficileCell PolarityMembrane ProteinsPseudomembranous colitisClostridium difficilePhosphoproteinsMolecular PathogenesisActinsCell biologyInfectious DiseasesMembrane proteinGlucosyltransferasesParacellular transportZonula Occludens-1 ProteinParasitologyInfection and Immunity
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Autocatalytic cleavage of Clostridium difficile toxin B.

2007

Clostridium difficile, the causative agent of nosocomial antibiotic-associated diarrhoea and pseudomembranous colitis, possesses two main virulence factors: the large clostridial cytotoxins A and B. It has been proposed that toxin B is cleaved by a cytosolic factor of the eukaryotic target cell during its cellular uptake. Here we report that cleavage of not only toxin B, but also all other large clostridial cytotoxins, is an autocatalytic process dependent on host cytosolic inositolphosphate cofactors. A covalent inhibitor of aspartate proteases, 1,2-epoxy-3-(p-nitrophenoxy)propane, completely blocked toxin B function on cultured cells and was used to identify its catalytically active prote…

Cell ExtractsProteasesPhytic AcidSwineVirulence Factorsmedicine.medical_treatmentBacterial ToxinsClostridium difficile toxin AVirulenceClostridium difficile toxin Bmedicine.disease_causeCatalysisMicrobiologyCell LineNitrophenolsBiological FactorsBacterial ProteinsmedicineAnimalsAspartic Acid EndopeptidasesMultidisciplinaryProteaseBinding SitesToxinChemistryClostridioides difficilePseudomembranous colitisClostridium difficileProtein TransportBiochemistryEpoxy CompoundsProtein Processing Post-TranslationalSpleenNature
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Does uremic enterocolitis exist?

1981

In rats a severe but compensated chronic renal insufficiency was induced by stepwise 9/10 nephrectomy. Despite this severe chronic renal insufficiency we observed no relevant pathological changes in the intestinal mucosa. In particular, we found no evidence of mucosal erosions, ulceration or pseudomembranous colitis, findings which are traditionally thought to be characteristic of the uremic state. This was also true of those animals dying prematurely from uremia. Thus serious doubts arise about the existence of “uremic enterocolitis”, doubts which also proved justified after a critical review of the literature on human pathology.

EnterocolitisPathologymedicine.medical_specialtybusiness.industrymedicine.medical_treatmentPseudomembranous colitismedicine.diseaseIntestinal absorptionNephrectomyUremiaIntestinal mucosamedicinemedicine.symptombusinessHuman PathologyPathologicalVirchows Archiv B Cell Pathology Including Molecular Pathology
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Inflammatory Bowel Diseases

1979

The endoscopic aspects of an inflammatory colon disease do not permit the differentiation of a nonspecific proctitis from a bacterial enterocolitis and an ulcerative proctitis.

Enterocolitismedicine.medical_specialtybusiness.industryInflammatory Bowel DiseasesDiseasePseudomembranous colitismedicine.diseaseGastroenterologyUlcerative colitisdigestive system diseasesIschemic colitisUlcerative proctitisInternal medicineMedicinemedicine.symptombusinessProctitis
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Clostridium difficile toxins A and B inhibit human immune response in vitro

1988

Two Clostridium difficile toxins isolated from strain VPI 10463 were tested for their effect on different human T-cell proliferation systems. In mitogen- and antigen-driven T-cell proliferation systems, toxins inhibited the proliferative response in a dose-dependent fashion. In interleukin-2-driven culture systems, no effect of toxins could be found on preactivated T cells. We suspected that monocytes were the influenced cells, since in antigen- and mitogen-driven systems monocytes were necessary for the proliferative response, whereas the interleukin-2-driven system was independent of monocytes. To prove this concept, purified monocytes were treated with toxins. The treatment was found to …

Interleukin 2Cellular immunityT-LymphocytesBacterial ToxinsImmunologyEnterotoxinIn Vitro TechniquesBiologyLymphocyte ActivationMicrobiologyMonocytesMicrobiologyEnterotoxinsImmune systemBacterial ProteinsAntigenmedicineHumansMonocytePseudomembranous colitisClostridium difficileInfectious Diseasesmedicine.anatomical_structureInterleukin-2ParasitologyMitogensResearch Articlemedicine.drugInfection and Immunity
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The Enterotoxin from Clostridium difficile (ToxA) Monoglucosylates the Rho Proteins

1995

The enterotoxin from Clostridium difficile (ToxA) is one of the causative agents of the antibiotic-associated pseudomembranous colitis. In cultured monolayer cells ToxA exhibits cytotoxic activity to induce disassembly of the actin cytoskeleton, which is accompanied by morphological changes. ToxA-induced depolymerization of actin filaments is correlated with a decrease in the ADP-ribosylation of the low molecular mass GTP-binding Rho proteins (Just, I., Selzer, J., von Eichel-Streiber, C., and Aktories, K. (1995) J. Clin. Invest. 95, 1026-1031). Here we report on the identification of the ToxA-induced modification of Rho. Applying electrospray mass spectrometry, the mass of the modification…

RHOAGlycoside HydrolasesBacterial ToxinsClostridium difficile toxin ARAC1macromolecular substancesEnterotoxinBiochemistrySubstrate SpecificityEnterotoxinsGTP-Binding ProteinsTumor Cells CulturedAmino AcidsMolecular BiologyActinbiologyMolecular massClostridioides difficileCell BiologyPseudomembranous colitisActin cytoskeletonMolecular biologycarbohydrates (lipids)GlucoseBiochemistrybiology.proteinrhoA GTP-Binding ProteinJournal of Biological Chemistry
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Severe Clostridium difficile infection with extremely high leucocytosis complicated by a concomitant bloodstream infection caused by Klebsiella pneum…

2020

Highlights • Exposure to antibiotics after surgery increase risk of Cl. difficile infection. • Sudden high leucocytosis may be sign of poor outcome in Cl. difficile case. • Oral Vancomycin could be responsible for the growth of bloodstream Kl. pneumonia.

medicine.medical_specialtyFulminantCefazolin03 medical and health sciences0302 clinical medicineVancomycinCase reportmedicineextremely high LeucocytosisSeptic shockbusiness.industryOsteomyelitisOsteomyelitisPseudomembranous colitisClostridium difficileClostridium difficilemedicine.diseaseSurgeryMetronidazoleKlebsiella pneumoniae030220 oncology & carcinogenesisVancomycin030211 gastroenterology & hepatologySurgerybusinessmedicine.drugInternational Journal of Surgery Case Reports
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