Search results for "Complement System"

showing 10 items of 157 documents

Complement activation by oxidatively modified low-density lipoproteins

1999

Background Oxidatively modified low-density lipoproteins (LDLs) have been implicated in the pathogenesis of atherosclerosis and are found in human vascular lesions. There is increasing evidence that complement activation may also play a role in atherogenesis. Activated complement proteins have been demonstrated to be present in early atherosclerotic lesions, and lipids isolated from lesions have been shown to activate complement, hence their designation as lesion complement activator (LCA). The question now arose whether oxidized LDLs would also activate complement. Material and methods The complement-activating capacity of a lesion complement activator preparation and of minimally as well …

medicine.medical_specialtyClinical BiochemistryInflammationImmunoelectrophoresis030204 cardiovascular system & hematologyBiochemistryLipid peroxidationPathogenesisLesion03 medical and health scienceschemistry.chemical_compound0302 clinical medicineInternal medicinemedicine030304 developmental biology0303 health sciencesmedicine.diagnostic_testChemistryVascular diseaseGeneral Medicinemedicine.diseaseComplement systemComplement (complexity)EndocrinologyBiochemistrylipids (amino acids peptides and proteins)medicine.symptomEuropean Journal of Clinical Investigation
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On the pathogenesis of atherosclerosis: enzymatic transformation of human low density lipoprotein to an atherogenic moiety.

1995

Combined treatment with trypsin, cholesterol esterase, and neuraminidase transforms LDL, but not HDL or VLDL, to particles with properties akin to those of lipid extracted from atherosclerotic lesions. Single or double enzyme modifications, or treatment with phospholipase C, or simple vortexing are ineffective. Triple enzyme treatment disrupts the ordered and uniform structure of LDL particles, and gives rise to the formation of inhomogeneous lipid droplets 10-200 nm in diameter with a pronounced net negative charge, but lacking significant amounts of oxidized lipid. Enzymatically modified LDL (E-LDL), but not oxidatively modified LDL (ox-LDL), is endowed with potent complement-activating c…

Very low-density lipoproteinArteriosclerosisImmunologyNeuraminidaseComplement Membrane Attack Complexchemistry.chemical_compoundLipid dropletmedicineExtracellularImmunology and AllergyHumansTrypsinReceptors ImmunologicComplement ActivationGlycoproteinsReceptors Lipoproteinchemistry.chemical_classificationReceptors ScavengerPhospholipase CCholesterolMacrophagesMembrane ProteinsComplement C3Complement System ProteinsArticlesScavenger Receptors Class BSterol EsteraseTrypsinLipid MetabolismLipoproteins LDLEnzymechemistryBiochemistryLow-density lipoproteinlipids (amino acids peptides and proteins)medicine.drugFoam CellsThe Journal of experimental medicine
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Human Amnion-Derived Mesenchymal Stromal Cells: A New Potential Treatment for Carbapenem-Resistant Enterobacterales in Decompensated Cirrhosis

2022

Background: Spontaneous bacterial peritonitis (SBP) is a severe and often fatal infection in patients with decompensated cirrhosis and ascites. The only cure for SBP is antibiotic therapy, but the emerging problem of bacterial resistance requires novel therapeutic strategies. Human amniotic mesenchymal stromal cells (hA-MSCs) possess immunomodulatory and anti-inflammatory properties that can be harnessed as a therapy in such a context. Methods: An in vitro applications of hA-MSCs in ascitic fluid (AF) of cirrhotic patients, subsequently infected with carbapenem-resistant Enterobacterales, was performed. We evaluated the effects of hA-MSCs on bacterial load, innate immunity factors, and macr…

QH301-705.5Placentacirrhosis; ascitic fluid; spontaneous bacterial peritonitis; human amnion-derived mesenchymal stromal cells; carbapenem-resistant Enterobacterales; pattern recognition molecules; ficolins; complement; placentaComplementEnterobacterPeritonitisMesenchymal Stem Cell Transplantationbeta-Lactam ResistanceCatalysisImmunomodulationInorganic ChemistryPhagocytosisSpontaneous bacterial peritonitisHumansHuman amnion-derived mesenchymal stromal cellsAmnionBiology (General)Physical and Theoretical ChemistryQD1-999Complement ActivationMolecular BiologySpectroscopyAscitic fluidMacrophagesCarbapenem-resistant EnterobacteralesOrganic ChemistryPattern recognition moleculesEnterobacteriaceae InfectionsMesenchymal Stem CellsPeritoneal FibrosisFicolinsComplement System ProteinsGeneral MedicineBacterial LoadComputer Science ApplicationsChemistryTreatment OutcomeCirrhosisCarbapenemsReceptors Pattern RecognitionDisease SusceptibilityInflammation MediatorsBiomarkersInternational Journal of Molecular Sciences; Volume 23; Issue 2; Pages: 857
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Application of C1-Esterase Inhibitor During Reperfusion of Ischemic Myocardium

2001

Background—Complement activation during reperfusion of ischemic myocardium augments myocardial injury, and complement inhibition with C1-esterase inhibitor (C1-INH) at the time of reperfusion exerts marked cardioprotective effects in experimental studies. Application of C1-INH in newborns, however, was recently reported to have dangerous and even lethal side effects. This study addresses the essential role of dosage in studies using C1-INH.Methods and Results—Cardioprotection by C1-INH was examined in a pig model with 60 minutes of coronary occlusion followed by 120 minutes of reperfusion. C1-INH was administered intravenously 5 to 10 minutes before coronary reperfusion without heparin at a…

Anaphylatoxinsmedicine.medical_specialtyNecrosisSwineHeart VentriclesPartial PressureMyocardial IschemiaIschemiaComplement C1 Inactivator ProteinsPharmacologyNecrosisTroponin TCoronary CirculationPhysiology (medical)Internal medicineAnimalsMedicineLactic AcidMyocardial infarctionCardiac OutputCreatine KinaseCardioprotectionDose-Response Relationship Drugbiologybusiness.industryMyocardiumHemodynamicsHeparinmedicine.diseaseComplement systemOxygenMicroscopy ElectronEndocrinologyCoronary occlusionEnzyme inhibitorReperfusion Injurybiology.proteinBlood Gas Analysismedicine.symptomCardiology and Cardiovascular Medicinebusinessmedicine.drugCirculation
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Differential expression of the murine mannose-binding lectins A and C in lymphoid and nonlymphoid organs and tissues.

2003

Abstract Mannose-binding lectin (MBL), a member of the collectin family, binds to carbohydrate structures on the surfaces of micro-organisms and may serve as a recognition molecule of the lectin pathway of complement activation. In rodents two forms, MBL-A and MBL-C, were described and shown to be products of two related, but uncoupled, genes. The liver is the main source of MBL biosynthesis. For rat MBL-A, expression has also been described in the kidney. Here we report that the two forms of murine MBL are differentially expressed in a number of nonhepatic tissues. Real-time RT-PCR revealed that the liver is the major site of expression for both MBL genes. Lower copy numbers were found in …

MaleLymphoid TissueImmunologyCollectinchemical and pharmacologic phenomenaIn situ hybridizationMannose-Binding LectinMiceIntestine SmallImmunology and AllergyAnimalsProtein IsoformsIn Situ HybridizationMannan-binding lectinMice Inbred BALB CInnate immune systembiologyLectinbacterial infections and mycosesAcquired immune systemMolecular biologyImmunohistochemistryComplement systemAnimals NewbornLiverOrgan SpecificityLectin pathwaybiology.proteinFemaleSpleenJournal of immunology (Baltimore, Md. : 1950)
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Reduction of myocardial infarct size with sCR1sLex, an alternatively glycosylated form of human soluble complement receptor type 1 (sCR1), possessing…

1999

1 This study investigated the effects of soluble complement receptor type 1 (sCR1) or sCR1sLex, agents which function as a complement inhibitor or as a combined complement inhibitor and selectin adhesion molecule antagonist, respectively, on the infarct size and cardiac troponin T (cTnT) release caused by regional myocardial ischaemia and reperfusion in the rat. 2 Eighty-two, male Wistar rats were subjected to 30 min occlusion of the left anterior descending coronary artery (LAD) followed by 2 h of reperfusion. Haemodynamic parameters were continuously recorded and at the end of the experiments infarct size (with p-nitro-blue tetrazolium) and cTnT release were determined. 3 Infusion of sCR1…

Pharmacologymedicine.medical_specialtyTroponin Tbusiness.industryAntagonistmedicine.diseaseComplement systemComplement inhibitorEndocrinologyComplement Receptor Type 1Troponin complexInternal medicineCardiovascular agentImmunologymedicineMyocardial infarctionbusinessBritish Journal of Pharmacology
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Involvement of complement pathways in patients with bacterial septicemia.

2007

The complement system is a major humoral portion of the innate immune system, playing a significant role in host defence against microorganisms. The biological importance of this system is underlined by the fact that at least three different pathways for its activation exist, the classical, the MBL and the alternative pathway. To elucidate the involvement of the classical and/or the MBL pathway during bacterial septicemia, 32 patients with gram-positive and 30 patients with gram-negative bacterial infections were investigated. In patients with gram-positive bacteria, a significant consumption of C1q (p=0.005) but not of mannose-binding lectin (MBL) (p=0.2) was found during the acute phase o…

MESH: Complement Pathway Mannose-Binding LectinLipopolysaccharidesSalmonellaMESH: Complement C1qLipopolysaccharideImmunologychemical and pharmacologic phenomenaBacteremiamedicine.disease_causeGram-Positive BacteriaMannose-Binding LectinMicrobiologyMESH: Gram-Positive Bacteria03 medical and health scienceschemistry.chemical_compoundClassical complement pathway0302 clinical medicinemedicineHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyComplement Pathway ClassicalMESH: BacteremiaMolecular Biology030304 developmental biology0303 health sciencesInnate immune systemMESH: HumansbiologyComplement C1qLectinSalmonella entericaComplement Pathway Mannose-Binding LectinMESH: Complement Pathway Classicalbiology.organism_classificationbacterial infections and mycoses3. Good healthComplement systemMESH: Mannose-Binding LectinchemistryMESH: Salmonella entericaImmunologyAlternative complement pathwaybiology.proteinMESH: LipopolysaccharidesBacteria030215 immunologyMolecular immunology
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Isolation and expression of a novel MBL-like collectin cDNA enhanced by LPS injection in the body wall of the ascidian Ciona intestinalis

2009

Collectins are a family of calcium-dependent lectins that are characterized by their collagen-like domains. Considerable interest has been focused on this class of proteins because of their ability to interact with components of the complement system activating a cascade of events responsible for the activation of the innate immune system. A differential screening between LPS-challenged and naïve Ciona intestinalis has been performed allowing the isolation of a full length cDNA encoding for a 221 AA protein. In silico analysis has shown that this polypeptide displays protein domains with similarities to mannose-binding lectins. A phylogenetic analysis suggested that C. intestinalis MBL has …

LipopolysaccharidesDNA ComplementaryIn silicoMolecular Sequence DataImmunologyProtein domainCollectinIn situ hybridizationBiologyCytoplasmic GranulesComplementary DNAAnimalsCiona intestinalisAmino Acid SequenceMolecular BiologyPhylogenyMannose-binding lectin innate immune system LPS Ciona intestinalisInnate immune systemBase Sequencebiology.organism_classificationMolecular biologyCollectinsCiona intestinalisProtein Structure TertiaryComplement systemMolecular Immunology
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Analysis of complement C3 activation products in human atherosclerotic lesions.

1991

Abstract Cleavage of the complement C3 protein is essential for complement activation. Saline extracts of human atherosclerotic lesions were examined by various techniques for the presence of C3 cleavage fragments. Crossed intermediate gel immunoelectrophoresis revealed that native C3 was the predominate C3 protein in extracts and that the C3dg fragment was also detected. SDS-PAGE/ Western blot analyses of lesion extracts employing monoclonal antibodies directed at C3c and C3dg fragment determinants demonstrated molecular weight bands corresponding to the known molecular weights of all the physiologic C3 cleavage fragments, except Cab which is known to have a short half-life. After C3, the …

medicine.diagnostic_testMolecular massArteriosclerosisBlotting WesternEnzyme-Linked Immunosorbent AssayImmunoelectrophoresisArteriesComplement C3BiologyCleavage (embryo)C3-convertasePeptide FragmentsComplement systemBlotBiochemistryWestern blotComplement C3bmedicineHumansLipid particleCardiology and Cardiovascular MedicineComplement ActivationImmunoelectrophoresisAtherosclerosis
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Innate immune response to tick-borne pathogens: Cellular and molecular mechanisms induced in the hosts

2020

This article belongs to the Special Issue Inflammasome.

0301 basic medicineInnate immune responseHost Defense MechanismReviewInflammasomelcsh:ChemistryTicksTheileriaTick borne pathogensRickettsialcsh:QH301-705.5SpectroscopyGene ontology analysisgene ontology analysisInflammasomeGeneral MedicineAcquired immune systemComputer Science ApplicationsTick-Borne DiseasesTumor necrosis factor alphamedicine.drugAnaplasma030106 microbiologyEhrlichiaBabesiaBiologyCatalysisMicrobiologyInorganic Chemistry03 medical and health sciencesAntigeninflammasomeparasitic diseasesmedicineAnimalsHumansPhysical and Theoretical ChemistryMolecular BiologyInnate immune systemOrganic Chemistrygene ontology analysibiology.organism_classificationImmunity InnateComplement systemInsect Vectors030104 developmental biologyRickettsialcsh:Biology (General)lcsh:QD1-999innate immune responsetick borne pathogens
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