Search results for "Complement C1"

showing 10 items of 125 documents

Intracoronary application of C1 esterase inhibitor improves cardiac function and reduces myocardial necrosis in an experimental model of ischemia and…

1997

Background Myocardial injury from ischemia can be aggravated by reperfusion of the jeopardized area. The precise underlying mechanisms have not been clearly defined, but proinflammatory events, including complement activation, leukocyte adhesion, and infiltration and release of diverse mediators, probably play important roles. The present study addresses the possibility of reducing reperfusion damage by the application of C1 esterase inhibitor (C1-INH). Methods and Results Cardioprotection by C1-INH 20 IU/kg IC was examined in a pig model with 60 minutes of coronary occlusion, followed by 120 minutes of reperfusion. C1-INH was administered during the first 5 minutes of coronary reperfusion…

Cardiac function curveMalemedicine.medical_specialtyAnaphylatoxinsNecrosisSwinePartial PressureIschemiaMyocardial IschemiaMyocardial ReperfusionComplement C1 Inactivator ProteinsCreatineInjectionschemistry.chemical_compoundNecrosisTroponin TPhysiology (medical)Internal medicinemedicineAnimalsMyocardial infarctionLactic AcidCreatine KinaseCardioprotectionTroponin Tbusiness.industryMyocardiumHemodynamicsHeartmedicine.diseaseCoronary VesselsTroponinOxygenchemistryCoronary occlusionAnesthesiaCardiologyFemalemedicine.symptomCardiology and Cardiovascular MedicinebusinessCirculation
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C1-esterase inhibitor in ischemia and reperfusion.

2002

Summary Myocardial injury from ischemia can be aggravated by reperfusion of the jeopardized area. The precise underlying mechanisms have not been clearly defined, but proinflammatory events including complement activation play important roles. Cardioprotection by complement inhibition inter alia C1-esterase-inhibitor (C1-INH) was examined in several experimental models and under clinical conditions with ischemia and reperfusion. C1-INH reduced local anaphylatoxin release revealing the importance of the classical complement pathway. Inhibition of local complement activation was accompanied by improvement of myocardial function and perfusion of the previously ischemic myocardium. Leukocyte en…

Cardiotonic AgentsImmunologyIschemiaMyocardial IschemiaMyocardial Reperfusion InjuryPharmacologyComplement C1 Inactivator ProteinsProinflammatory cytokineClassical complement pathwayIschemiamedicineImmunology and AllergyAnimalsHumansAnaphylatoxinComplement Pathway ClassicalCardioprotectionbusiness.industryHeartHematologymedicine.diseaseC1 esteraseComplement systemAnesthesiaModels AnimalbusinessPerfusionComplement C1 Inhibitor ProteinImmunobiology
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Pyridinedicarboxylates, the first mechanism-derived inhibitors for prolyl 4-hydroxylase, selectively suppress cellular hydroxyprolyl biosynthesis. De…

1987

Two pyridinedicarboxylates, predicted [Hanauske-Abel (1983) M.D.-Ph.D. Thesis, Philipps Universität Marburg] and later found to be potent reversible inhibitors of purified prolyl 4-hydroxylase [Majaama, Hanauske-Abel, Günzler & Kivirikko (1984) Eur. J. Biochem. 138, 239-245] were investigated with respect to their effect on hydroxyprolyl biosynthesis in the fibroblast/collagen and the macrophage/Clq systems, and the effect was compared with that of the iron chelator 2,2′-dipyridyl, the compound usually employed to inhibit cellular hydroxyprolyl formation. Only the enzyme-mechanism-derived pyridinedicarboxylates were highly selective inhibitors, and only they lacked overt cytotoxicity. M…

Cell typeCell SurvivalComplement Activating EnzymesGuinea PigsProcollagen-Proline DioxygenaseBiologyBiochemistrychemistry.chemical_compoundBiosynthesisComplement C1In vivomedicineAnimalsHumansSecretionPicolinic AcidsFibroblastCytotoxicityMolecular BiologyCells CulturedDose-Response Relationship DrugComplement C1qEndoplasmic reticulumCell BiologyFibroblastsHydroxyprolineMicroscopy Electronmedicine.anatomical_structureBiochemistrychemistryLipophilicityCollagenResearch ArticleBiochemical Journal
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Subcellular targeting of multiligand-binding protein gC1qR.

1999

Abstract gC1q receptor, a protein originally described as the cell surface receptor for the globular heads of complement factor C1q, has been found to bind human H-kininogen with high affinity and specificity. Therefore, gC1qR has been considered candidate kininogen docking site on the surfaces of platelets, neutrophils and endothelial cells. Recent work demonstrating that gC1qR is an intracellular protein that is tightly associated with mitochondria rather than targeted to the cell surface has challenged this view. To further probe cellular trafficking routes of gC1qR, we overexpressed human gC1qR in a mammalian cell and monitored cell surface exposure of recombinant gC1qR by virtue of its…

CellComplement factor IBiologyLigandsMitochondrial ProteinsCell surface receptormedicineAnimalsHumansBinding siteReceptorPharmacologyBinding SitesMembrane GlycoproteinsBinding proteinComplement C1qBiological TransportTransfectionMolecular biologyCell biologyReceptors Complementmedicine.anatomical_structureHyaluronan ReceptorsCell cultureCOS CellsCarrier ProteinsProtein Processing Post-Translationalcirculatory and respiratory physiologySubcellular FractionsImmunopharmacology
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Effect of EDTA and citrate on the functional activity of the first component of complement, C1, and the C1q subcomponent.

1985

The first component of complement, C1, is a calcium-dependent complex of the three distinct subcomponents, C1q, C1r, and C1s. Earlier observations revealed that treatment of C1 with EDTA led to a loss of hemolytic C1 activity even after recalcification. Therefore, it was of interest to study whether EDTA has an additional effect on C1 and its subcomponents, beside its chelating capacity. The chelating effect of EDTA was compared to that of citrate. It was found that treatment of C1 or C1 with EDTA followed by addition of Ca++ led to a loss of hemolytic activity up to 90%, depending on EDTA concentration. Even pretreatment of EDTA with varying amounts of Ca++ did not prevent the inactivation…

Chemical PhenomenaComplement Activating EnzymesMacromolecular SubstancesImmunologyKineticschemistry.chemical_elementCalciumHemolysisDissociation (chemistry)Structure-Activity RelationshipComplement C1medicineImmunology and AllergyStructure–activity relationshipHumansChelationCitratesComplement C1qEdetic AcidComplement C1qHematologymedicine.diseaseHemolysisChemistryKineticsBiochemistrychemistryEdetic AcidCalciumImmunobiology
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Binding and activation of human and mouse complement by Cryptosporidium parvum (Apicomplexa) and susceptibility of C1q- and MBL-deficient mice to inf…

2008

Cryptosporidium parvum is a protozoan parasite (Apicomplexa) that causes gastrointestinal disease in animals and humans. Whereas immunocompetent hosts can limit the infection within 1 or 2 weeks, immunocompromised individuals develop a chronic, life-threatening disease. The importance of the adaptive cellular immune response, with CD4+ T-lymphocytes being the major players, has been clearly demonstrated. Several non-adaptive immune mechanisms have been suggested to contribute to the host defence, such as interferon-gamma (IFN-gamma) from NK cells, certain chemokines, beta-defensins and pro-inflammatory cytokines, but the influence of the complement systems has been less well studied. We ana…

ChemokineImmunologyProtozoan ProteinsCryptosporidiosisComplement factor ISodium ChlorideMannose-Binding LectinMicrobiologyMiceImmune systemmedicineAnimalsHumansRNA MessengerMolecular BiologyComplement ActivationImmunodeficiencyMannan-binding lectinCryptosporidium parvumbiologyReverse Transcriptase Polymerase Chain ReactionComplement C1qOocystsTemperaturemedicine.diseasebiology.organism_classificationVirologyComplement systemMice Inbred C57BLCryptosporidium parvumGene Expression RegulationLectin pathwayComplement C3bbiology.proteinCattleDisease SusceptibilityMolecular immunology
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The Role of the Classical Pathway for the Bactericidal Effect of Normal Sera Against Gram-Negative Bacteria

1985

Many gram-negative bacteria are killed after treatment with normal serum. This phenomenon was already described in 1889 by Buchner. The serum-bactericidal effect is abolished when serum has been incubated for 30 min at 56° C. Gram-positive bacteria are less sensitive than gram-negative bacteria to direct killing, although gram-positive cocci are opsonized by the action of serum mediated by antibodies and complement (Inoue et al. 1968; Johnston et al. 1969). Normal sera exhibit bactericidal and bacteriolytic properties against some gramnegative strains; whereas, other gram-negative strains are serum resistant. It has been shown that serum from C4-deficient guinea pigs is able to kill some gr…

Classical complement pathwayGram-negative bacteriaAlternative complement pathwayBiologybiology.organism_classificationComplement membrane attack complexComplement C1qOpsoninBacteriaComplement systemMicrobiology
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Enzymatic alteration of C1q, the collagen-like subcomponent of the first component of complement, leads to cross-reactivity with type II collagen

1988

AbstractNative serum C1q, the collagenous-like subcomponent of the first component of complement, is not recognized by polyclonal anti-collagen type II antibodies. However, when purified C1q was subjected to limited proteolysis by collagenase it showed antigenic cross-reactivity with collagen type II. The same cross-reactivity was observed with hemolytically active C1q in synovial fluids of patients with rheumatoid arthritis (RA), whereas C1q from synovial fluids of patients with osteoarthritis (OA), villo-nodular synovitis and ankylosing spondylitis was not recognized by this antibody. However, incubation of synovial fluid C1q of OA patients with synovial fluid leucocytes from RA patients …

Complement Activating EnzymesCollagenaseComplementBiophysicsType II collagenEnzyme-Linked Immunosorbent Assaychemical and pharmacologic phenomenaOsteoarthritisBiochemistryAntibodiesArthritis Rheumatoidfluids and secretionsAntigenComplement C1immune system diseasesStructural BiologySynovitisOsteoarthritisSynovial FluidGeneticsmedicineAnimalsHumansSynovial fluidSpondylitis AnkylosingAntigensRheumatoid arthritisskin and connective tissue diseasesMolecular BiologyC1qAutoantibodiesSheepSynovitisbiologyChemistryComplement C1qAntibodies MonoclonalCell Biologymedicine.diseaseMolecular biologyMicrobial CollagenasePolyclonal antibodiesImmunologyCollagenasebiology.proteinCollagenAntibodyGranulocytesmedicine.drugFEBS Letters
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Evidence for the presence of autoantibodies to the collagen-like portion of C1q in systemic lupus erythematosus.

1988

We investigated the connection between the C1q solid-phase binding assay (C1q SPBA) and double-stranded DNA antibodies, and analyzed the immune complex material in systemic lupus erythematosus (SLE) sera. Comparison with a new monoclonal assay for C1q-bearing immune complexes (the 242G3 assay) revealed that the immune complexes in SLE bind specifically to solid-phase C1q, and not to fluid-phase C1q. The C1q solid-phase binding activity sedimented as 7S IgG, was insensitive to DNase treatment, and could be selectively absorbed by C1q-coupled beads and by bovine serum albumin-anti-bovine serum albumin C1q beads, but not by DNA. Thus, antibodies to double-stranded DNA do not interfere in the C…

Complement Activating EnzymesImmunologySerum albuminchemical and pharmacologic phenomenaEnzyme-Linked Immunosorbent AssayAntigen-Antibody Complexurologic and male genital diseasesfluids and secretionsImmune systemRheumatologyimmune system diseasesComplement C1medicineImmunology and AllergyHumansLupus Erythematosus SystemicPharmacology (medical)Bovine serum albuminskin and connective tissue diseasesAutoantibodiesLupus erythematosusbiologybusiness.industryLigand binding assayComplement C1qAutoantibodyDNA Neoplasmmedicine.diseaseImmune complexImmunoglobulin GImmunologybiology.proteinCollagenAntibodybusinessUltracentrifugationArthritis and rheumatism
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The reconstitution of human C1, the first complement component Binding of C1r and C1s to C1q influences the C1q conformation

1981

Complement Activating EnzymesMacromolecular SubstancesProtein ConformationBiophysicsPlasma protein bindingBiochemistryProtein structureComplement C1Structural BiologyGeneticsHumansTrypsinMolecular BiologyComplement C1qComplement C1sEnzyme PrecursorsComplement C1sComplement C1rChemistryComponent (thermodynamics)Complement C1qComplement component 7Immunoglobulin Fc FragmentsCell BiologyHydrogen-Ion ConcentrationImmunoglobulin Fc FragmentsComplement (complexity)BiophysicsProtein BindingFEBS Letters
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