Search results for "Complement Activation"

showing 10 items of 56 documents

The apolipoprotein(a) moiety of lipoprotein(a) interacts with the complement activation fragment iC3b but does not functionally affect C3 activation …

1992

A previous study has shown that complement component C3 binds to recombinant apolipoprotein(a) (r-apo(a)). In the present report we have investigated the interactions between lipoprotein(a) (Lp(a)), r-apo(a) and C3 in relation to complement activation and degradation. Neither Lp(a) nor r-apo(a) affected complement activation as indicated by sheep and rabbit red blood cell hemolytic assays, and by assessment of the amount of C3a generated in zymosan-activated human serum in the presence or absence of Lp(a). Crossed immunoelectrophoretic analyses indicated that Lp(a) retarded the migration of iC3b in complement-activated serum but had no effects on C3, C3b, C3c or C3dg. Recombinant apo(a) exh…

Apolipoprotein BLipoproteinsApoprotein(a)chemistry.chemical_compoundHumansComplement ActivationbiologyComplement C3Lipoprotein(a)N-Acetylneuraminic AcidComplement systemSialic acidApolipoproteinsBiochemistrychemistryLow-density lipoproteinComplement C3bSialic Acidsbiology.proteiniC3bElectrophoresis Polyacrylamide Gellipids (amino acids peptides and proteins)Cardiology and Cardiovascular MedicineImmunoelectrophoresis Two-DimensionalN-Acetylneuraminic acidLipoprotein(a)LipoproteinAtherosclerosis
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Isolation and characterization of a complement-activating lipid extracted from human atherosclerotic lesions.

1990

The major characteristics of human atherosclerotic lesions are similar to those of a chronic inflammatory reaction, namely fibrosis, mesenchymal cell proliferation, the presence of resident macrophages, and cell necrosis. Atherosclerosis exhibits in addition the feature of lipid (mainly cholesterol) accumulation. The results of the present report demonstrate that a specific cholesterol-containing lipid particle present in human atherosclerotic lesions activates the complement system to completion. Thus, lipid could represent a stimulatory factor for the inflammatory reaction, whose underlying mechanistic basis may be, at least in part, complement activation. The complement-activating lipid …

ArteriosclerosisComplement Pathway AlternativeImmunologyInflammationMuscle Smooth VascularC5-convertasechemistry.chemical_compoundMesenchymal cell proliferationmedicineHumansImmunology and AllergyComplement ActivationImmunoelectrophoresisAortaTriglyceridesCholesterolFatty AcidsComplement System ProteinsArticlesLipidsComplement systemCarotid ArteriesCholesterolchemistryBiochemistryLow-density lipoproteinChromatography GelAlternative complement pathwaylipids (amino acids peptides and proteins)Lipid particlemedicine.symptomJournal of Experimental Medicine
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Complement and atherogenesis: The unknown connection

1999

The question why low-density lipoprotein (LDL) stranded in the subendothelium of arteries should acquire the proinflammatory properties that initiate and sustain atherogenesis has puzzled researchers for decades. The most popular concept contends that oxidative processes are crucial because oxidized LDL (ox-LDL) produced in vitro has atherogenic properties and small amounts of it are found in atherosclerotic lesions. Recently, a possible role for vascular infections has also been considered because infectious agents, in particular Chlamydia pneumoniae, are sometimes present in the lesions. Here, evidence is summarized for a different concept of atherogenesis, which evolves from the fact tha…

ArteriosclerosisVascular diseaseInflammationGeneral MedicineChlamydia InfectionsChlamydophila pneumoniaeMacrophage ActivationBiologymedicine.diseaseProinflammatory cytokineLipoproteins LDLPathogenesischemistry.chemical_compoundImmune systemchemistryLow-density lipoproteinImmunologymedicineHumansMacrophagelipids (amino acids peptides and proteins)medicine.symptomComplement ActivationLipoproteinAnnals of Medicine
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An inherited deficiency of the third component of complement, C3, in guinea pigs

1986

Hereditary deficiency of the third component of complement, C3, is found very seldom in the human. C3 deficiency is associated with severe bacterial infections revealing the central role of C3 in complement activation via the classical or alternative pathway. We describe a new hereditary C3 deficiency in strain 2 guinea pigs. Serum from these animals had a markedly reduced lytic activity in a standard assay for complement-dependent, antibody-mediated cytotoxicity. In functional assays of individual components, the hemolytic activity of the components C4, C2, C5 and of factors B, D and H was in the normal range. The functional C3 titer, and similarly C3 antigenic activity in the serum of the…

Blood Bactericidal ActivityGuinea PigsImmunologyMacrophage-1 Antigenchemical and pharmacologic phenomenaBiologyHemolysisMajor Histocompatibility ComplexGuinea pigInbred strainAntigenIn vivoAnimalsImmunology and AllergyComplement ActivationRecombination GeneticComplement C3Molecular biologyIn vitroPedigreeReceptors ComplementComplement systemImmunologyAlternative complement pathwaybiology.proteinC3a receptorEuropean Journal of Immunology
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Functionally active complement proteins C6 and C7 detected in C6- and C7-deficient individuals

1991

SUMMARYTwo sensitive sandwich ELISAs based on monoclonal antibodies directed to native C6 and C7 allowed the detection and quantitation of these complement proteins in 20 out of 37 serum samples from individuals who had previously been classified as deficient in these proteins as assessed by immunochemical and/or functional assays. Furthermore, serum from four C6-deficient and one combined C6-/C7-deficient individual showed an increase in the terminal complement complex (TCC) and a decrease in native C6 and C7 after complement activation as assayed by specific ELISAs. Despite their (incomplete) deficiencies, these individuals therefore possess functionally active terminal complement protein…

Blood Bactericidal Activitymedicine.drug_classImmunoblottingImmunologyEnzyme-Linked Immunosorbent AssayBiologyMonoclonal antibodyComplement Hemolytic Activity AssaySpecimen Handling03 medical and health sciences0302 clinical medicineTerminal complement complexImmunopathologymedicineHumansImmunology and AllergyComplement ActivationVolume concentration030304 developmental biology0303 health sciencesTemperatureZymosanAntibodies MonoclonalComplement deficiencyComplement C9Serum samplesmedicine.diseaseMolecular biologyComplement C7Complement C63. Good healthComplement (complexity)Complement systemImmunologyElectrophoresis Polyacrylamide GelResearch Article030215 immunologyClinical and Experimental Immunology
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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 human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, …

2001

The proteases of the lectin pathway of complement activation, MASP-1 and MASP-2, are encoded by two separate genes. The MASP1 gene is located on chromosome 3q27, the MASP2 gene on chromosome 1p36.23-31. The genes for the classical complement activation pathway proteases, C1r and C1s, are linked on chromosome 12p13. We have shown that the MASP2 gene encodes two gene products, the 76 kDa MASP-2 serine protease and a plasma protein of 19 kDa, termed MAp19 or sMAP. Both gene products are components of the lectin pathway activation complex. We present the complete primary structure of the human MASP2 gene and the tight cluster that this locus forms with non-complement genes. A comparison of the …

Chromosomes Artificial BacterialTranscription GeneticGenetic LinkageRNA SplicingImmunologyMolecular Sequence DataBiologyGeneticsHumansPromoter Regions GeneticComplement ActivationGenetics (clinical)Mannan-binding lectinGeneticsComplement component 2Base SequenceCD69Serine EndopeptidasesC4AChromosome MappingCollectinsKLRB1Chromosomes Human Pair 1Lectin pathwayMannose-Binding Protein-Associated Serine ProteasesMultigene Familybiology.proteinCarrier ProteinsMASP2MASP1
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Combined complete C5 and partial C4 deficiency in humans: clinical consequences and complement-mediated functions in vitro.

1990

A family is described with two siblings who suffered at different times from a single episode of meningococcal meningitis by Neisseria meningitidis groups B and C, respectively. In the two subjects, hemolytically active fifth component of complement (C5) was not detectable and antigenic C5 was less than 0.05% and less than 0.7% of normal, respectively. Repletion of sera by purified human C5 (70 micrograms/ml) restored total complement hemolytic activities. The asymptomatic first degree family members had C5 levels compatible with a heterozygous state of C5 deficiency. C4 allotyping revealed an inherited partial deficiency (Q0) of C4A and C4B in the family with a combined C4AQ0 and C4BQ0 het…

Complement component 5AdultMaleAdolescentImmunologyC4AComplement C5Complement C4C5 DeficiencyBiologyPathology and Forensic MedicinePedigreeClassical complement pathwayImmune systemAntigenImmunologyAlternative complement pathwayImmunology and AllergyHumansFemaleImmunoglobulin AllotypesOpsoninComplement ActivationClinical immunology and immunopathology
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P-selectin glycoprotein ligand-1 as a potential target for humoral immunotherapy of multiple myeloma.

2008

Monoclonal antibodies (mAbs), successfully adopted in the treatment of several haematological malignancies, have proved almost ineffective in multiple myeloma (MM), because of the lack of an appropriate antigen for targeting and killing MM cells. Here, we demonstrate that PSGL1, the major ligand of P-Selectin, a marker of plasmacytic differentiation expressed at high levels on normal and neoplastic plasma cells, may represent a novel target for mAb-mediated MM immunotherapy. The primary effectors of mAb-induced cell-death, complement-mediated lysis (CDC) and antibody-dependent cell-mediated cytotoxicity (ADCC), were investigated using U266B1 and LP1 cell-lines as models. Along with immunolo…

Cytotoxicity ImmunologicMembrane Glycoproteinsmieloma multiplo; ab therapy; PSGL-1ab therapyAntibody-Dependent Cell CytotoxicityDrug Evaluation PreclinicalAntibodies MonoclonalBone Marrow CellsSettore MED/08 - Anatomia Patologicamultiple myelomaDrug Delivery SystemsCell Line TumorHumanscomplementimmunotherapymieloma multiploPSGL-1ADCCComplement Activationmonoclonal antibodie
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The modulation of immune complex aggregation by classical pathway-mediated reactions.

1985

Abstract Classical pathway (CP)-triggered reactions of complement-modulated immune complex(IC) aggregation (tetanus toxoid/human anti-tetanus toxoid-IgG; ICs of equivalence) were investigated turbidimetrically during the early stages of reaction. Monospecific Fab'- or Fab-fragments (rabbit) directed against certain complement components were used to block the complement function in normal human serum (NHS). Additionally, parts of the reactions were studied using purified complement components. C1q in serum generated by the addition of EDTA as well as purified C1q were found to increase the IC aggregation. In contrast to C1q, macromolecular C1 is able to inhibit IC aggregation, whereas addit…

EffectorChemistryComplement Activating EnzymesComplement C1qImmunologyToxoidHematologyAntigen-Antibody ComplexComplement System ProteinsComplement C1 Inactivator ProteinsImmune complexComplement componentsComplement (complexity)Classical complement pathwayBiochemistrySolubilityComplement C1ImmunologyImmunology and AllergyHumansComplement Pathway ClassicalComplement ActivationFunction (biology)MacromoleculeImmunobiology
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