Search results for "Kininogens"

showing 10 items of 11 documents

Analysis of cold activation of the contact system in hereditary angioedema with normal C1 inhibitor.

2021

Hereditary angioedema (HAE) attacks are caused by excessive activation of the contact system. Understanding how the contact system is activated in HAE, especially in patients with normal C1 inhibitor (HAEnCI), is essential to effectively treat this disease. Contact system activation involves the cleavage of several proteins including Factor XII (FXII), high molecular weight kininogen (HK), prekallikrein, sgp120 (ITIH4) and C1 inhibitor (C1-INH) before the subsequent generation of bradykinin that mediates HAE. In this study, we evaluated the fragmentation and enzymatic activity of contact system proteins in HAEnCI plasma samples before and after contact system activation induced by incubatio…

0301 basic medicineAdultMalemedicine.medical_specialtyHigh-molecular-weight kininogenImmunologyProteinase Inhibitory Proteins SecretoryBradykininBradykininC1-inhibitorHereditary Angioedema Type III03 medical and health scienceschemistry.chemical_compoundYoung Adult0302 clinical medicineInternal medicinemedicineHumansFragmentation (cell biology)Molecular BiologyBlood CoagulationFactor XIIbiologyKininogensPrekallikreinPrekallikreinEstrogensPlasminogenKallikreinMiddle Agedmedicine.diseaseCold Temperature030104 developmental biologyEndocrinologychemistryHereditary angioedemaFactor XIIbiology.proteinFemaleKallikreinsComplement C1 Inhibitor Protein030215 immunologyMolecular immunology
researchProduct

Assembly of human contact phase proteins and release of bradykinin at the surface of curli-expressing Escherichia coli.

1996

Previous work has demonstrated that most strains of the human pathogen Streptococcus pyogenes bind kininogens through M protein, a fibrous surface protein and virulence determinant. Here we find that strains of several other pathogenic bacterial species, both Gram-positive and Gram-negative, isolated from patients with sepsis, also bind kininogens, especially kininogen (HK). The most pronounced interaction was seen between HK and Escherichia coli. Among clinical isolates of E. coli, the majority of the enterohaemorrhagic, enterotoxigenic, and sepsis strains, but none of the enteroinvasive and enteropathogenic strains, bound HK. Binding of HK to E. coli correlated with the expression of curl…

Factor XIIKininogenGram-Negative Facultatively Anaerobic RodsStaphylococcus aureusKininogensPrekallikreinVirulenceProteinsKallikreinBiologybiology.organism_classificationmedicine.disease_causeBradykininMicrobiologyMicrobiologyStreptococcus pneumoniaeStreptococcus pyogenesmedicineEscherichia coliHumansMolecular BiologyEscherichia coliBacteriacirculatory and respiratory physiologyMolecular microbiology
researchProduct

Mapping the cell binding site on high molecular weight kininogen domain 5.

1995

Investigations mapped the region(s) on the light chain of high molecular weight kininogen (HK) that participates in cell binding. Sequential and overlapping peptides of domain 5 (D5H) were synthesized to determine its cell binding site(s). Three peptides from non-overlapping regions on D5H were found to inhibit biotin-HK binding to endothelial cells. Peptides GKE19 and HNL 21 weakly inhibited biotin-HK binding with IC50 of 792 and 215 microM, respectively. Peptide HKH20 inhibited biotin-HK binding with an IC50 of 0.2 microM. Two peptides, GGH18 and HVL24, which overlapped HKH20, also inhibited biotin-HK binding to endothelial cells with IC50 values of 108 and 0.8 microM, respectively. Bioti…

High-molecular-weight kininogenMolecular Sequence DataBiotinPeptideBiochemistryHumansAmino Acid SequenceBinding siteMolecular BiologyCells Culturedchemistry.chemical_classificationKininogenBinding SitesbiologyCoagulantsKininogensCell BiologyMolecular biologyPeptide FragmentsMolecular WeightEnzymechemistryPolyclonal antibodiesBiotinylationbiology.proteinEndothelium VascularAntibodyProtein BindingThe Journal of biological chemistry
researchProduct

Identification of an endothelial cell binding site on kininogen domain D3

1995

High and low molecular mass kininogen, two multidomain plasma proteins, bind to endothelial cells, platelets, and neutrophils in the intravascular compartment. The specific cell attachment site on their common heavy chain is mediated by domain-3, a cystatin-like structure with inhibitory capacity for papain-like proteinases (Jiang, Y., Müller-Esterl, W., and Schmaier, A. H. (1992) J. Biol. Chem. 267, 3712-3717). In this report, the domain-3 cell binding site is determined by an antibody-directed strategy. The epitope of monoclonal antibody HKH15, which binds to domain-3 and blocks the binding of kininogens to platelets and endothelial cells, was mapped using seven synthetic peptides, which …

Kininogen bindingBlotting WesternMolecular Sequence DataBiotinBinding CompetitiveBiochemistryEpitopeEpitopesHumansAmino Acid SequenceBinding siteMolecular BiologyKininogenBinding SitesMolecular massKininogensChemistryAntibodies MonoclonalCell BiologyMolecular biologyEndothelial stem cellBiochemistryBiotinylationEndothelium VascularCystatinPeptidesJournal of Biological Chemistry
researchProduct

Mapping of the high molecular weight kininogen binding site of prekallikrein. Evidence for a discontinuous epitope formed by distinct segments of the…

1993

Prekallikrein, a glycoprotein involved in contact phase activation, circulates in plasma in the form of a binary complex with high molecular weight kininogen (H-kininogen). The binding to H-kininogen is mediated by the prekallikrein heavy chain consisting of four repetitive domains, A1-A4. To define more precisely the region(s) involved in kininogen binding, we have employed an affinity cross-linking strategy with a synthetic peptide of 31 residues which mimics the prekallikrein binding site of H-kininogen. Cross-linking of the radiolabeled peptide to (pre)kallikrein revealed a binding segment in the NH2-terminal portion of the prekallikrein heavy chain; another binding segment was located …

Kininogen bindingHigh-molecular-weight kininogenMacromolecular SubstancesMolecular Sequence DataEnzyme-Linked Immunosorbent AssayBiochemistryBinding CompetitiveIodine RadioisotopesHigh molecular weight kininogen bindingEpitopesZymogenHumansAmino Acid SequenceBinding siteMolecular BiologyKininogenBinding SitesChemistryKininogensPrekallikreinPrekallikreinCell BiologyKallikreinPeptide FragmentsModels StructuralMolecular WeightKineticsBiochemistryAutoradiographyElectrophoresis Polyacrylamide GelPeptidescirculatory and respiratory physiology
researchProduct

Human kininogens interact with M protein, a bacterial surface protein and virulence determinant.

1995

Streptococcus pyogenes, the most significant streptococcal species in clinical medicine, expresses surface proteins with affinity for several human plasma proteins. Here we report that kininogens, the precursors to the vasoactive kinins, bind to the surface of S. pyogenes. M protein, a surface molecule and a major virulence factor-in these bacteria, occurs in > 80 different serotypes. Among 49 strains of S. pyogenes, all of different M serotypes, 41 bound radiolabelled kininogens, whereas 6 M protein-negative mutant strains showed no affinity. M protein of most serotypes bind fibrinogen, and among the 55 strains tested, binding of kininogens was closely correlated to fibrinogen bindi…

Kininogen bindingMyeloma proteinStreptococcus pyogenesM1 proteinMolecular Sequence DataEnzyme-Linked Immunosorbent Assaymedicine.disease_causeBiochemistryPeptide MappingAntibodiesBacterial ProteinsmedicineHumansAmino Acid SequenceBinding siteMolecular BiologyKininogenAntigens BacterialBinding SitesbiologyVirulenceKininogensFibrinogen bindingFibrinogenCell BiologyLow-molecular-weight kininogenMolecular biologyStreptococcus pyogenesbiology.proteinCarrier Proteinscirculatory and respiratory physiologyResearch ArticleBacterial Outer Membrane ProteinsProtein Binding
researchProduct

Tissue kallikrein and kininogen in human sweat glands and psoriatic skin

1991

The cellular localization of immunoreactive tissue kallikrein and kininogen was studied in normal and psoriatic human skin. Immunoreactivity to both enzyme and substrate was observed in secretory granules of the dark cells in the secretory fundus (acinus) of the sweat glands. Double immunostaining revealed a segmental distribution of the two antigens. Each acinar section contained either tissue kallikrein or kininogen. However, there appeared to be a junctional zone in which both were present, but in separate dark cells. Immunoreactivity for both antigens was also observed in close apposition to the luminal microvilli of the duct cells. No specific immunostaining was seen in sebaceous gland…

Kininogenmedicine.medical_specialtyPathologyStaining and LabelingKininogensTissue kallikreinMyoepithelial cellHuman skinDermatologyKallikreinBiologyKininImmunohistochemistrySweat GlandsEndocrinologymedicine.anatomical_structureSweat glandInternal medicinemedicineHumansPsoriasisKallikreinsCellular localizationSkincirculatory and respiratory physiologyBritish Journal of Dermatology
researchProduct

Genome- wide association study with additional genetic and post-transcriptional analyses reveals novel regulators of plasma factor XI levels

2017

International audience; Coagulation factor XI (FXI) has become increasingly interesting for its role in pathogenesis of thrombosis. While elevated plasma levels of FXI have been associated with venous thromboembolism and ischemic stroke, its deficiency is associated with mild bleeding. We aimed to determine novel genetic and post-transcriptional plasma FXI regulators.We performed a genome-wide association study (GWAS) for plasma FXI levels, using novel data imputed to the 1000 Genomes reference panel. Individual GWAS analyses, including a total of 16,169 European individuals from the ARIC, GHS, MARTHA and PROCARDIS studies, were meta-analysed and further replicated in 2,045 individuals from…

Male0301 basic medicineIn silicoReceptors Cell SurfaceSingle-nucleotide polymorphismGenome-wide association study030204 cardiovascular system & hematologyBiologyPolymorphism Single Nucleotide03 medical and health sciences0302 clinical medicine[SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular system[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]GeneticsmedicineHumansComputer SimulationGene Regulatory NetworksGenetic Predisposition to Disease1000 Genomes ProjectMolecular BiologyGeneGenetics (clinical)Adaptor Proteins Signal TransducingGeneticsmedicine.diagnostic_testKininogensAssociation Studies ArticlesHaplotypeThrombosisGeneral Medicine3. Good health030104 developmental biologyGene Expression RegulationFemalePartial Thromboplastin TimeCell Adhesion MoleculesProtein Processing Post-TranslationalImputation (genetics)Genome-Wide Association StudyPartial thromboplastin time
researchProduct

Absorption of kininogen from human plasma by Streptococcus pyogenes is followed by the release of bradykinin.

1997

H-kininogen (high-molecular-mass kininogen, HK) is the precursor of the vasoactive peptide hormone bradykinin (BK). Previous work has demonstrated that HK binds to Streptococcus pyogenesthrough M-proteins, fibrous surface proteins and important virulence factors of these bacteria. Here we find that M-protein-expressing bacteria absorb HK from human plasma. The HK bound to the bacteria was found to be cleaved, and analysis of the degradation pattern suggested that the cleavage of HK at the bacterial surface is associated with the release of BK. Moreover, addition of activated plasma prekallikrein to bacteria preincubated with human plasma, resulted in BK release. This mechanism, by which a p…

chemistry.chemical_classificationKininogenbiologyKininogensStreptococcus pyogenesBradykininVirulencePeptideCell BiologyPlasma protein bindingbiology.organism_classificationmedicine.disease_causeBradykininBiochemistryMicrobiologyProinflammatory cytokinechemistry.chemical_compoundchemistryStreptococcus pyogenesmedicineHumansMolecular BiologyBacteriaProtein BindingResearch Article
researchProduct

Hereditary angioneurotic oedema and blood-coagulation: interaction between C1-esterase-inhibitor and the activation factors of the proteolytic enzyme…

1983

C-1-inactivator (C-1-INA) does not only exert its important inhibitory functions in the complement system but also in the first step in the activation of the coagulation, fibrinolytic and kallikrein system. We therefore determined in nine patients with hereditary angioneurotic oedema (HANE) with obvious quantitative or functional defects of C-1-INA, and one further patient with Quincke-type oedema of different origin, the coagulation factors of the initial phase such as Hageman factor, plasma thromboplastin antecedent (PTA) and high molecular weight kininogen (HMWK). These factors were further correlated with the concentration as well as functional activity of C-1-INA. Nine of ten patients …

medicine.medical_specialtyHigh-molecular-weight kininogenInternal medicineDrug DiscoverymedicineHumansAngioedemaFactor XIBlood CoagulationGenetics (clinical)Factor XIFactor XIIComplement C1sChemistryKininogensProteolytic enzymesGeneral MedicineKallikreinMolecular medicineBlood Coagulation FactorsComplement systemEnzyme ActivationEndocrinologyCoagulationFactor XIIMolecular MedicinePeptide HydrolasesKlinische Wochenschrift
researchProduct