2025
Redox modulation of the complement cascade contributes to synapse loss in Alzheimer's disease
Oh C, Wang Y, Lipton S. Redox modulation of the complement cascade contributes to synapse loss in Alzheimer's disease. Neurotherapeutics 2025, e00707. PMID: 40713246, DOI: 10.1016/j.neurot.2025.e00707.Peer-Reviewed Original ResearchAberrant S-nitrosylationAlzheimer's diseaseRedox-mediated posttranslational modificationSynaptic lossNitric oxide (NO)-related speciesReactive nitrogen speciesPhagocytosis of synapsesProgression of ADCorrelated to cognitive declineComplement systemPosttranslational modificationsInnate immune systemSenile plaquesSynapse lossS-nitrosylationDying CellsImmune responseRedox modulationComplement cascadeSpeciesCentral nervous systemComplement proteinsNitrosative stressComplementAlzheimer
2024
Complement factor H in molecular regulation of angiogenesis
Li J, Wang K, Starodubtseva M, Nadyrov E, Kapron C, Hoh J, Liu J. Complement factor H in molecular regulation of angiogenesis. Medical Review 2024, 4: 452-466. PMID: 39444793, PMCID: PMC11495524, DOI: 10.1515/mr-2023-0048.Peer-Reviewed Original ResearchComplement factor HComplement factor H geneAge-related macular degenerationComplement factor H proteinFactor HComplement activation fragmentsC-reactive proteinAnti-angiogenic effectsEndothelial heparan sulfateChoroidal neovascularizationMacular degenerationRegulation of angiogenesisMolecular regulation of angiogenesisDeficient miceComplement 3aMembrane attack complexComplement 5aPro-angiogenic eventsAngiogenesis-related diseasesCFH expressionPro-angiogenic capacityAlternative pathwayTherapeutic potentialComplement systemBlood vessels
2023
Functional Analysis of a Novel Complement C5a Receptor 1-Blocking Monoclonal Antibody
Cyranka L, Mariegaard I, Skjødt M, Bayarri-Olmos R, Mollnes T, Garred P, Rosbjerg A. Functional Analysis of a Novel Complement C5a Receptor 1-Blocking Monoclonal Antibody. Journal Of Innate Immunity 2023, 15: 836-849. PMID: 37952515, PMCID: PMC10691831, DOI: 10.1159/000535084.Peer-Reviewed Original ResearchConceptsC5a receptor 1C5aR1 inhibitionPolymorphonuclear leukocytesComplement C5a receptor 1Receptor 1Monoclonal antibodiesWhole bloodActivation markers CD11bIsolated polymorphonuclear leukocytesPotential therapeutic candidateInflammatory disease treatmentWhole blood modelCalcium flux assaysCell-binding studiesMouse monoclonal antibodyC5a-C5aR1Marker CD11bTherapeutic candidateHuman whole bloodC5aCalcium fluxComplement systemC5aR1Hybridoma clonesDisease treatment
2021
Broadly effective metabolic and immune recovery with C5 inhibition in CHAPLE disease
Ozen A, Kasap N, Vujkovic-Cvijin I, Apps R, Cheung F, Karakoc-Aydiner E, Akkelle B, Sari S, Tutar E, Ozcay F, Uygun DK, Islek A, Akgun G, Selcuk M, Sezer OB, Zhang Y, Kutluk G, Topal E, Sayar E, Celikel C, Houwen RHJ, Bingol A, Ogulur I, Eltan SB, Snow AL, Lake C, Fantoni G, Alba C, Sellers B, Chauvin SD, Dalgard CL, Harari O, Ni YG, Wang MD, Devalaraja-Narashimha K, Subramanian P, Ergelen R, Artan R, Guner SN, Dalgic B, Tsang J, Belkaid Y, Ertem D, Baris S, Lenardo MJ. Broadly effective metabolic and immune recovery with C5 inhibition in CHAPLE disease. Nature Immunology 2021, 22: 128-139. PMID: 33398182, PMCID: PMC7856263, DOI: 10.1038/s41590-020-00830-z.Peer-Reviewed Original ResearchConceptsBlockade of C5Complement C5 inhibitorInnate immune complement systemOveractivation of complementComplement regulatory proteins CD55Healthy gut microbiomeImmune complement systemCD55 deficiencyComplement hyperactivationImmune recoveryImmunoglobulin replacementGastrointestinal pathologyNormal immunityC5 inhibitionC5 inhibitorImmunoglobulin concentrationsMedical treatmentPathophysiological manifestationsInnate immunityLethal diseaseGut microbiomeProteins CD55Complement systemDiseaseHuman data
2020
Circulating Ficolin-2 and Ficolin-3 Form Heterocomplexes.
Jarlhelt I, Pilely K, Clausen J, Skjoedt M, Bayarri-Olmos R, Garred P. Circulating Ficolin-2 and Ficolin-3 Form Heterocomplexes. The Journal Of Immunology 2020, 204: 1919-1928. PMID: 32094208, DOI: 10.4049/jimmunol.1900694.Peer-Reviewed Original ResearchConceptsProtein complexesHeteromeric protein complexesNovel protein complexChinese hamster ovary cellsHamster ovary cellsPattern recognition moleculesHeterocomplexWestern blot analysisInnate immune systemBiological relevanceOvary cellsBlot analysisRecognition moleculesFicolin-2Soluble pattern recognition moleculesFicolin-3Lectin pathwayComplexesImmune systemCoimmunoprecipitationComplement systemMolecules
2019
Innate Immunity: Recognition and Effector Functions
Kavathas P, Krause P, Ruddle N. Innate Immunity: Recognition and Effector Functions. 2019, 39-53. DOI: 10.1007/978-3-030-25553-4_3.ChaptersDanger-associated molecular patternsPathogen-associated molecular patternsTypes of pathogensMolecular patternsInducer of inflammationSecretion of cytokinesTypes of receptorsChronic inflammationInflammatory responseEffector mechanismsEffector functionsInnate immunityInflammationComplement systemComplement proteinsMicrobial invasionReceptorsFighting infectionsInfectionCell-cell communicationSecretionCell stressNucleic acidsPathogensCellsProteomics-Based Comparative Mapping of the Secretomes of Human Brown and White Adipocytes Reveals EPDR1 as a Novel Batokine
Deshmukh A, Peijs L, Beaudry J, Jespersen N, Nielsen C, Ma T, Brunner A, Larsen T, Bayarri-Olmos R, Prabhakar B, Helgstrand C, Severinsen M, Holst B, Kjaer A, Tang-Christensen M, Sanfridson A, Garred P, Privé G, Pedersen B, Gerhart-Hines Z, Nielsen S, Drucker D, Mann M, Scheele C. Proteomics-Based Comparative Mapping of the Secretomes of Human Brown and White Adipocytes Reveals EPDR1 as a Novel Batokine. Cell Metabolism 2019, 30: 963-975.e7. PMID: 31668873, DOI: 10.1016/j.cmet.2019.10.001.Peer-Reviewed Original ResearchConceptsHuman adipocytesExtracellular matrix proteinsWhite adipocytesComparative mappingAdipose secretomeMatrix proteinsMetabolic crosstalkImportant regulatorFunctional studiesProtein 1ProteinBrown adipocytesSecretomeWhite adipose tissueWhite adipose depotsProteomicsAdipocytesBrown adiposeGrowth factorHuman brownCell mediumBatokinesAdipose depotsAdipose tissueComplement systemCombining MAP‐1:CD35 or MAP‐1:CD55 fusion proteins with pattern‐recognition molecules as novel targeted modulators of the complement cascade
Pérez‐Alós L, Bayarri‐Olmos R, Skjoedt M, Garred P. Combining MAP‐1:CD35 or MAP‐1:CD55 fusion proteins with pattern‐recognition molecules as novel targeted modulators of the complement cascade. The FASEB Journal 2019, 33: 12723-12734. PMID: 31469600, PMCID: PMC6902692, DOI: 10.1096/fj.201901643r.Peer-Reviewed Original ResearchConceptsMannose-binding lectinComplement cascadePattern recognition moleculesFeasible therapeutic optionLevels of C3Lectin pathwayEffective therapeutic approachTerminal effector functionsComplement activation assaysSites of inflammationComplement receptor 1Membrane-anchored regulatorTerminal complement complexTherapeutic optionsInflammatory pathologyLP activationTherapeutic approachesEffector functionsDecay-accelerating factorFicolin-3Receptor 1CD35Complement complexMAP-1Complement systemThe role of Mannose Binding Lectin in the immune response against Borrelia burgdorferi sensu lato
Coumou J, Wagemakers A, Narasimhan S, Schuijt TJ, Ersoz JI, Oei A, de Boer OJ, Roelofs JJTH, Fikrig E, Hovius JW. The role of Mannose Binding Lectin in the immune response against Borrelia burgdorferi sensu lato. Scientific Reports 2019, 9: 1431. PMID: 30723261, PMCID: PMC6363739, DOI: 10.1038/s41598-018-37922-8.Peer-Reviewed Original ResearchConceptsMannose-binding lectinB. burgdorferiImmune responseComplement systemRole of MBLMBL-deficient miceWhole blood stimulationIgG serum antibodiesB. burgdorferi infectionB. burgdorferi numbersHost complement systemMechanism warrants further investigationSerum-sensitive isolatesBorrelia burgdorferi sensu lato groupWarrants further investigationBorrelia burgdorferi sensu latoLater time pointsBinding lectinsSevere courseBlood stimulationDetectable antibodiesBurgdorferi sensu latoSerum antibodiesMBL deficiencyDeficient mice
2018
Chimeric Proteins Containing MAP-1 and Functional Domains of C4b-Binding Protein Reveal Strong Complement Inhibitory Capacities
Hertz C, Bayarri-Olmos R, Kirketerp-Møller N, van Putten S, Pilely K, Skjoedt M, Garred P. Chimeric Proteins Containing MAP-1 and Functional Domains of C4b-Binding Protein Reveal Strong Complement Inhibitory Capacities. Frontiers In Immunology 2018, 9: 1945. PMID: 30210498, PMCID: PMC6120983, DOI: 10.3389/fimmu.2018.01945.Peer-Reviewed Original ResearchConceptsChimeric proteinFunctional domainsNetwork of proteinsMAP-1Dependent dimerizationN-terminusPattern recognition moleculesHuman C4BPCHO cellsLectin pathwayProteinComplement systemCo-factor activitySingle inhibitorRecognition moleculesC4BPComplement inhibitory propertiesPathwayComplement cascadeNovel therapeutic approachesAdaptive immune responsesDifferent inflammatory diseasesActivationCascadeInhibitorsCommon and rare genetic variants of complement components in human disease
Goicoechea de Jorge E, López Lera A, Bayarri-Olmos R, Yebenes H, Lopez-Trascasa M, Rodríguez de Córdoba S. Common and rare genetic variants of complement components in human disease. Molecular Immunology 2018, 102: 42-57. PMID: 29914697, DOI: 10.1016/j.molimm.2018.06.011.Peer-Reviewed Original ResearchConceptsGenetic variabilityGenetic variantsImportant genotype-phenotype correlationsDetailed functional characterizationRare genetic variantsFunctional characterizationHuman diseasesGenotype-phenotype correlationGenetic makeupFunctional implicationsDevelopment of diseaseComplement systemComplement variantsCommon polymorphismsPathogenic mechanismsComplement proteinsVariantsUnknown featuresNumber of reportsProteinKey insightsPrecision medicine approachRegulationParticular diseaseComplement components
2016
Clinical Practice Guidelines for the Management of Atypical Hemolytic Uremic Syndrome in Korea
Cheong H, Jo S, Yoon S, Cho H, Kim J, Kim Y, Koo J, Park Y, Park Y, Shin J, Yoo K, Oh D. Clinical Practice Guidelines for the Management of Atypical Hemolytic Uremic Syndrome in Korea. Journal Of Korean Medical Science 2016, 31: 1516-1528. PMID: 27550478, PMCID: PMC4999392, DOI: 10.3346/jkms.2016.31.10.1516.Peer-Reviewed Original ResearchConceptsAtypical hemolytic uremic syndromeHemolytic uremic syndromeUremic syndromeManagement of atypical hemolytic uremic syndromeTreatment of atypical hemolytic uremic syndromePathogenesis of atypical hemolytic uremic syndromeMicro-angiopathic hemolytic anemiaEnd-stage renal diseaseAcute kidney injuryTreatment of patientsClinical practice guidelinesThrombotic microangiopathyDelayed DiagnosisKidney injuryRare syndromeHemolytic anemiaComplement C5 activationRenal diseaseAppropriate managementEffective agentKorean populationSyndromeComplement systemLack of evidenceC5 activation
2015
Targeting Host Complement C3a/C5a Receptors to Control of Acute Graft-Versus-Host Disease in Mice
Nguyen H, Heinrichs J, Fu J, Wu Y, Bastian D, Schutt S, Daenthanasanmak A, Dany M, Liu C, Fairlie D, Tomlinson S, Yu X. Targeting Host Complement C3a/C5a Receptors to Control of Acute Graft-Versus-Host Disease in Mice. Blood 2015, 126: 3076. DOI: 10.1182/blood.v126.23.3076.3076.Peer-Reviewed Original ResearchC3aR/C5aRAntigen presenting cellsDonor T cellsT cellsGVL activityHost diseaseC5aR signalingAlloreactive donor T cellsDonor T cell activationDonor T-cell responsesHost antigen presenting cellsAllogeneic hematopoietic cell transplantationComplement systemAcute Graft-VersusControl of GVHDHost hematopoietic cellsDevelopment of GVHDGVHD target organsAdaptive immune cellsHematopoietic cell transplantationEffector T cellsT cell responsesTotal body irradiationAlloreactive T cellsPro-inflammatory cytokines
2003
The evolving roles of cell surface proteases in health and disease: Implications for developmental, adaptive, inflammatory, and neoplastic processes
Madri JA. The evolving roles of cell surface proteases in health and disease: Implications for developmental, adaptive, inflammatory, and neoplastic processes. Current Topics In Developmental Biology 2003, 54: 391-410. PMID: 12696757, DOI: 10.1016/s0070-2153(03)54016-9.Peer-Reviewed Original ResearchConceptsCell surface proteolysisCell surface proteaseSurface proteolysisSurface proteaseDiversity of enzymesExtracellular matrix remodelingMaintenance of homeostasisBiological functionsMatrix remodelingAdaptive responseNormal homeostasisProteolytic responseCell proliferationProteolysisProtease activityEnzyme systemGeneral importanceHomeostasisProteaseCell attractionVascular systemDegenerative diseasesImportant processNeoplastic processComplement system
1999
ETIOPATHOGENESIS OF ACUTE PANCREATITIS
Karne S, Gorelick F. ETIOPATHOGENESIS OF ACUTE PANCREATITIS. 1999, 79: 699-710. PMID: 10470320, DOI: 10.1016/s0039-6109(05)70036-0.Peer-Reviewed Original ResearchConceptsAcute pancreatitisCourse of APPotent proteolytic enzymesCapillary leak syndromeAcinar cellsPreliminary clinical studySpecific clinical settingsSystemic complicationsLeak syndromeCytokine inhibitorsInflammatory moleculesCascade of eventsInflammatory cellsPancreatic edemaVasoactive moleculesClinical studiesParticular neutrophilsPancreatitisFurther secretionClinical settingNitric oxideComplement systemCytokinesPremature activationImmediate release
1995
Anti-C5 monoclonal antibody therapy prevents collagen-induced arthritis and ameliorates established disease.
Wang Y, Rollins S, Madri J, Matis L. Anti-C5 monoclonal antibody therapy prevents collagen-induced arthritis and ameliorates established disease. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 8955-8959. PMID: 7568051, PMCID: PMC41086, DOI: 10.1073/pnas.92.19.8955.Peer-Reviewed Original ResearchConceptsCollagen-induced arthritisRheumatoid arthritisComplement activationAnti-C5 mAbInflammatory joint diseaseOnset of arthritisMonoclonal antibody therapyTerminal complement activationAttractive therapeutic targetJoint inflammationAntibody therapySystemic administrationJoint diseaseNumerous disease statesImmunized animalsArthritisAnimal modelsTherapeutic targetPotent mediatorTerminal complement componentsActivated componentsComplement cascadeComplement componentsComplement systemMonoclonal antibodies
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