Search results for "Citrullination"

showing 5 items of 5 documents

Externalized decondensed neutrophil chromatin occludes pancreatic ducts and drives pancreatitis

2016

Ductal occlusion has been postulated to precipitate focal pancreatic inflammation, while the nature of the primary occluding agents has remained elusive. Neutrophils make use of histone citrullination by peptidyl arginine deiminase-4 (PADI4) in contact to particulate agents to extrude decondensed chromatin as neutrophil extracellular traps (NETs). In high cellular density, NETs form macroscopically visible aggregates. Here we show that such aggregates form inside pancreatic ducts in humans and mice occluding pancreatic ducts and thereby driving pancreatic inflammation. Experimental models indicate that PADI4 is critical for intraductal aggregate formation and that PADI4-deficiency abrogates…

0301 basic medicineExtracellular TrapsHydrolasesNeutrophilsScienceGeneral Physics and AstronomyBiologyExtracellular TrapsArticleGeneral Biochemistry Genetics and Molecular BiologyMice03 medical and health sciencesPancreatic JuiceProtein-Arginine Deiminase Type 4medicineAnimalsHumansPancreasCeruletideMultidisciplinaryReverse Transcriptase Polymerase Chain ReactionQInterleukin-17Pancreatic DuctsGeneral ChemistryNeutrophil extracellular trapsFlow Cytometrymedicine.diseaseImmunohistochemistryChromatinCell biologyChromatinDisease Models AnimalHistone citrullination030104 developmental biologymedicine.anatomical_structurePancreatitisChronic DiseasePancreatic juiceImmunologyProtein-Arginine DeiminasesCytokinesPancreatitisPancreasCeruletideNature Communications
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Neonatal NET-inhibitory factor and related peptides inhibit neutrophil extracellular trap formation.

2016

Neutrophil granulocytes, also called polymorphonuclear leukocytes (PMNs), extrude molecular lattices of decondensed chromatin studded with histones, granule enzymes, and antimicrobial peptides that are referred to as neutrophil extracellular traps (NETs). NETs capture and contain bacteria, viruses, and other pathogens. Nevertheless, experimental evidence indicates that NETs also cause inflammatory vascular and tissue damage, suggesting that identifying pathways that inhibit NET formation may have therapeutic implications. Here, we determined that neonatal NET-inhibitory factor (nNIF) is an inhibitor of NET formation in umbilical cord blood. In human neonatal and adult neutrophils, nNIF inhi…

0301 basic medicineLipopolysaccharidesMaleExtracellular TrapsNeutrophilsAntimicrobial peptidesInflammationSystemic inflammationExtracellular TrapsHistones03 medical and health sciencesmedicineAnimalsHumansCells CulturedInflammationbiologyInfant NewbornGeneral MedicineNeutrophil extracellular trapsBlood ProteinsChromatin Assembly and DisassemblyFetal BloodMolecular biologyIn vitroCell biologyNeoplasm ProteinsMice Inbred C57BLHistone citrullination030104 developmental biologyHistonebiology.proteinmedicine.symptomProtein Processing Post-TranslationalResearch ArticleThe Journal of clinical investigation
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Neutrophil extracellular traps impair fungal clearance in a mouse model of invasive pulmonary aspergillosis

2019

Abstract Neutrophil extracellular traps (NETs) are formed by polymorphonuclear neutrophils (PMN) and contribute to the innate host defense by binding and killing bacterial and fungal pathogens. Because NET formation depends on histone hypercitrullination by peptidylarginine deiminase 4 (PAD4), we used PAD4 gene deficient (Pad4-/-) mice in a mouse model of invasive pulmonary aspergillosis (IPA) to address the contribution of NETs to the innate host defense in vivo. After the induction (24 h) of IPA by i.t. infection with Aspergillus fumigatus conidia, Pad4-/- mice revealed lower fungal burden in the lungs, accompanied by less acute lung injury, TNFα and citH3 compared to wildtype controls. T…

0301 basic medicineNeutrophilsImmunologyMedizinApoptosisLung injuryExtracellular TrapsArticleAspergillus fumigatusMicrobiologyMice03 medical and health sciences0302 clinical medicineProtein-Arginine Deiminase Type 4In vivomedicineAnimalsHumansImmunology and Allergyskin and connective tissue diseasesLungInvasive Pulmonary AspergillosisMice KnockoutLungbiologyAspergillus fumigatusWild typeHematologyNeutrophil extracellular trapsbiology.organism_classificationmedicine.diseaseImmunity Innaterespiratory tract diseasesMice Inbred C57BLDisease Models AnimalPneumonia030104 developmental biologymedicine.anatomical_structureCitrullinationTumor necrosis factor alpha030215 immunologyImmunobiology
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Hsp60 Post-translational Modifications: Functional and Pathological Consequences.

2020

Hsp60 is a chaperone belonging to the Chaperonins of Group I and typically functions inside mitochondria in which, together with the co-chaperonin Hsp10, maintains protein homeostasis. In addition to this canonical role, Hsp60 plays many others beyond the mitochondria, for instance in the cytosol, plasma-cell membrane, extracellular space, and body fluids. These non-canonical functions include participation in inflammation, autoimmunity, carcinogenesis, cell replication, and other cellular events in health and disease. Thus, Hsp60 is a multifaceted molecule with a wide range of cellular and tissue locations and functions, which is noteworthy because there is only one hsp60 gene. The questio…

0301 basic medicinechaperoninnon-canonical functionsReviewMitochondrioncanonical functionsBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistrychaperonopathies03 medical and health sciences0302 clinical medicineUbiquitinMolecular Bioscienceslcsh:QH301-705.5Molecular Biologybiologycanonical functions chaperonin Hsp60 non-canonical functions post-translation modificationChemistryfungiCitrullinationCell cycleHsp60Cell biology030104 developmental biologylcsh:Biology (General)Mitochondrial permeability transition pore030220 oncology & carcinogenesisChaperone (protein)biology.proteinPhosphorylationHSP60post-translation modificationFrontiers in molecular biosciences
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Identification of KRT16 as a target of an autoantibody response in complex regional pain syndrome

2016

Abstract Objective Using a mouse model of complex regional pain syndrome (CRPS), our goal was to identify autoantigens in the skin of the affected limb. Methods A CRPS-like state was induced using the tibia fracture/cast immobilization model. Three weeks after fracture, hindpaw skin was homogenized, run on 2-d gels, and probed by sera from fracture and control mice. Spots of interest were analyzed by liquid chromatography-mass spectroscopy (LC-MS) and the list of targets validated by examining their abundance and subcellular localization. In order to measure the autoantigenicity of selected protein targets, we quantified the binding of IgM in control and fracture mice sera, as well as in co…

AdultMale0301 basic medicinePathologymedicine.medical_specialtyPeripherinsTibia FractureAutoantigensProtein citrullinationArticlelaw.inventionMiceYoung Adult03 medical and health sciencesPeptide Elongation Factor 10302 clinical medicineDevelopmental NeuroscienceENO3Downregulation and upregulationlawAnimalsHumansMedicineAnnexin A2Skinbusiness.industryKeratin-6AutoantibodyMiddle Agedmedicine.diseaseHindlimbUp-RegulationMice Inbred C57BLTibial FracturesDisease Models Animal030104 developmental biologyComplex regional pain syndromeNeurologyPhosphopyruvate HydrataseImmunologyRecombinant DNABiomarker (medicine)businessComplex Regional Pain Syndromes030217 neurology & neurosurgerySubcellular FractionsExperimental Neurology
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