Search results for "CLEAVAGE"

showing 10 items of 281 documents

Cleavage of desmoglein 3 can explain its depletion from keratinocytes in pemphigus vulgaris.

2008

We have previously demonstrated that serum of patients with pemphigus vulgaris induces reduction of desmoglein 3 (Dsg3) half-life in keratinocytes (FEBS Lett 2006: 580: 3276). This phenomenon seems to occur as a consequence of the progressive depletion of Dsg3 from desmosomes. Here we reported that reduction of full-length Dsg3 may be due to its progressive cleavage, leading to the formation of two fragmentation products with apparent molecular masses of about 60 kDa (fragment 1) and 70 kDa (fragment 2), as revealed by Western blotting. Unexpectedly, analysis of fragmentation pattern suggested cleavage to occur intracellularly. Consistently, fragment 1 was shed and localized within the cyto…

KeratinocytesPathologymedicine.medical_specialtyBlotting WesternPlakoglobinDermatologyBiologyCleavage (embryo)BiochemistryCell LinemedicineHumanseducationMolecular Biologyeducation.field_of_studyDesmoglein 3Desmoglein 1Pemphigus vulgarisBlood Proteinsmedicine.diseaseMolecular biologyBlotPemphigusmedicine.anatomical_structureDesmoplakinsDesmoglein 1Desmoglein 3gamma CateninKeratinocytePemphigusExperimental dermatology
researchProduct

Processing of procollagen III by meprins: new players in extracellular matrix assembly?

2010

Meprins α and β, a subgroup of zinc metalloproteinases belonging to the astacin family, are known to cleave components of the extracellular matrix, either during physiological remodeling or in pathological situations. In this study we present a new role for meprins in matrix assembly, namely the proteolytic processing of procollagens. Both meprins α and β release the N- and C-propeptides from procollagen III, with such processing events being critical steps in collagen fibril formation. In addition, both meprins cleave procollagen III at exactly the same site as the procollagen C-proteinases, including bone morphogenetic protein-1 (BMP-1) and other members of the tolloid proteinase family. …

Keratinocytesmacromolecular substancesDermatologyMatrix metalloproteinaseCleavage (embryo)BiochemistryBone Morphogenetic Protein 1Substrate SpecificityExtracellular matrix03 medical and health sciencesDermismedicineHumansEnhancerMolecular BiologyCells Cultured030304 developmental biology0303 health sciencesExtracellular Matrix Proteinsintegumentary systemChemistryExtracellular matrix assembly030302 biochemistry & molecular biologyMetalloendopeptidasesCell BiologyDermisFibroblastsFibrosisProcollagen peptidasemedicine.anatomical_structureCollagen Type IIIHEK293 CellsBiochemistryKeloidAstacinThe Journal of investigative dermatology
researchProduct

Heat-stable antigen is expressed by murine keratinocytes and delivers costimulatory signals in T-cell activation.

1995

Heat-stable antigen (HSA), expressed by various antigen-presenting cells (APC), has been described as a costimulatory molecule for CD4+ T cells. Recently, we observed that HSA also serves as an important costimulatory molecule on epidermal Langerhans cells (LC). During these studies, low levels of HSA staining were also detected on normal murine keratinocytes (KC). To investigate whether HSA also is involved in T-cell activation by KC, normal murine KC or the spontaneously transformed KC cell-line PAM 212 were treated with PDB or PMA to induce HSA-expression. FACS analyses showed induction of HSA expression on normal murine KC, as well as PAM 212 cells. In functional assays PDB or PMA-treat…

Keratinocytesmedicine.drug_classT cellT-LymphocytesMolecular Sequence DataProtein Data Bank (RCSB PDB)DermatologyBiologyCleavage (embryo)Monoclonal antibodyLymphocyte ActivationBiochemistryMicePhosphoinositide Phospholipase CAntigenAntigens CDPhorbol EstersmedicineAnimalsInducerRNA MessengerMolecular BiologyCells CulturedMice Inbred BALB CMice Inbred C3HPhospholipase CBase SequencePhosphoric Diester HydrolasesPhosphatidylinositol Diacylglycerol-LyaseAntibodies MonoclonalMolecular biologyStainingbody regionsmedicine.anatomical_structureMolecular Probesembryonic structuresImmunizationLymph NodesExperimental dermatology
researchProduct

Hereditary angioedema cosegregating with a novel kininogen 1 gene mutation changing the N‐terminal cleavage site of bradykinin

2019

Kininogen 1 Genechemistry.chemical_compoundchemistrybusiness.industryImmunologyHereditary angioedemamedicineImmunology and AllergyBradykininmedicine.diseasebusinessCleavage (embryo)Molecular biologyAllergy
researchProduct

Alcohol oxidation by dioxygen and aldehydes catalysed by square-planar cobalt(III) complexes of disubstituted oxamides and related ligands

2001

The square-planar cobalt(III) complexes of o-phenylenebis(N′-methyloxamidate) (Me2opba) and related oxamate (Meopba) and bis(oxamate) (opba) ligands catalyse the selective oxidation, by dioxygen and pivalaldehyde, of a wide range of secondary alcohols to the corresponding ketones, in good yields and under mild conditions in acetonitrile at room temperature. Thus, the oxidation of the series of α-alkylbenzyl alcohols PhCH(OH)R (R = Me, Et, iPr, tBu) results in the exclusive formation of ketones as a product of C−H bond cleavage, and no C−C bond cleavage products are observed in any case. The modulation of catalytic activity by ligand substituents among this series of cobalt catalysts highlig…

LigandHydrideOrganic ChemistrySubstituentchemistry.chemical_elementPhotochemistryMedicinal chemistryCatalysisElectron transferchemistry.chemical_compoundchemistryAlcohol oxidationPhysical and Theoretical ChemistryCobaltBond cleavage
researchProduct

A dinucleating ligand which promotes DNA cleavage with one and without a transition metal ion.

2013

The dinucleating ligand L (1,3-bis[bis(pyridin-2-ylmethyl)amino]propan-2-ol) combined with metal ions efficiently cleaves DNA when M : L is 1 : 1 (M = Co(II) or Fe(III)) at pH 5.5–7.0, with free L being more active at acidic pH than when bound to Zn(II), Cu(II) or Ni(II) at neutral pH.

LigandPyridinesMetal ions in aqueous solutionInorganic chemistryMetals and AlloysGeneral ChemistryDNALigandsTransition metal ionsCatalysisSurfaces Coatings and FilmsElectronic Optical and Magnetic Materialschemistry.chemical_compoundchemistryDna cleavageCoordination ComplexesPolymer chemistryMaterials ChemistryCeramics and CompositesTransition ElementsNeutral phDNA CleavageDNAPlasmidsChemical communications (Cambridge, England)
researchProduct

Triazolopyridopyrimidines: an emerging family of effective DNA photocleavers. DNA binding. Antileishmanial activity.

2015

Triazolopyridopyrimidines 3-phenyl-6,8-di(2-pyridyl)-[1,2,3]triazolo[5',1':6,1]pyrido[2,3-d]pyrimidine (1a), 6,8-di(pyridin-2-yl)-[1,2,3]triazolo[1',5':1,6]pyrido[2,3-d]pyrimidine (1b) and 3-methyl-6,8-di(2-pyridyl)-[1,2,3]triazolo[5',1':6,1]pyrido[2,3-d]pyrimidine (1c) were prepared and their electrochemical and luminescence properties were studied in depth. The DNA binding ability of this series of compounds has been investigated by means of UV-vis absorption and fluorescence titrations, steady-state emission quenching with ferrocyanide as well as viscosity measurements. Results have shown that triazolopyridopyrimidine 1a interacts strongly at DNA grooves. This compound also displays pref…

LuminescencePyrimidineStereochemistryGuaninePyridinesUltraviolet RaysRadicalTriazoleSubstituentAntiprotozoal AgentsBiochemistrychemistry.chemical_compoundStructure-Activity RelationshipParasitic Sensitivity TestsStructure–activity relationshipPhysical and Theoretical ChemistryBinding siteDNA CleavageLeishmaniaBinding SitesDose-Response Relationship DrugMolecular StructureOrganic ChemistryDNAPhotochemical ProcesseschemistryHeterocyclic Compounds 3-RingDNAOrganicbiomolecular chemistry
researchProduct

The neuropeptide PACAP promotes ?‐secretase pathway for processing Alzheimer amyloid precursor protein

2006

SPECIFIC AIMSProteolytic cleavage of the amyloid precursor protein (APP) by α-secretase within the Aβ sequence precludes formation of amyloidogenic peptides and leads to a release of soluble APPsα,...

MAP kinase kinase kinasebiologyNeuropeptideMitogen-activated protein kinase kinaseCleavage (embryo)BiochemistryAlpha secretaseBiochemistrymental disordersGeneticsAmyloid precursor proteinbiology.proteinASK1Molecular BiologyBiotechnologyG protein-coupled receptorThe FASEB Journal
researchProduct

Symplekin, a polyadenylation factor, prevents MOZ and MLL activity on HOXA9 in hematopoietic cells

2013

International audience; MOZ and MLL encoding a histone acetyltransferase and a histone methyltransferase, respectively, are targets for recurrent chromosomal translocations found in acute myeloblastic or lymphoblastic leukemia. We have previously shown that MOZ and MLL cooperate to activate HOXA9 gene expression in hematopoietic stem/progenitors cells. To dissect the mechanism of action of this complex, we decided to identify new proteins interacting with MOZ. We found that the scaffold protein Symplekin that supports the assembly of polyadenylation machinery was identified by mass spectrometry. Symplekin interacts and co-localizes with both MOZ and MLL in immature hematopoietic cells. Its …

MLLScaffold proteinPolyadenylationHematopoietic System[SDV]Life Sciences [q-bio]PolyadenylationCell Line03 medical and health scienceschemistry.chemical_compound0302 clinical medicinehemic and lymphatic diseasesGene expressionTranscriptional regulationHumansRNA MessengerPromoter Regions GeneticSymplekinHSF1neoplasmsMolecular BiologyHistone Acetyltransferases030304 developmental biologyHomeodomain ProteinsmRNA Cleavage and Polyadenylation Factors0303 health sciences[ SDV ] Life Sciences [q-bio]biologyNuclear ProteinsHistone-Lysine N-MethyltransferaseHOXA9Transcription regulationCell BiologyHistone acetyltransferaseMOZCell biology[SDV] Life Sciences [q-bio]Protein TransportRUNX1chemistry030220 oncology & carcinogenesisHistone methyltransferaseCancer researchbiology.proteinMyeloid-Lymphoid Leukemia ProteinProtein BindingBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
researchProduct

Intracellular activation of ovastacin mediates pre-fertilization hardening of the zona pellucida

2017

Study question How and where is pro-ovastacin activated and how does active ovastacin regulate zona pellucida hardening (ZPH) and successful fertilization? Study finding Ovastacin is partially active before exocytosis and pre-hardens the zona pellucida (ZP) before fertilization. What is known already The metalloproteinase ovastacin is stored in cortical granules, it cleaves zona pellucida protein 2 (ZP2) upon fertilization and thereby destroys the ZP sperm ligand and triggers ZPH. Female mice deficient in the extracellular circulating ovastacin-inhibitor fetuin-B are infertile due to pre-mature ZPH. Study design, samples/materials, methods We isolated oocytes from wild-type and ovastacin-de…

Male0301 basic medicineEmbryologyPrimary Cell CultureFertilization in VitroBiologyCleavage (embryo)Zona Pellucida GlycoproteinsExocytosisExocytosisMice03 medical and health sciences0302 clinical medicineHuman fertilizationGeneticsmedicineAnimalsChymotrypsinZona pellucidaMolecular BiologyMetaphaseZona PellucidaOriginal Research030219 obstetrics & reproductive medicineGene Expression Regulation DevelopmentalObstetrics and GynecologyOocyte activationEmbryoCell BiologyPolyspermySpermatozoaSpermFetuin-BCell biology030104 developmental biologymedicine.anatomical_structureReproductive MedicineProteolysisMetalloproteasesOocytesFemaleSignal TransductionDevelopmental Biology
researchProduct