Search results for "Disintegrin"

showing 10 items of 30 documents

ADAM10, myelin-associated metalloendopeptidase

2013

Publisher Summary This chapter discusses the structural chemistry and the biological aspects of ADAM10. Originally, ADAM10 was characterized as a myelin-associated metalloproteinase. After cloning the bovine ADAM10 cDNA, the deduced amino acid sequence indicated that the enzyme belonged to the reprolysin subfamily and therefore was named MADM (mammalian disintegrin metalloprotease). The mammalian reprolysin subfamily has been named ADAM (a disintegrin and metalloproteinase) and MADM has been designated ADAM10. The ADAM10 homologs in Drosophila melanogaster and Caenorhabditis elegans are named kuzbanian and sup-17, respectively. The enzymatic activity of isolated ADAM10 can be monitored in v…

MetalloproteinaseSubfamilybiologyChemistryADAM10Cell biologyMyelin basic proteinMyelinmedicine.anatomical_structureBiochemistrymedicinebiology.proteinDisintegrinAmyloid precursor proteinMetalloendopeptidasePeptide sequence
researchProduct

Anti-ADAMTS13 autoantibody profiling in patients with immune-mediated thrombotic thrombocytopenic purpura.

2021

Anti-A Disintegrin and Metalloproteinase with a ThromboSpondin type 1 motif, member 13 (ADAMTS13) autoantibodies cause a severe ADAMTS13 deficiency in immune-mediated thrombotic thrombocytopenic purpura (iTTP). ADAMTS13 consists of a metalloprotease (M), a disintegrin-like (D) domain, 8 thrombospondin type 1 repeats (T1-T8), a cysteine-rich (C), a spacer (S), and 2 CUB domains (CUB1-2). We recently developed a high-throughput epitope mapping assay based on small, nonoverlapping ADAMTS13 fragments (M, DT, CS, T2-T5, T6-T8, CUB1-2). With this assay, we performed a comprehensive epitope mapping using 131 acute-phase samples and for the first time a large group of remission samples (n = 50). Ne…

MetalloproteinaseThrombospondinPurpura Thrombocytopenic IdiopathicbiologyPurpura Thrombotic Thrombocytopenicbusiness.industryThrombotic thrombocytopenic purpuraAutoantibodyHematologymedicine.diseaseADAMTS13Thrombosis and HemostasisCohort StudiesThrombospondin 1Epitope mappingImmune systemImmunologymedicineDisintegrinbiology.proteinHumansbusinessAgedAutoantibodiesBlood advances
researchProduct

Changing fate

2020

Abstract The alpha-secretase A disintegrin and metalloproteinase 10 (ADAM10) and the beta-secretase beta-APP cleaving enzyme 1 (BACE-1) compete in neurons to cleave the amyloid precursor protein (APP). The reaction started by BACE-1, designated the amyloidogenic pathway, leads to formation of neurotoxic amyloid beta peptides (A-betas), while alpha-secretase prevents this and gives rise to an alternative cleavage product (APPs-alpha, nonamyloidogenic pathway). The latter is also known to have neurotrophic and neuroprotective properties. Therefore, identification of mechanisms that lead to a switch in APP processing from the amyloidogenic to the nonamyloidogenic pathway is an attractive avenu…

MetalloproteinasebiologyAmyloid betaTranscription (biology)ChemistryADAM10biology.proteinDisintegrinAmyloid precursor proteinNeuroprotectionNeurotrophinCell biology
researchProduct

Snake venom disintegrins: evolution of structure and function.

2005

Disintegrins represent a family of polypeptides present in the venoms of various vipers that selectively block the function of integrin receptors. Here, we review our current view and hypothesis on the emergence and the structural and functional diversification of disintegrins by accelerated evolution and the selective loss of disulfide bonds of duplicated genes. Research on disintegrins is relevant for understanding the biology of viper venom toxins, but also provides information on new structural determinants involved in integrin recognition that may be useful in basic and clinical research. The role of the composition, conformation, and dynamics of the integrin inhibitory loop acting in …

Models MolecularIntegrinsStereochemistryDisintegrinsIntegrinAmino Acid MotifsMolecular Sequence DataSequence alignmentVenomToxicologyViper VenomsEvolution MolecularStructure-Activity RelationshipProtein structureGenes DuplicateAnimalsAmino Acid SequencePeptide sequencePhylogenybiologyBase SequenceSnakesCell biologyProtein Structure TertiarySnake venombiology.proteinSequence AlignmentFunction (biology)Snake VenomsToxicon : official journal of the International Society on Toxinology
researchProduct

Evolution of Snake Venom Disintegrins by Positive Darwinian Selection

2008

PII-disintegrins, cysteine-rich polypeptides broadly distributed in the venoms of geographically diverse species of vipers and rattlesnakes, antagonize the adhesive functions of beta(1) and beta(3) integrin receptors. PII-disintegrins evolved in Viperidae by neofunctionalization of disintegrin-like domains of duplicated PIII-snake venom hemorrhagic metalloproteinase (SVMP) genes recruited into the venom proteome before the radiation of the advanced snakes. Minimization of the gene (loss of introns and coding regions) and the protein structures (successive loss of disulfide bonds) underpins the postduplication divergence of disintegrins. However, little is known about the underlying genetic …

Models MolecularProtein ConformationDisintegrinsMolecular Sequence DataEvolution MolecularNegative selectionPhylogeneticsMolecular evolutionViperidaeGeneticsDisintegrinAnimalsAmino Acid SequenceSelection GeneticMolecular BiologyGenePhylogenyEcology Evolution Behavior and SystematicsGeneticsEvolution of snake venomBinding SitesbiologyPhylogenetic treeMultigene Familybiology.proteinNeofunctionalizationProtein MultimerizationSnake VenomsMolecular Biology and Evolution
researchProduct

NMR Solution Structure of the Non-RGD Disintegrin Obtustatin

2003

The solution structure of obtustatin, a novel non-RGD disintegrin of 41 residues isolated from Vipera lebetina obtusa venom, and a potent and selective inhibitor of the adhesion of integrin alpha(1)beta(1) to collagen IV, has been determined by two-dimensional nuclear magnetic resonance. Almost the whole set of chemical shifts for 1H, 13C and 15N were assigned at natural abundance from 2D homonuclear and heteronuclear 500 MHz, 600 MHz and 800 MHz spectra at pH 3.0 recorded at 298 K and 303 K. Final structural constraints consisted of 302 non-redundant NOE (95 long-range, 60 medium, 91 sequential and 56 intra-residue), four disulfide bond distances, five chi1 dihedral angles and four hydroge…

Models MolecularProtein ConformationStereochemistryDisintegrinsMolecular Sequence DataStatic ElectricityViper VenomsDihedral angleCrystallography X-RayStructural BiologyDisintegrinAnimalsAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyProtein secondary structureConformational isomerismRGD motifMolecular StructureSequence Homology Amino AcidbiologyHydrogen bondChemistryCircular DichroismChemical shiftHydrogen BondingHydrogen-Ion ConcentrationSolutionsKineticsHeteronuclear moleculebiology.proteinOligopeptidesJournal of Molecular Biology
researchProduct

cDNA Cloning and Functional Expression of Jerdostatin, a Novel RTS-disintegrin from Trimeresurus jerdonii and a Specific Antagonist of the α1β1 Integ…

2005

Jerdostatin represents a novel RTS-containing short disintegrin cloned by reverse transcriptase-PCR from the venom gland mRNA of the Chinese Jerdons pit viper Trimeresurus jerdonii. The jerdostatins precursor cDNA contained a 333-bp open reading frame encoding a signal peptide, a pre-peptide, and a 43-amino acid disintegrin domain, whose amino acid sequence displayed 80% identity with that of the KTS-disintegrins obtustatin and viperistatin. The jerdostatin cDNA structure represents the first complete open reading frame of a short disintegrin and points to the emergence of jerdostatin from a short-coding gene. The different residues between jerdostatin and obtustatin/viperistatin are segreg…

Models MolecularSignal peptideProtein FoldingDNA ComplementaryMagnetic Resonance SpectroscopyProtein ConformationDisintegrinsMolecular Sequence DataIntegrinMutantGene ExpressionPeptide MappingBiochemistryIntegrin alpha1beta1Open Reading FramesExocrine GlandsComplementary DNACrotalid VenomsDisintegrinAnimalsTrimeresurusTrypsinAmino Acid SequenceCysteineDisulfidesCloning MolecularMolecular BiologyPeptide sequenceMessenger RNABase SequencebiologyCell BiologyMolecular biologyRecombinant ProteinsOpen reading frameMutagenesis Site-Directedbiology.proteinJournal of Biological Chemistry
researchProduct

Concerted motions of the integrin-binding loop and the C-terminal tail of the non-RGD disintegrin obtustatin.

2003

Obtustatin is a potent and selective inhibitor of the alpha1beta1 integrin in vitro and of angiogenesis in vivo. It possesses an integrin recognition loop that harbors, in a lateral position, the inhibitory 21KTS23 motif. We report an analysis of the dynamics of the backbone and side-chain atoms of obtustatin by homonuclear NMR methods. Angular mobility has been calculated for 90 assigned cross-peaks from 22 off-resonance rotating frame nuclear Overhauser effect spectroscopy spectra recorded at three magnetic fields. Our results suggest that the integrin binding loop and the C-terminal tail display concerted motions, which can be interpreted by hinge effects. Among the integrin-binding moti…

Models MolecularThreonineIntegrinsMagnetic Resonance SpectroscopyStereochemistryProtein ConformationIntegrinAmino Acid MotifsPlasma protein bindingNuclear Overhauser effectViper VenomsBiochemistryIntegrin alpha1beta1SerineProtein structureDisintegrinSerineThreonineMolecular BiologyIntegrin bindingAlanineModels StatisticalbiologyChemistryHydrogen BondingCell BiologyProtein Structure Tertiarybiology.proteinCollagenPeptidesProtein BindingThe Journal of biological chemistry
researchProduct

Determining a healthy reference range and factors potentially influencing PRO-C3 – A biomarker of liver fibrosis

2021

Background & Aims Progressive fibrosis has been identified as the major predictor of mortality in patients with non-alcoholic fatty liver disease (NAFLD). Several biomarkers are currently being evaluated for their ability to substitute the liver biopsy as the reference standard. Recent clinical studies in NAFLD/NASH patients support the utility of PRO-C3, a marker of type III collagen formation, as a marker for the degree of fibrosis, disease activity, and effect of treatment. Here we establish the healthy reference range, optimal sample handling conditions for both short- and long-term serum storage, and robustness for the PRO-C3 assay. Methods PRO-C3 was measured in 269 healthy volunteers…

NASH-CRN NASH Clinical Research NetworkBiopsyDiseaseAST aspartate aminotransferaseRC799-869Ethnic groupsGastroenterologyNIMBLE Non-Invasive Biomarkers of Metabolic Liver Disease (consortium)FibrosisImmunology and AllergyBody mass indexmedicine.diagnostic_testFatty liverNAS NAFLD Activity ScoreGastroenterologyDiseases of the digestive system. GastroenterologyHospitalsNPV negative predictive valueLiver biopsyBiomarker (medicine)Research Articlemedicine.medical_specialtyNAFLD non-alcoholic fatty liver diseaseADAM A Disintegrin and MetalloproteasesNASH non-alcoholic steatohepatitisReference rangeReference valuesAUROC area under the receiver operating characteristics curveInternal medicineALT alanine aminotransferaseBiopsyInternal MedicinemedicineHumansFIB-4 fibrosis-4Healthy volunteersHepatologyALP alkaline phosphatasebusiness.industryCLSI Clinical and Laboratory Standards InstituteT2DM type 2 diabetes mellitusELF™ test Enhanced Liver Fibrosis testmedicine.diseaseLITMUS Liver Investigation: Testing Marker Utility in Steatohepatitis (consortium)Collagen type IIIFibrosisPPV positive predictive valueReference standardsbusinessBody mass indexBiomarkersNon-alcoholic fatty liver disease
researchProduct

Microvesicles shed by oligodendroglioma cells and rheumatoid synovial fibroblasts contain aggrecanase activity

2012

Membrane microvesicle shedding is an active process and occurs in viable cells with no signs of apoptosis or necrosis. We report here that microvesicles shed by oligodendroglioma cells contain an ‘aggrecanase’ activity, cleaving aggrecan at sites previously identified as targets for adamalysin metalloproteinases with disintegrin and thrombospondin domains (ADAMTSs). Degradation was inhibited by EDTA, the metalloproteinase inhibitor GM6001 and by tissue inhibitor of metalloproteinases (TIMP)-3, but not by TIMP-1 or TIMP-2. This inhibitor profile indicates that the shed microvesicles contain aggrecanolytic ADAMTS(s) or related TIMP-3-sensitive metalloproteinase(s). The oligodendroglioma cells…

OligodendrogliomaMembrane vesicleRA rheumatoid arthritisADAMTSMatrix metalloproteinaseCell Physiological PhenomenaAdamalysin03 medical and health sciences0302 clinical medicineSettore BIO/10 - BiochimicaEndopeptidasesHumansAggrecansADAM adamalysinADAMTS a disintegrin and metalloproteinase with thrombospondin motifsMolecular BiologyMetalloproteinase030304 developmental biologyAggrecanaseTissue Inhibitor of Metalloproteinase-3MEF mouse embryonic fibroblasts0303 health sciencesMetalloproteinaseChemistryBrief ReportMVs microvesiclesADAMTSMicrovesicleCytoplasmic VesiclesDipeptidesFibroblastsMolecular biologyRecombinant ProteinsMicrovesiclesECM extracellular matrixMembrane vesiclesCell biologyEnzyme ActivationMMP matrix metalloproteinaseADAM ProteinsADAMTS4030220 oncology & carcinogenesisProteolysisADAMTS5 ProteinRheumatic FeverTIMP tissue inhibitor of metalloproteinaseAggrecan
researchProduct