Search results for "Substrate specificity"

showing 10 items of 217 documents

Low Density Lipoprotein Receptor-related Protein (LRP) Interacts with Presenilin 1 and Is a Competitive Substrate of the Amyloid Precursor Protein (A…

2005

Presenilin 1 (PS1) is a critical component of the gamma-secretase complex, which is involved in the cleavage of several substrates including the amyloid precursor protein (APP) and the Notch receptor. Recently, the low density receptor-related protein (LRP) has been shown to be cleaved by a gamma-secretase-like activity. We postulated that LRP may interact with PS1 and tested its role as a competitive substrate for gamma-secretase. In this report we show that LRP colocalizes and interacts with endogenous PS1 using coimmunoprecipitation and fluorescence lifetime imaging microscopy. In addition, we found that gamma-secretase active site inhibitors do not disrupt the interaction between LRP an…

ImmunoprecipitationNotch signaling pathwayMice TransgenicBinding CompetitiveBiochemistryPresenilinCell LineSubstrate SpecificityRats Sprague-DawleyAmyloid beta-Protein PrecursorMiceEndopeptidasesmental disordersPresenilin-1Amyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansBinding siteMolecular BiologyBrain ChemistryBinding SitesbiologyChemistryMembrane ProteinsCell BiologyRatsnervous system diseasesCell biologyTransmembrane domainBiochemistryMultiprotein ComplexesLDL receptorbiology.proteinlipids (amino acids peptides and proteins)Amyloid Precursor Protein SecretasesAmyloid precursor protein secretaseLow Density Lipoprotein Receptor-Related Protein-1Journal of Biological Chemistry
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A novel galactose- and arabinose-specific lectin from the sponge Pellina semitubulosa: isolation, characterization and immunobiological properties.

1992

A new lectin from the sponge Pellina semitubulosa is derived which was extracted and purified to homogeneity. The purified lectin is probably a hexamer of polypeptide chains (each M(r) 34,000) which are covalently linked via disulfide linkages; the isoelectric point is 6.1. The lectin displays the following specificities: D-galactose (50% inhibition of hemagglutination at 0.2 mM) = L-arabinose (0.2 mM) greater than D-fucose (1.5 mM) greater than D-glucose (3.0 mM). It precipitates human erythrocytes (A1, A2, A1B, B, and O) with a titer between 2(8) and 2(11) and erythrocytes from sheep and rabbits with a titer between 2(5) and 2(10). The Pellina lectin displays a strong mitogenic effect on …

Interleukin 2HemagglutinationChemical PhenomenaLymphocyte ActivationBiochemistrySubstrate Specificitychemistry.chemical_compoundLectinsmedicineAnimalsLymphocytesAmino AcidsbiologyChemistry PhysicalMacrophagesInterleukinLectinGalactoseGeneral MedicineHemagglutination TestsMolecular biologyArabinosePoriferaTiterIsoelectric pointchemistryBiochemistryConcanavalin AGalactosebiology.proteinInterleukin-2medicine.drugInterleukin-1Biochimie
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Role of Neutral Amino Acid Transport and Protein Breakdown for Substrate Supply of Nitric Oxide Synthase in Human Endothelial Cells

2003

Endothelial dysfunction is often associated with a relative substrate deficiency of the endothelial nitric oxide synthase (eNOS) in spite of apparently high intracellular arginine concentrations. For a better understanding of the underlying pathophysiological mechanisms, we aimed to characterize the intracellular arginine sources of eNOS. Our previous studies in human endothelial EA.hy926 cells suggested the existence of two arginine pools: pool I can be depleted by extracellular lysine, whereas pool II is not freely exchangeable with the extracellular space, but accessible to eNOS. In this study, we demonstrate that the eNOS accessible pool II is also present in human umbilical vein endoth…

Intracellular FluidUmbilical VeinsNitric Oxide Synthase Type IIIArginineEndotheliumPhysiologyGlutamineArginineTransfectionSubstrate Specificitychemistry.chemical_compoundEnosNeutral amino acid transportCitrullinemedicineAnimalsHumansAmino AcidsCells CulturedbiologyCarcinomaMembrane Transport ProteinsProteinsNitric Oxide Synthase Type IIIBiological Transportbiology.organism_classificationRatsEndothelial stem cellNitric oxide synthaseAmino Acid Transport Systems NeutralAmino Acids Neutralmedicine.anatomical_structureUrinary Bladder NeoplasmsBiochemistrychemistrybiology.proteinCitrullineEndothelium VascularNitric Oxide SynthaseCardiology and Cardiovascular MedicineCirculation Research
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Proteomic Analyses Reveal an Acidic Prime Side Specificity for the Astacin Metalloprotease Family Reflected by Physiological Substrates

2011

Astacins are secreted and membrane-bound metalloproteases with clear associations to many important pathological and physiological processes. Yet with only a few substrates described their biological roles are enigmatic. Moreover, the lack of knowledge of astacin cleavage site specificities hampers assay and drug development. Using PICS (proteomic identification of protease cleavage site specificity) and TAILS (terminal amine isotopic labeling of substrates) degradomics approaches >3000 cleavage sites were proteomically identified for five different astacins. Such broad coverage enables family-wide determination of specificities N- and C-terminal to the scissile peptide bond. Remarkably, me…

KeratinocytesModels MolecularProteomicsVascular Endothelial Growth Factor AProteasesmedicine.medical_treatmentProteolysisMolecular Sequence DataBiologyCleavage (embryo)BiochemistryCell LineSubstrate SpecificityAnalytical Chemistry03 medical and health sciencesTandem Mass SpectrometrymedicineHumansAmino Acid SequenceMolecular BiologyPeptide sequencePhylogeny030304 developmental biologyEnzyme Precursors0303 health sciencesProteaseStaining and LabelingEdman degradationmedicine.diagnostic_testResearch030302 biochemistry & molecular biologyTioproninMetalloendopeptidasesTerminal amine isotopic labeling of substratesRecombinant ProteinsKineticsBiochemistryProteolysisKallikreinsAstacinPeptidesSequence AlignmentChromatography LiquidMolecular & Cellular Proteomics
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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
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Enantioselective addition of nitromethane to α-keto esters catalyzed by copper(ii)–iminopyridine complexes

2008

The copper complex of a chiral iminopyridine easily prepared from (R)-(-)-fenchone and picolylamine catalyzes the enantioselective Henry (nitroaldol) reaction between nitromethane and alpha-keto esters. Good yields and modest to good enantioselectivities are obtained for a wide range of alpha-keto esters, bearing aromatic, alkyl or alkenyl groups attached to the ketone carbonyl group.

KetonePyridineschemistry.chemical_elementLigandsBiochemistryMedicinal chemistryCatalysisNitroparaffinsSubstrate SpecificityCatalysischemistry.chemical_compoundOrganic chemistryPhysical and Theoretical ChemistryAlkylchemistry.chemical_classificationCopper complexNitromethaneChemistryOrganic ChemistryEnantioselective synthesisEstersStereoisomerismCopperCarbonyl grouplipids (amino acids peptides and proteins)MethaneCopperOrg. Biomol. Chem.
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Monohydroxylated fatty acid substrate specificity of human leukocyte 5-lipoxygenase and ω-hydroxylase

1988

Various monohydroxylated fatty acids were synthesized from eicosapolyenoic acids, namely arachidonic (20:4 omega-6), timnodonic (20:5 omega-3), dihomogammalinolenic (20:3 omega-6) and mead (20:3 omega-9) acids. 12-Hydroxy derivatives, as well as 12-hydroxy-5,8,10-heptadecatrienoic acid (HHT), were produced with platelets as the enzyme source, and 15-hydroxy derivatives were produced by soya bean lipoxygenase treatment. Each monohydroxylated fatty acid was incubated with human leukocytes in the presence or absence of the calcium ionophore A23187, and dihydroxylated products were analysed by h.p.l.c. 12-Hydroxy derivatives of 20:4 omega-6, 20:5 omega-3 and 20:3 omega-9 were similarly oxygenat…

Leukotriene B4StereochemistryHydroxylationArachidonate LipoxygenasesBiochemistryMixed Function OxygenasesSubstrate SpecificityHydroxylationchemistry.chemical_compoundLipoxygenaseCytochrome P-450 Enzyme SystemHydroxyeicosatetraenoic AcidsLeukocytesHumansMolecular Biologychemistry.chemical_classificationArachidonate 5-LipoxygenasebiologyFatty AcidsFatty acidSubstrate (chemistry)Cell BiologyEnzymechemistryBiochemistryArachidonate 5-lipoxygenasebiology.proteinCytochrome P-450 CYP4AResearch ArticlePolyunsaturated fatty acidBiochemical Journal
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Calcium-Dependent Assembly of Centrin-G-Protein Complex in Photoreceptor Cells

2002

Photoexcitation of rhodopsin activates a heterotrimeric G-protein cascade leading to cyclic GMP hydrolysis in vertebrate photoreceptors. Light-induced exchanges of the visual G-protein transducin between the outer and inner segment of rod photoreceptors occur through the narrow connecting cilium. Here we demonstrate that transducin colocalizes with the Ca(2+)-binding protein centrin 1 in a specific domain of this cilium. Coimmunoprecipitation, centrifugation, centrin overlay, size exclusion chromatography, and kinetic light-scattering experiments indicate that Ca(2+)-activated centrin 1 binds with high affinity and specificity to transducin. The assembly of centrin-G-protein complex is medi…

Lightgenetic structuresChromosomal Proteins Non-HistoneMacromolecular SubstancesImmunoprecipitationG proteinCentrifugationPlasma protein bindingBiologyRetinaSubstrate SpecificityRats Sprague-DawleyMiceHeterotrimeric G proteinCalcium-binding proteinAnimalsScattering RadiationTransducinMicroscopy ImmunoelectronCell Growth and DevelopmentMolecular BiologyCalcium-Binding ProteinsCell BiologyHeterotrimeric GTP-Binding ProteinsPrecipitin TestsRatsCell biologyMice Inbred C57BLMolecular WeightRhodopsinCentrinChromatography Gelbiology.proteinCalciumCattlesense organsTransducinPhotoreceptor Cells VertebrateProtein BindingSignal TransductionMolecular and Cellular Biology
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Potential biological role of laccase from the sponge Suberites domuncula as an antibacterial defense component

2014

Abstract Background Laccases are copper-containing enzymes that catalyze the oxidation of a wide variety of phenolic substrates. Methods We describe the first poriferan laccase from the marine demosponge Suberites domuncula. Results This enzyme comprises three characteristic multicopper oxidase homologous domains. Immunohistological studies revealed that the highest expression of the laccase is in the surface zone of the animals. The expression level of the laccase gene is strongly upregulated after exposure of the animals to the bacterial endotoxin lipopolysaccharide. To allow the binding of the recombinant enzyme to ferromagnetic nanoparticles, a recombinant laccase was prepared which con…

LipopolysaccharidesMolecular Sequence DataBiophysicsMulticopper oxidaseFerric CompoundsLigninBiochemistryMichaelis–Menten kineticsGene Expression Regulation EnzymologicSubstrate Specificitychemistry.chemical_compoundEscherichia coliAnimalsLigninAmino Acid SequenceMolecular BiologyPhylogenyLaccasechemistry.chemical_classificationDose-Response Relationship DrugSequence Homology Amino AcidbiologyReverse Transcriptase Polymerase Chain ReactionChemistryLaccaseHydrazonesSubstrate (chemistry)biology.organism_classificationRecombinant ProteinsAnti-Bacterial AgentsUp-RegulationSuberites domunculaKineticsEnzymeBiochemistryBiocatalysisNanoparticlesSuberitesOxidation-ReductionIron oxide nanoparticlesBiochimica et Biophysica Acta (BBA) - General Subjects
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The synthesis of SNAT2 transporters is required for the hypertonic stimulation of system A transport activity

2004

AbstractIn cultured human fibroblasts incubated under hypertonic conditions, the stimulation of system A for neutral amino acid transport, associated to the increased expression of the mRNA for SNAT2 transporter, leads to an expanded intracellular amino acid pool and to the recovery of cell volume. A protein of nearly 60 kDa, recognized by an antiserum against SNAT2, is increased both in the pool of biotinylated membrane proteins and in the total cell lysate of hypertonically stressed cells. The increased level of SNAT2 transporters in hypertonically stressed cells is confirmed by immunocytochemistry. DRB, an inhibitor of transcription, substantially inhibits the increase of SNAT2 proteins …

LysisAmino Acid Transport System AProlineTranscription GeneticGlutamineBlotting WesternHypertonic SolutionsBiophysicsStimulationBiologyHuman fibroblastBiochemistrySubstrate SpecificityAmino acid starvationHypertonic stressCell volumeNeutral amino acid transportHumansBiotinylationRNA MessengerCells CulturedCell Sizechemistry.chemical_classificationRadioisotopesCell MembraneBiological TransportPhosphorusCell BiologyFibroblastsImmunohistochemistryAmino acidGlutamineMolecular WeightKineticschemistryBiochemistryMembrane proteinHypertonic StressIntracellularDichlororibofuranosylbenzimidazoleBiochimica et Biophysica Acta (BBA) - Biomembranes
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