Search results for "rypsi"

showing 10 items of 240 documents

Complement and Atherogenesis

1999

Abstract —Complement activation occurs in temporal correlation with the subendothelial deposition of LDL during early atherogenesis, and complement also plays a pathogenetic role in promoting lesion progression. Two lesion components have been identified that may be responsible for complement activation. First, enzymatic degradation of LDL generates a derivative that can spontaneously activate complement, and enzymatically degraded LDL (E-LDL) has been detected in the lesions. Second, C-reactive protein (CRP) colocalizes with complement C5b-9, as evidenced by immunohistological studies of early atherosclerotic lesions, so the possibility exists that this acute phase protein also fulfills a…

PhosphorylcholineNeuraminidaseComplement Membrane Attack ComplexCoronary Artery DiseaseBiologyPhospholipaseLesionPathogenesismedicineHumansElectrophoresis Gel Two-DimensionalTrypsinComplement Activationchemistry.chemical_classificationPhosphorylcholineC-reactive proteinAcute-phase proteinCholesterol LDLComplement C3Coronary VesselsMolecular biologyComplement systemC-Reactive ProteinEnzymeBiochemistrychemistryType C Phospholipasesbiology.proteinCalciummedicine.symptomCardiology and Cardiovascular MedicineProtein BindingArteriosclerosis, Thrombosis, and Vascular Biology
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Possible protective role for C-reactive protein in atherogenesis: complement activation by modified lipoproteins halts before detrimental terminal se…

2004

Background—Previous work indicated that enzymatically remodeled LDL (E-LDL) might activate complement in atherosclerotic lesions via a C-reactive protein (CRP)–dependent and CRP-independent pathway. We sought to substantiate this contention and determine whether both pathways drive the sequence to completion.Methods and Results—E-LDL was prepared by sequential treatment of LDL with a protease and cholesteryl esterase. Trypsin, proteinase K, cathepsin H, or plasmin was used with similar results. Functional tests were used to assess total complement hemolytic activity, and immunoassays were used to demonstrate C3 cleavage and to quantify C3a, C4a, C5a, and C5b-9. E-LDL preparations activated …

PlasminArteriosclerosisLipoproteinsCathepsin HPhysiology (medical)EndopeptidasesmedicineHumansComplement ActivationbiologyC-reactive proteinC4ADrug SynergismComplement System ProteinsSterol EsteraseProteinase KTrypsinImmunohistochemistryComplement systemLipoproteins LDLC-Reactive ProteinBiochemistrybiology.proteinCardiology and Cardiovascular MedicineLipoproteinmedicine.drugCirculation
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Activation of the first component of complement, C1: comparison of the effect of sixteen different enzymes on serum C1.

1983

In this study, the effect of sixteen different enzymes on serum C1 and its subcomponents was investigated. The sixteen enzymes could be divided into three groups. First, enzymes which activate native C1: trypsin (optimal concentration 2.4 x 10(-4) mM); alpha-chymotrypsin (2.3 x 10(3) mM); thrombin (1.0 x 10(-5) mM); plasmin (1.9 x 10(-5) mM); elastase (5.8 x 10(-5) mM); pronase (3.0 x 10(-6) mM). All these enzymes are serine esterase and activate native serum C1 bound to EAC4 at the given concentration within 10 min at 30 degrees C. Furthermore, native C1 inhibited by a pentosanpolysulfoester, Sp54, is unable to undergo the internal activation but can be externally activated by the serine e…

PlasminComplement Activating EnzymesImmunologyGuinea PigsDose-Response Relationship ImmunologicPronaseSerinechemistry.chemical_compoundComplement C1medicineImmunology and AllergyAnimalsHumansTrypsinFibrinolysinComplement Activationchemistry.chemical_classificationPentosan Sulfuric PolyesterbiologyHematologyTrypsinCarboxypeptidaseKineticsEnzymeBiochemistrychemistrybiology.proteinCollagenaseCattleRabbitsLysozymemedicine.drugPeptide HydrolasesImmunobiology
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α-Chymotrypsin-Catalyzed Reaction Confined in Block-Copolymer Vesicles

2010

Herein the reactivity of the enzyme α-chymotrypsin in the confinement of polystyrene-block-poly(acrylic acid) (PS-b-PAA) vesicles was investigated. Enzyme and substrate molecules were encapsulated in PS-b-PAA vesicles with internal diameters ranging from 26 nm to 165 nm during the formation of the vesicles. While the loading efficiencies of enzyme and substrate molecules were practically identical for vesicles of identical size, they were found to increase with decreasing vesicle size. The kinetics of the α-chymotrypsin catalyzed hydrolysis of N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin (AMC) was evaluated following the increase of the absorption of the product 7-amino-4-methylcoumarin …

PolymersKineticsAcrylic ResinsPhotochemistryMETIS-269964Ultraviolet visible spectroscopyCoumarinsChymotrypsinNanotechnologyOrganic chemistryReactivity (chemistry)Physical and Theoretical ChemistryChymotrypsinbiologyChemistryHydrolysisVesicleSubstrate (chemistry)Atomic and Molecular Physics and OpticsTurnover numberKineticsBiocatalysisbiology.proteinPolystyrenesSpectrophotometry UltravioletAbsorption (chemistry)ChemPhysChem
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Apoptotic Cell Debris and Phosphatidylserine-Containing Lipid Vesicles Induce Apolipoprotein J (Clusterin) Gene Expression in Vital Fibroblasts

2001

The molecular events in cells undergoing programmed cell death (apoptosis) are well studied; however, the response of the surviving neighbor cells to local cell death is largely uncharacterized. Apolipoprotein J (clusterin) is an 80-kDa glycoprotein that has been implied in cytoprotection of the vital cells, presumably by assisting in the clearance of apoptotic vesicles and membrane remnants. Its mRNA is specifically up-regulated in the vital cells of apoptotic tissues. The molecular mechanisms, however, leading to this response are not known. We here show that exposure of vital fibroblasts to apoptotic vesicles, disrupted vital cells, and trypsin-treated membrane remnants induces apoJ mRNA…

Programmed cell deathEndocytic cycleGene ExpressionApoptosisPhosphatidylserinesCell Linechemistry.chemical_compoundCricetinaeAnimalsTrypsinGlycoproteinsClusterinbiologyVesicleCell BiologyPhosphatidylserinePhosphatidic acidFibroblastsLipid MetabolismMolecular biologyCytoprotectionRatsCell biologyClusterinchemistryApoptosisbiology.proteinMolecular ChaperonesExperimental Cell Research
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Role of toxin activation on binding and pore formation activity of the Bacillus thuringiensis Cry3 toxins in membranes of Leptinotarsa decemlineata (…

2004

AbstractBinding and pore formation constitute key steps in the mode of action of Bacillus thuringiensis δ-endotoxins.In this work, we present a comparative analysis of toxin-binding capacities of proteolytically processed Cry3A, Cry3B and Cry3C toxins to brush border membranes (BBMV) of the Colorado potato beetle Leptinotarsa decemlineata (CPB), a major potato coleopteran-insect pest. Competition experiments showed that the three Cry3 proteolytically activated toxins share a common binding site. Also heterologous competition experiments showed that Cry3Aa and Cry3Ca toxins have an extra binding site that is not shared with Cry3Ba toxin. The pore formation activity of the three different Cry…

ProteasesBrush borderBacterial ToxinsBacillus thuringiensisBiophysicsmedicine.disease_causeBinding CompetitiveBiochemistryHemolysin ProteinsBacterial ProteinsBacillus thuringiensisEndopeptidasesmedicineAnimalsProtoxin activationBinding siteProtein PrecursorsChymotrypsinBinding SitesbiologyBacillus thuringiensis ToxinsMicrovilliToxinColorado potato beetleCell MembranefungiCell Biologybiology.organism_classificationTrypsinColeopteraEndotoxinsBiochemistryMode of actionbiology.proteinmedicine.drugBiochimica et Biophysica Acta (BBA) - Biomembranes
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Proteolytic Processing ofBacillus thuringiensisCryIIIA Toxin and Specific Binding to Brush-Border Membrane Vesicles ofLeptinotarsa decemlineata(Color…

1996

Abstract The mode of action of Bacillus thuringiensis insecticidal proteins in lepidopteran insects is known to involve five steps: ingestion, solubilization, protease activation, binding to midgut membrane receptors, and disruption of the intestinal membrane. Two of these steps, protease activation and binding to midgut membrane receptors, have been analyzed in the major potato pest, the coleoptera Leptinotarsa decemlineata (Colorado potato beetle). Unlike recently proposed, after treatment of the coleopteran-specific B. thuringiensis toxin CryIIIA with gut content from the Colorado potato beetle, a 42-kDa processing polypeptide has been identified. The study of binding to midgut membrane …

ProteasesChymotrypsinProteasebiologyHealth Toxicology and Mutagenesismedicine.medical_treatmentfungiColorado potato beetleBiological pest controlfood and beveragesMidgutGeneral Medicinebiology.organism_classificationBiochemistryBacillus thuringiensisbiology.proteinmedicineBinding siteAgronomy and Crop SciencePesticide Biochemistry and Physiology
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Metalloprotease meprin β is activated by transmembrane serine protease matriptase-2 at the cell surface thereby enhancing APP shedding.

2014

Increased expression of metalloprotease meprin β is associated with fibrotic syndromes and Alzheimer's disease (AD). Hence, regulation of meprin activity might be a suitable strategy for the treatment of these conditions. Meprin β is a type 1 transmembrane protein, but can be released from the cell surface by ectodomain shedding. The protease is expressed as an inactive zymogen and requires proteolytic maturation by tryptic serine proteases. In the present study, we demonstrate, for the first time, the differences in the activation of soluble and membrane bound meprin β and suggest transmembrane serine protease 6 [TMPRSS6 or matriptase-2 (MT2)] as a new potent activator, cleaving off the pr…

ProteasesTMPRSS6Swinemedicine.medical_treatmentMolecular Sequence DataBiologyBiochemistryProtein Structure SecondaryAmyloid beta-Protein PrecursorChlorocebus aethiopsmedicineAnimalsHumansAmino Acid SequenceMolecular BiologySerine proteaseProteaseCell MembraneSerine EndopeptidasesMetalloendopeptidasesCell BiologySheddaseTrypsinTransmembrane proteinHEK293 CellsBiochemistryEctodomainCOS Cellsbiology.proteinmedicine.drugThe Biochemical journal
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Potent Inhibitor of Human Trypsins from the Aeruginosin Family of Natural Products

2021

Funding Information: We would like to thank A. Löfhjelm and L. Saari for excellent technical assistance. This work was supported by a Sigrid Jusélius Foundation grant to H.K. and the Academy of Finland funding (321809) to T.S. We would also like to thank the Erkko Foundation and Nordforsk Nordic center of Excellency NordAqua (project number #82845) and University of Helsinki’s Doctoral Programme in Microbiology and Biotechnology funding to M.N.A. D.O.A. was supported by a postdoctoral research fellowship from the São Paulo Research Foundation (FAPESP #2018/01563-2). We thank Biocenter Kuopio for the use of their facilities for molecular modeling and MD simulations. We thank the DNA Sequenci…

Proteasesserine proteases116 Chemical sciencesproteaasiluonnontuotteet01 natural sciencesBiochemistryGenomeproteomiikkaSerine03 medical and health sciencesCell Line TumorGene clusterinhibitorsHumansIC50Genetrypsiinit030304 developmental biologyCell ProliferationinhibiittoritSerine protease0303 health sciencesBiological Productsbiologybiokemia010405 organic chemistryCell growthChemistrybioinformatiikkaGeneral MedicineArticlesseriiniproteaasi0104 chemical sciences3. Good healthsyöpäsolutBiochemistryGenes Bacterialbiology.proteinMolecular MedicineproteasessyöpätauditproteiinitTrypsin InhibitorsAzabicyclo CompoundsNodulariaAeruginosins
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Optimization of peptidomimetic boronates bearing a P3 bicyclic scaffold as proteasome inhibitors

2014

Abstract A new series of pseudopeptide boronate proteasome inhibitors (2–3) was developed, through optimization of our previously described analogs of bortezomib, bearing a bicyclic 1,6-naphthyridin-5(6H)-one scaffold as P3 fragment (1). The biological evaluation on human 20S proteasome displayed a promising inhibition profile, especially for compounds bearing a P2 ethylene fragment, which exhibited Ki values in the nanomolar range for the ChT-L activity (e.g. 2a, Ki = 0.057 μM) and considerable selectivity for proteasome over bovine pancreatic α-chymotrypsin. Docking experiments into the yeast 20S proteasome revealed that the ligands are accommodated predominantly into the ChT-L site and t…

Proteasome Endopeptidase ComplexProtein ConformationStereochemistryPeptidomimeticAntineoplastic AgentsPeptidomimetic boronatePeptidomimetic boronates; Docing studies; Proteasome inhibitorsBortezomibchemistry.chemical_compoundCell Line TumorEndopeptidasesDrug DiscoverymedicineAnimalsHumansProteasome inhibitoranticancer drugTrypsinThreonineCell ProliferationPharmacologybiologyBicyclic moleculeBortezomibHydrolysisOrganic ChemistryActive siteGeneral MedicineBoronic AcidsCombinatorial chemistryMolecular Docking SimulationchemistryProteasomeDocking (molecular)Docking studieCaspasesDrug DesignPyrazinesProteolysisbiology.proteinCattlePeptidomimeticsProteasome InhibitorsLead compoundmedicine.drugEuropean Journal of Medicinal Chemistry
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