Search results for "substrate"

showing 10 items of 1018 documents

Development of Novel Selective Peptidomimetics Containing a Boronic Acid Moiety, Targeting the 20S Proteasome as Anticancer Agents

2014

This paper describes the design, synthesis, and biological evaluation of peptidomimetic boronates as inhibitors of the 20S proteasome, a validated target in the treatment of multiple myeloma. The synthesized compounds showed a good inhibitory profile against the ChT-L activity of 20S proteasome. Compounds bearing a β-alanine residue at the P2 position were the most active, that is, 3-ethylphenylamino and 4-methoxyphenylamino (R)-1-{3-[4-(substituted)-2-oxopyridin-1(2H)-yl]propanamido}-3-methylbutylboronic acids (3 c and 3 d, respectively), and these derivatives showed inhibition constants (Ki ) of 17 and 20 nM, respectively. In addition, they co-inhibited post glutamyl peptide hydrolase act…

Proteasome Endopeptidase ComplexPeptidomimeticStereochemistryCell Survivalanticancer agents; boronates; bortemib; Docking studies; Peptidomimetics; inhibitor; proteasomesAntineoplastic AgentsSaccharomyces cerevisiaedocking studieBiochemistrySubstrate Specificitychemistry.chemical_compoundCell Line TumorDrug DiscoverymedicineMoietyHumansGeneral Pharmacology Toxicology and PharmaceuticsPharmacologychemistry.chemical_classificationBinding SitesproteasomesBortezomibOrganic ChemistrybortezomibboronateBoronic AcidspeptidomimeticProtein Structure Tertiaryanticancer agentMolecular Docking SimulationinhibitorEnzymechemistryProteasomeBiochemistryDocking (molecular)Molecular MedicinePeptidomimeticsGrowth inhibitionDrug Screening Assays AntitumorProteasome InhibitorsBoronic acidmedicine.drug
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Kinetic analysis and molecular modeling of the inhibition mechanism of roneparstat (SST0001) on human heparanase

2016

Heparanase is a β-d-glucuronidase which cleaves heparan sulfate chains in the extracellular matrix and on cellular membranes. A dysregulated heparanase activity is intimately associated with cell invasion, tumor metastasis and angiogenesis, making heparanase an attractive target for the development of anticancer therapies. SST0001 (roneparstat; Sigma-Tau Research Switzerland S.A.) is a non-anticoagulant 100% N-acetylated and glycol-split heparin acting as a potent heparanase inhibitor, currently in phase I in advanced multiple myeloma. Herein, the kinetics of heparanase inhibition by roneparstat is reported. The analysis of dose-inhibition curves confirmed the high potency of roneparstat (I…

Protein Conformation alpha-Helical0301 basic medicineSST0001Molecular modelhomology modelingAmino Acid MotifsPlasma protein bindingMolecular Dynamics SimulationBiochemistryMolecular Docking SimulationheparanaseSubstrate Specificity03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePolysaccharidesHumansProtein Interaction Domains and MotifsHeparanaseHomology modelingEnzyme InhibitorsGlucuronidaseBinding Siteskinetic inhibition analysisHeparinComputational BiologyHeparan sulfateRecombinant ProteinsAcidobacteriaMolecular Docking SimulationEnzyme bindingKinetics030104 developmental biologyCarbohydrate SequenceFondaparinuxchemistryBiochemistryStructural Homology ProteinDocking (molecular)030220 oncology & carcinogenesisBiophysicsroneparstatThermodynamicsProtein Conformation beta-StrandORIGINAL ARTICLESProtein BindingGlycobiology
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Two amino acid residues determine the low substrate affinity of human cationic amino acid transporter-2A.

2003

Mammalian cationic amino acid transporters (CAT) differ in their substrate affinity and sensitivity to trans-stimulation. The apparent Km values for cationic amino acids and the sensitivity to trans-stimulation of CAT-1, -2B, and -3 are characteristic of system y+. In contrast, CAT-2A exhibits a 10-fold lower substrate affinity and is largely independent of substrate at the trans-side of the membrane. CAT-2A and -2B demonstrate such divergent transport properties, even though their amino acid sequences differ only in a stretch of 42 amino acids. Here, we identify two amino acid residues within this 42-amino acid domain of the human CAT-2A protein that are responsible for the apparent low af…

Protein ConformationRecombinant Fusion ProteinsBlotting WesternGreen Fluorescent ProteinsMolecular Sequence DataGene ExpressionArginineTransfectionBiochemistryStructure-Activity RelationshipXenopus laevisExtracellularAnimalsHumansBiotinylationAmino acid transporterAmino Acid SequenceAmino AcidsCationic Amino Acid Transporter 2Molecular BiologyGlutathione Transferasechemistry.chemical_classificationBinding SitesSubstrate (chemistry)Biological TransportCell BiologyPhoto-reactive amino acid analogAmino acidTransmembrane domainLuminescent ProteinsS-tagchemistryBiochemistryMutagenesis Site-DirectedOocytesElectrophoresis Polyacrylamide GelFemaleIntracellularThe Journal of biological chemistry
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The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains.

2007

Abstract Procollagen C-proteinase (PCP) removes the C-terminal pro-peptides of procollagens and also processes other matrix proteins. The major splice form of the PCP is termed BMP1 (bone morphogenetic protein 1). Active BMP1 is composed of an astacin-like protease domain, three CUB (complement, sea urchin Uegf, BMP1) domains and one EGF-like domain. Here we compare the recombinant human full-length BMP1 with its isolated proteolytic domain to further unravel the functional influence of the CUB and EGF domains. We show that the protease domain alone cleaves truncated procollagen VII within the short telopeptide region into fragments of similar size as the full-length enzyme does. However, u…

Protein FoldingCollagen Type VIIDNA Complementarymedicine.medical_treatmentClinical BiochemistryAmino Acid MotifsGene ExpressionGlutamic AcidBiochemistryBone morphogenetic protein 1Mass SpectrometryBone Morphogenetic Protein 1Cell LineSubstrate SpecificityProtein structuremedicineEscherichia coliAnimalsHumansCysteineDisulfidesMolecular BiologyInclusion BodiesMetalloproteinaseProteasebiologyChemistryMetalloendopeptidasesRecombinant ProteinsProtein Structure TertiaryFibronectinProcollagen peptidaseDrosophila melanogasterBiochemistryBone Morphogenetic ProteinsMutationbiology.proteinProtein foldingAstacinBiological chemistry
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Calcium negatively regulates meprin β activity and attenuates substrate cleavage

2015

The meprin β metalloproteinase is an important enzyme in extracellular matrix turnover, inflammation, and neurodegeneration in humans and mice. Previous studies showed a diminished cleavage of certain meprin β substrates in the presence of calcium, although the mechanism was not clear. With the help of a specific fluorogenic peptide assay and the human amyloid precursor protein as substrate, we demonstrated that the influence of calcium is most likely a direct effect on human meprin β itself. Analyzing the crystal structures of pro- and mature meprin β helped to identify a cluster of negatively charged amino acids forming a potential calcium binding site. Mutation of 2 of these residues (D2…

Protein Foldingchemistry.chemical_elementCalciumEndoplasmic ReticulumBiochemistryCell LineSubstrate SpecificityAmyloid beta-Protein PrecursorChlorocebus aethiopsGeneticsAmyloid precursor proteinAnimalsHumansAmino Acid SequenceBinding siteProtein precursorMolecular BiologyCellular localizationSecretory pathwayMetalloproteinaseAmyloid beta-PeptidesBinding SitesbiologyEndoplasmic reticulumMetalloendopeptidasesCell biologyHEK293 CellschemistryCOS CellsMutationMetalloproteasesbiology.proteinCalciumAmyloid Precursor Protein SecretasesSequence AlignmentBiotechnologyThe FASEB Journal
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Inhibition of intrinsic protein tyrosine kinase activity of EGF-receptor kinase complex from human breast cancer cells by the marine sponge metabolit…

1990

1. (+)-Aeroplysinin-1, a naturally occurring tyrosine metabolite from the marine sponge Verongia aerophoba, was found to inhibit the phosphorylation of lipocortin-like proteins by a highly purified preparation of the epidermal growth factor (EGF) receptor-tyrosine protein kinase complex from MCF-7 breast carcinoma cells. 2. (+)-Aeroplysinin-1 blocked the EGF-dependent proliferation of both MCF-7 and ZR-75-1 human breast cancer cells and inhibited the ligand-induced endocytosis of the EGF receptor in vitro. 3. Treatment with aeroplysinin-1 in the concentration range at 0.25-0.5 microM resulted in a time- and dose-dependent total tumor cell death in vitro. 4. At a 10-fold higher concentration…

Protein kinase complexAcetonitrilesTime FactorsPhysiologyBlotting WesternBreast NeoplasmsBiologyBiochemistrySubstrate SpecificityMiceEpidermal growth factorCyclohexenesTumor Cells CulturedAnimalsHumansPhosphorylationTyrosineMolecular BiologyDose-Response Relationship DrugKinaseGeneral MedicineProtein-Tyrosine KinasesMolecular biologyPoriferaErbB ReceptorsBiochemistryCell cultureCancer cellPhosphorylationCalciumTyrosine kinaseCell DivisionComparative Biochemistry and Physiology Part B: Comparative Biochemistry
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Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity

2009

Heat shock protein 27 (HSP27) accumulates in stressed cells and helps them to survive adverse conditions. We have already shown that HSP27 has a function in the ubiquitination process that is modulated by its oligomerization/phosphorylation status. Here, we show that HSP27 is also involved in protein sumoylation, a ubiquitination-related process. HSP27 increases the number of cell proteins modified by small ubiquitin-like modifier (SUMO)-2/3 but this effect shows some selectivity as it neither affects all proteins nor concerns SUMO-1. Moreover, no such alteration in SUMO-2/3 conjugation is achievable by another HSP, such as HSP70. Heat shock factor 1 (HSF1), a transcription factor responsib…

Protein sumoylationTranscriptional ActivationCancer Researchendocrine systemanimal structuresSUMO proteinHSP27 Heat-Shock ProteinsBiologyurologic and male genital diseasesenvironment and public healthSubstrate Specificity03 medical and health sciencesTransactivation0302 clinical medicineHeat Shock Transcription FactorsHeat shock proteinGeneticsAnimalsHumansAnimals Cell Nucleus/metabolism DNA-Binding Proteins/*metabolism HSP27 Heat-Shock Proteins/chemistry/*metabolism Hela Cells Humans Protein Multimerization Protein Structure[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyHSF1Protein Structure QuaternaryMolecular BiologyTranscription factorUbiquitinsHeat-Shock Proteins030304 developmental biologyCell Nucleus0303 health sciencesMolecular biologyHsp70Cell biologyHeat shock factorDNA-Binding ProteinsProtein TransportQuaternary Protein Transport Small Ubiquitin-Related Modifier Proteins/*metabolism Substrate Specificity Transcription Factors/*metabolism Transcriptional Activation Ubiquitins/*metabolism030220 oncology & carcinogenesisembryonic structuresSmall Ubiquitin-Related Modifier ProteinsProtein MultimerizationHeLa CellsMolecular ChaperonesTranscription Factors
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Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 t…

2010

Abstract The metalloproteases meprin α and β are expressed in several tissues, leukocytes, and cancer cells. In skin, meprins are located in separate layers of human epidermis indicating distinct physiological functions, supported by effects on cultured keratinocytes. Meprin β induces a dramatic change in cell morphology and a significant reduction in cell number, whereas in vitro evidence suggests a role for meprin α in basal keratinocyte proliferation. Meprins are secreted as zymogens that are activated by tryptic proteolytical processing. Here, we identify human kallikrein-related peptidases (KLKs) 4, 5, and 8 to be specific activators of meprins. KLK5 is capable of activating both metal…

Proteolysismedicine.medical_treatmentClinical BiochemistryBiologyBiochemistrySubstrate SpecificitymedicineHumansAmino Acid SequenceProtein precursorMolecular BiologySkinSerine proteaseEnzyme PrecursorsMetalloproteinaseProteasemedicine.diagnostic_testMetalloendopeptidasesKLK5Trypsinddc:Enzyme Activationmedicine.anatomical_structureBiochemistrybiology.proteinKallikreinsKeratinocytemedicine.drug
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Identification of Rothia Bacteria as Gluten-Degrading Natural Colonizers of the Upper Gastro-Intestinal Tract

2011

Background Gluten proteins, prominent constituents of barley, wheat and rye, cause celiac disease in genetically predisposed subjects. Gluten is notoriously difficult to digest by mammalian proteolytic enzymes and the protease-resistant domains contain multiple immunogenic epitopes. The aim of this study was to identify novel sources of gluten-digesting microbial enzymes from the upper gastro-intestinal tract with the potential to neutralize gluten epitopes. Methodology/Principal Findings Oral microorganisms with gluten-degrading capacity were obtained by a selective plating strategy using gluten agar. Microbial speciations were carried out by 16S rDNA gene sequencing. Enzyme activities wer…

ProteomicsApplied Microbiologylcsh:MedicineBiochemistryGliadinEpitopeSubstrate SpecificityUpper Gastrointestinal Tractlcsh:ScienceBifidobacterium2. Zero hungerchemistry.chemical_classification0303 health sciencesAniline CompoundsMultidisciplinarymedicine.diagnostic_testbiologyHydrolysisProteolytic enzymesfood and beveragesHydrogen-Ion ConcentrationEnzymes3. Good healthSolutionsBiochemistryMedical MicrobiologyMedicineSmall IntestineResearch ArticleProteasesGlutensProteolysisMolecular Sequence DataDental PlaqueGastroenterology and HepatologyMicrobiologydigestive systemMicrobiology03 medical and health sciencesAntigenmedicineHumansAmino Acid SequenceSalivaBiology030304 developmental biologyBinding Sites030306 microbiologylcsh:Rnutritional and metabolic diseasesbiology.organism_classificationGlutenPeptide Fragmentsdigestive system diseasesMolecular WeightCeliac DiseasechemistryProteolysisbiology.proteinlcsh:QGliadinMicrococcaceaePLoS ONE
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Breast cancer cells exhibit selective modulation induced by different collagen substrates.

2008

During the invasive phase of malignant tumors, neoplastic cells break into the basal lamina and enter in contact with the underlying connective tissue, which concurrently undergoes extensive modifications. The aim of our present minireview is to focus the changes in the collagenous matrix occurring during breast cancer progression and to explore the possible effects of different collagen substrates on breast cancer cell behavior and proteomic modulation.

ProteomicsPathologymedicine.medical_specialtyConnective tissueBreast NeoplasmsMatrix (biology)ProteomicsBiochemistryBreast cancerRheumatologymedicineAnimalsHumansOrthopedics and Sports MedicineNeoplasm InvasivenessNeoplasm MetastasisSettore BIO/06 - Anatomia Comparata E Citologiaskin and connective tissue diseasesCollagen substrateMolecular BiologyCollagen Substrate Breast Cancer ProteomicsChemistryCell Biologymedicine.diseaseExtracellular MatrixSelective modulationSettore BIO/18 - Geneticamedicine.anatomical_structureCancer researchBasal laminaBreast cancer cellsCollagenStromal Cells
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