Search results for "Proteinase"

showing 10 items of 407 documents

Specialized Movement on the Rowing Ergometer and Post-workout Changes in Selected Peripheral Blood Parameters - a Case Report.

2018

Rowing is a sport discipline, which requires extreme physical strength and endurance and appropriate aerobic and anaerobic capacity as well. However, when the workout intensity and load is very high, exercise is associated with temporary changes in cellular metabolism and the immune system. The study included one male rower aged 28 years - the highly-skilled and experienced athlete. We determined basic cardiorespiratory fitness measures, complete blood count, and 24 clinical chemistry parameters including relevant biochemical and haematological parameters and matrix metaloproteinases activities. Maximal exercise on the rowing ergometer induced 2-fold increase in absolute counts of all leuko…

PhysiologyRowingPhysiologyPhysical Therapy Sports Therapy and RehabilitationPhysical exercisePhysical strengthlcsh:Physiologychemistry.chemical_compoundhaematological markerslcsh:GV557-1198.995biochemical markersmedicineOrthopedics and Sports Medicinelcsh:Sports medicinelcsh:SportsCreatininerowingmedicine.diagnostic_testlcsh:QP1-981Complete blood countmatrix metalloproteinasesCardiorespiratory fitnessPeripheral bloodchemistryTourism Leisure and Hospitality ManagementMaximal exerciselcsh:RC1200-1245Central European Journal of Sport Sciences and Medicine
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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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SPIONs embedded in polyamino acid nanogels to synergistically treat tumor microenvironment and breast cancer cells.

2018

Abstract The extremely complex tumor microenvironment (TME) in humans is the major responsible for the therapeutic failure in cancer nanomedicine. A new concept of disease-driven nanomedicine, henceforth named “Theranomics”, which attempts to target cancer cells and TME on the whole, represents an attractive alternative. Herein, a nanomedicine able to co-deliver doxorubicin and a tumor suppressive proteolytic protein such as collagenase-2 was developed. We successfully obtained superparamagnetic nanogels (SPIONs/Doco@Col) via the intermolecular azide-alkyne Huisgen cycloaddition. We demonstrated that a local ECM degradation and remodeling in solid tumors by means of collagenase-2 could enha…

Polyamino acidPolyamino acidsCollagenasePharmaceutical ScienceBreast Neoplasms02 engineering and technology030226 pharmacology & pharmacy03 medical and health sciences0302 clinical medicineBreast cancerBreast cancerDrug Delivery SystemsCell Line TumormedicineTumor MicroenvironmentHumansDoxorubicinTargeted cancer therapyAmino AcidsMagnetite NanoparticlesTumor microenvironmentAntibiotics AntineoplasticChemistrySPIONCancerTheranomicDrug Synergism021001 nanoscience & nanotechnologymedicine.diseasenanomedicineNanomedicinesDrug LiberationSPIONsMatrix Metalloproteinase 8DoxorubicinCancer cellCancer researchNanomedicineTheranomicsFemaleBreast cancer cellspolyamino acid0210 nano-technologyGelsmedicine.drugInternational journal of pharmaceutics
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Oral plus vaginal alpha-lipoic acid in women at risk for preterm delivery

2018

Objective: The etiology of preterm labor is multifactorial. An inflammatory response is always involved with the activation of NF-kB that determines synthesis and release of inflammatory molecules, implicated in fetal membrane activation, cervical modifications, abdominal pain and spontaneous uterine contractions. There is a close relationship between preterm birth and cervical shortening in the second quarter of pregnancy. We evaluated the benefits of alpha-lipoic acid administration on women considered at risk of preterm delivery due to the presence of symptoms (pelvic pain and uterine contractions) or reduced cervical length. Patients and Methods: This prospective observational study was…

Preterm labor Cervicometry length Trans-vaginal ultrasound NF-kB Interleukin-1 Matrix metalloproteinases Prostaglandin E2.Settore MED/40 - Ginecologia E Ostetricia
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Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

2009

Abstract Both the cellular prion protein (PrPc) and the amyloid precursor protein (APP) are physiologically subjected to complex proteolytic processing events. While for APP the proteinases involved – alpha-, beta- and gamma-secretase – have been identified in vitro and in vivo, the cleavage of PrPc by now has been linked only to the shedding activity of the metalloproteinase ADAM10 and/or ADAM17 in cell culture. Here we show that neuronal overexpression of the alpha-secretase ADAM10 in mice reduces all PrPc species detected in the brain instead of leading to enhanced amounts of specific cleavage products of PrPc. Additionally, the incubation time of mice after scrapie infection is signific…

Prionsanimal diseasesADAM10Molecular Sequence DataPrion diseaseScrapieMice Transgeniclcsh:RC321-571ADAM10 ProteinMiceIn vivomental disordersNeurotoxicitymedicineAmyloid precursor proteinAnimalsHumansGliosisAmino Acid Sequencealpha-Secretaselcsh:Neurosciences. Biological psychiatry. NeuropsychiatrySheddingMetalloproteinasebiologyChemistryBrainMembrane ProteinsMolecular biologyIn vitronervous system diseasesMice Inbred C57BLADAM ProteinsNeurologyAlpha secretaseGliosisbiology.proteinCattlemedicine.symptomAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalScrapieNeurobiology of disease
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Caspase-dependent apoptosis during infection with Cryptosporidium parvum

1999

The protozoan parasite Cryptosporidium parvum causes persistent diarrhea and malnutrition in children and the diarrhea-wasting syndrome in AIDS. No therapy exists for eliminating the parasite in the absence of a healthy immune response. Although it had been reported that infection of intestinal cell lines with C. parvum leads to host cell death, the mechanisms of cytolysis have not been characterized. We show here that infection with C. parvum leads to typical apoptotic nuclear condensation and DNA fragmentation in host cells. Both nuclear condensation and DNA fragmentation are inhibited by a caspase inhibitor, showing that caspases are involved in this type of apoptosis. Finally, blocking …

Programmed cell deathImmunologyCryptosporidiosisApoptosisDNA FragmentationCysteine Proteinase InhibitorsMicrobiologyCaspase-Dependent ApoptosisAmino Acid Chloromethyl KetonesCell LineImmune systemparasitic diseasesAnimalsHumansComputingMilieux_MISCELLANEOUSCaspaseCryptosporidium parvumbiologybiology.organism_classificationCaspase InhibitorsVirologyCytolysisPOUVOIR PATHOGENE[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyInfectious DiseasesCryptosporidium parvumMicroscopy FluorescenceApoptosisCaspasesbiology.proteinDNA fragmentationHeLa CellsMicrobes and Infection
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Inhibition of proteasome function induces programmed cell death in proliferating endothelial cells.

2000

Proteolysis mediated by the ubiquitin-proteasome system has been implicated in the regulation of programmed cell death. Here we investigated the differential effects of proteasomal inhibitors on the viability of proliferating and quiescent primary endothelial cells in vitro and in vivo. Subconfluent, proliferating cells underwent carbobenzoxy-L-isoleucyl-gamma-t-butyl-L-glutamyl-L-alanyl-L-leucinal (PSI) -induced apoptosis at low concentrations (EC(50)=24 nM), whereas at least 340-fold higher concentrations of PSI were necessary to obtain the same effect in confluent, contact-inhibited cells. PSI-mediated cell death could be blocked by a caspase-3 inhibitor (Ac-DEVD-H), but not by a caspase…

Programmed cell deathProteasome Endopeptidase ComplexAngiogenesisProteolysisApoptosisChick EmbryoCysteine Proteinase InhibitorsBiochemistryDogsMultienzyme ComplexesGeneticsmedicineAnimalsHumansMolecular BiologyCells Culturedmedicine.diagnostic_testChemistryCell cycleDifferential effectsCell biologyCysteine EndopeptidasesProteasomeCattleEndothelium VascularFunction (biology)Cell DivisionBiotechnologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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A membrane associated metalloprotease cleaves Cry3Aa Bacillus thuringiensis toxin reducing pore formation in Colorado potato beetle brush border memb…

2007

AbstractInsect proteases are implicated in Bacillus thuringiensis insecticidal proteins mode of action determining toxin specificity and sensitivity. Few data are available on the involvement of proteases in the later steps of toxicity such as protease interaction with toxin–receptor complexes and the pore formation process. In this study, a Colorado potato beetle (CPB) midgut membrane metalloprotease was found to be involved in the proteolytic processing of Cry3Aa. Interaction of Cry3Aa with BBMV membrane proteases resulted in a distinct pattern of proteolysis. Cleavage was demonstrated to occur in protease accessible regions of domain III and was specifically inhibited by the metalloprote…

ProteasesCell Membrane PermeabilityPore formationProteolysismedicine.medical_treatmentBacterial ToxinsBacillus thuringiensisBiophysicsInsecticidal toxinBiochemistryCry3Aa proteolysisHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineColorado potato beetleAnimalsMetalloprotease inhibitorMetalloproteinaseBinding SitesProteaseBacillus thuringiensis ToxinsMicrovillibiologymedicine.diagnostic_testSecretory VesiclesAcetohydroxamic acidColorado potato beetleCell Biologybiology.organism_classificationProteaseColeopteraEndotoxinsModels ChemicalBiochemistryPorosityProtein Bindingmedicine.drugBiochimica et Biophysica Acta (BBA) - Biomembranes
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Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors.

1996

The extracellular domains of a diverse group of membrane proteins are shed in response to protein kinase C activators such as phorbol 12-myristate 13-acetate (PMA). The lack of sequence similarity in the cleavage sites suggests the involvement of many proteases of diverse specificity in this process. However, a mutant Chinese hamster ovary cell line recently isolated for being defective in PMA-activated shedding of the membrane-anchored growth factor transforming growth factor alpha precursor (proTGF-alpha) is concomitantly defective in the shedding of many other unrelated membrane proteins. Here we show that independent mutagenesis and selection experiments yield shedding mutants having th…

ProteasesCellCHO CellsBiologyHydroxamic AcidsTransfectionBiochemistryAmyloid beta-Protein PrecursorAntigens CDCricetinaemedicineAnimalsProtease InhibitorsL-SelectinProtein PrecursorsCell adhesionMolecular BiologyProtein kinase CMetalloproteinaseChinese hamster ovary cellCell MembraneGenetic Complementation TestMembrane ProteinsMetalloendopeptidasesCell BiologyReceptors InterleukinTransforming Growth Factor alphaReceptors Interleukin-6Cell biologyKineticsmedicine.anatomical_structurePhenotypeEctodomainMembrane proteinMutagenesisTetradecanoylphorbol AcetatePhenanthrolinesThe Journal of biological chemistry
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A cellular metalloproteinase activates Vibrio cholerae pro-cytolysin.

2004

Many strains of Vibrio cholerae produce a cytolysin (VCC) that forms oligomeric transmembrane pores in animal cells. The molecule is secreted as a procytolysin (pro-VCC) of 79 kDa that must be cleaved at the N terminus to generate the active 65-kDa toxin. Processing can occur in solution, and previous studies have described the action of mature VCC thus generated. However, little is known about the properties of pro-VCC itself. In this study, it is shown that pro-VCC exist as a monomer in solution and binds as a monomer to eukaryotic cells. Bound pro-VCC can then be activated either by exogenous, extracellular, or by endogenous, cell-bound proteases. In both cases, cleavage generates the 65…

ProteasesCholera Toxingenetic structuresCHO CellsBiologyADAM17 Proteinmedicine.disease_causeBiochemistryMiceCricetinaemedicineADAM17 ProteinAnimalsHumansProtein PrecursorsMolecular BiologyFurinMetalloproteinaseCytotoxinsCell MembraneMetalloendopeptidasesCell BiologyADAM Proteinseye diseasesTransmembrane proteinADAM ProteinsBiochemistryVibrio choleraebiology.proteinsense organsCytolysinRabbitsThe Journal of biological chemistry
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