Search results for "cathepsin B"

showing 10 items of 38 documents

Osteoclast-like Giant Cell Tumor of the Pancreas With Ductal Adenocarcinoma: Case Report with Novel Data on Histogenesis

2002

MalePathologymedicine.medical_specialtyPancreatic diseaseEndocrinology Diabetes and MetabolismCathepsin KOsteoclastsBiologyHistogenesisCathepsin BEndocrinologyImmunophenotypingOsteoclastInternal MedicinemedicineHumansPancreatic ductHepatologyGiant Cell TumorsOsteoclast-Like Giant CellMiddle Agedmedicine.diseaseCathepsinsImmunohistochemistryPancreatic Neoplasmsmedicine.anatomical_structureAdenocarcinomaPancreasCarcinoma Pancreatic DuctalPancreas
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Association of cathepsin B gene polymorphisms with tropical calcific pancreatitis

2006

Background and aims: Tropical calcific pancreatitis (TCP) is a type of chronic pancreatitis unique to countries in the tropics. Mutations in pancreatic secretory trypsin inhibitor (SPINK1) rather than cationic trypsinogen (PRSS1) explain the disease in only 50% of TCP patients. As cathepsin B (CTSB) is known to activate cationic trypsinogen, we attempted to understand the role of CTSB mutations in TCP. Evidence of epistatic interaction was investigated with the previously associated N34S SPINK1 allele, a variant considered to be a modifier rather than a true susceptibility allele. Subjects and methods: We sequenced the coding region of CTSB gene in 51 TCP patients and 25 controls and furthe…

Malemedicine.medical_specialtyTrypsinogenSingle-nucleotide polymorphismBiologyPolymerase Chain ReactionGastroenterologyCathepsin BCathepsin Bchemistry.chemical_compoundGene FrequencyPancreatitis ChronicInternal medicinemedicineHumansGenetic Predisposition to DiseaseTrypsinogen activationAlleleAllele frequencyGeneticsPolymorphism GeneticHaplotypeGastroenterologyCase-control studyCalcinosisHaplotypesPancreatitischemistryCase-Control StudiesMutationAcute DiseaseFemaleGut
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Proteomic identification of protease cleavage sites characterizes prime and non-prime specificity of cysteine cathepsins B, L, and S.

2011

Cysteine cathepsins mediate proteome homeostasis and have pivotal functions in diseases such as cancer. To better understand substrate recognition by cathepsins B, L, and S, we applied proteomic identification of protease cleavage sites (PICS) for simultaneous profiling of prime and non-prime specificity. PICS profiling of cathepsin B endopeptidase specificity highlights strong selectivity for glycine in P3' due to an occluding loop blocking access to the primed subsites. In P1', cathepsin B has a partial preference for phenylalanine, which is not found for cathepsins L and S. Occurrence of P1' phenylalanine often coincides with aromatic residues in P2. For cathepsin L, PICS identifies 845 …

Models MolecularProteomicsTime Factorsmedicine.medical_treatmentProteolysisCathepsin LPhenylalanineGlycineBiologyBiochemistryCathepsin BPichiaCathepsin BSubstrate SpecificityCathepsin LCathepsin OPeptide LibraryCatalytic DomainmedicineHumansCathepsin SEnzyme AssaysCathepsinProteasemedicine.diagnostic_testGeneral ChemistryHydrogen-Ion ConcentrationMolecular biologyCathepsinsHEK293 CellsBiochemistryProteolysisbiology.proteinCysteinePeptide HydrolasesProtein BindingJournal of proteome research
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Development of Bimetallic Titanocene−Ruthenium−Arene Complexes As Anticancer Agents: Relationships between Structural and Biological Properties

2010

A series of bimetallic titanium-ruthenium complexes of general formula [(η(5)-C(5)H(5))(μ-η(5):κ(1)-C(5)H(4)(CR(2))(n)PR'R'')TiCl(2)](η(6)-p-cymene)RuCl(2) (n = 0, 1, 2 or 4; R = H or Me; R' = H, Ph, or Cy; R'' = Ph or Cy) have been synthesized, including two novel compounds as well as two cationic derivatives of formula [(η(5)-C(5)H(5))(μ-η(5):κ(1)-C(5)H(4)(CH(2))(n)PPh(2))TiCl(2)] [(η(6)-p-cymene)RuCl](BF(4)) (n = 0 or 2). The solid state structure of two of these compounds was also established by X-ray crystallography. The complexes showed a cytotoxic effect on human ovarian cancer cells and were markedly more active than their Ti or Ru monometallic analogues titanocene dichloride and RA…

Models MolecularStereochemistrychemistry.chemical_elementAntineoplastic AgentsCrystal structureCrystallography X-RayRutheniumCathepsin BMetalStructure-Activity Relationshipchemistry.chemical_compoundCoordination ComplexesCell Line TumorDrug DiscoveryAnimalsHumansBimetallic stripAlkylTitaniumchemistry.chemical_classificationCationic polymerizationTitanocene dichlorideRutheniumEnzymechemistryDrug Resistance Neoplasmvisual_artvisual_art.visual_art_mediumMolecular MedicineCattleDrug Screening Assays AntitumorProtein BindingJournal of Medicinal Chemistry
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Toward very potent, non-covalent organophosphonate inhibitors of cathepsin C and related enzymes by 2-amino-1-hydroxy-alkanephosphonates dipeptides

2013

Cathepsins play an important role in several human disorders and therefore the design and synthesis of their inhibitors attracts considerable interest in current medicinal chemistry approaches. Due to the presence of a strong sulphydryl nucleophile in the active center of the cysteine type cathepsins, most strategies to date have yielded covalent inhibitors. Here we present a series of non-covalent β-amino-α-hydroxyalkanephosphonate dipeptidic inhibitors of cathepsin C, ranking amongst the best low-molecular weight inhibitors of this enzyme. Their binding modes determined by molecular modelling indicate that the hydroxymethyl fragment of the molecule, not the phosphonate moiety, acts as a t…

Models MolecularStereochemistryhydroxyphosphonateBiochemistryCathepsin CCathepsin BCathepsin CInhibitory Concentration 50chemistry.chemical_compoundCathepsin OTransition state analogCathepsin KHumanscysteine proteasePeptide bondcathepsinAminesEnzyme InhibitorsCathepsinDipeptideChemistryMolecular MimicryDipeptidesGeneral MedicineOrganophosphatesEnzyme ActivationinhibitorBiochemistryHydroxy AcidsBiochimie
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Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes

2021

AbstractRhodesain is the lysosomal cathepsin L-like cysteine protease ofT. brucei rhodesiense, the causative agent of Human African Trypanosomiasis. The enzyme is essential for the proliferation and pathogenicity of the parasite as well as its ability to overcome the blood-brain barrier of the host. Lysosomal cathepsins are expressed as zymogens with an inactivating pro-domain that is cleaved under acidic conditions. A structure of the uncleaved maturation intermediate from a trypanosomal cathepsin L-like protease is currently not available. We thus established the heterologous expression ofT. brucei rhodesiensepro-rhodesain inE. coliand determined its crystal structure. The trypanosomal pr…

Models MolecularTrypanosoma brucei rhodesiense0301 basic medicinemedicine.medical_treatmentBiochemistrycysteine proteaseproenzymefluorescence correlation spectroscopy (FCS)Trypanosoma bruceiBBB blood–brain barrierCD circular dichroismchemistry.chemical_classificationEnzyme PrecursorsbiologyChemistryhsCathL human cathepsin LHydrogen-Ion ConcentrationCysteine proteaseFCS fluorescence correlation spectroscopyCysteine EndopeptidasesBiochemistryHAT Human African TrypanosomiasisNTD neglected tropical diseaseResearch Articlecrystal structureProteasesSEC size-exclusion chromatographyPET-FCS photoinduced electron transfer–fluorescence correlation spectroscopyAfrican Sleeping SicknessTrypanosoma bruceiCleavage (embryo)03 medical and health sciencesTbCathB T. brucei cathepsin BProtein DomainsZymogenmedicineMolecular BiologyzymogenrhodesainCathepsinProtease030102 biochemistry & molecular biologyActive siteTrypanosoma brucei rhodesienseCell Biologybiology.organism_classificationmolecular dynamicsEnzyme ActivationEnzyme030104 developmental biologybiology.proteinautoinhibitionHeterologous expressionJournal of Biological Chemistry
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Flow cytometric DNA analysis and lysosomal cathepsins b and l in locally advanced laryngeal cancer. Relationship with clinicopathologic parameters an…

1995

Background. The traditional factors of locally advanced laryngeal squamous cell carcinoma (LSCC) have limited predictive value for the identification of high risk patients. Therefore, it is extremely important to define prognostic factors that identify the more aggressive types. Reliable and reproducible prognostic indicators are being investigated to help clinicians identify high risk groups and address more rational treatment. Methods. Flow cytometric DNA ploidy and S-phase fraction (SPF) measurements were performed on frozen tumor tissues from a consecutive series of 71 patients with Stage III and IV LSCC. Lysosomal cathepsin B and L activity levels were determined biochemically in match…

OncologyCancer Researchmedicine.medical_specialtyUnivariate analysisPathologybiologybusiness.industryCancermedicine.diseaseCathepsin BCathepsin Lmedicine.anatomical_structureOncologyEpidermoid carcinomaInternal medicineRelative riskmedicinebiology.proteinStage (cooking)businessLymph nodeCancer
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Effects of E-64 (cysteine-proteinase inhibitor) and pepstatin (aspartyl-proteinase inhibitor) on metastasis formation in mice with mammary and ovaria…

1994

The effects of E-64 (Cathepsin B and L inhibitor) and Pepstatin A (Cathepsin D inhibitor) on spontaneous and experimental metastasis formation were investigated in mice with MCa mammary carcinoma, M5076 ovarian sarcoma and L1210 leukemia. Pepstatin induced a marked decrease in the number of spontaneous metastasis in MCa or M5076 tumor bearing mice. This phenomenon was also noted with E-64 but only in M5076 tumor bearing mice. On the other hand, both these agents were unable to prevent the formation of experimental metastasis in mice injected i.v. with L1210, MCa or M5076 tumor cells or with tumor cells in which Cathepsin B, L and D activities were inhibited by a 24 hour continuous exposure …

Ovarian NeoplasmsCathepsin LMammary Neoplasms ExperimentalpepstatinCysteine Proteinase Inhibitorsproteinase inhibitors.Cathepsin DCathepsinsCathepsinCathepsin BCysteine EndopeptidasesMiceLeucineEndopeptidasesPepstatinsTumor Cells CulturedAnimalsmetastasiFemaleNeoplasm MetastasisLeukemia L1210E-64In vivo (Athens, Greece)
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Antimetastatic activity of adriamycin in combinations with proteinase inhibitors in mice

1990

The antimetastatic activity of adriamycin in combination with proteinase inhibitors was investigated in mice bearing the metastatic tumors L1210 leukemia, Lewis lung carcinoma or M5076 sarcoma. Leupeptin, a cathepsin B inhibitor, when administered as a single agent was devoid of antimetastatic activity but some therapeutic activity was noted in mice with Lewis lung carcinoma when the agent was administered in combination with adriamysin. Pepstatin A, a cathepsin D inhibitor, had no effect as a single agent in mice with L1210 leukemia but displayed some antimetastatic activity in mice with Lewis lung carcinoma. In mice with M5076 sarcoma the combination of pepstatin A and adriamycin resulted…

Pepstatin AadriamycinLeupeptinsLeupeptinMice Inbred StrainsNeoplasms ExperimentalMetastasiCathepsin DCathepsin BMiceDoxorubicinAntineoplastic Combined Chemotherapy ProtocolsPepstatinsTumor Cells CulturedAnimalsFemaleProtease InhibitorsNeoplasm MetastasisOligopeptides
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Development of rhodesain inhibitors with a 3-bromoisoxazoline warhead

2013

Novel rhodesain inhibitors were obtained by combining an enantiomerically pure 3-bromoisoxazoline warhead with a specific peptidomimetic recognition moiety. All derivatives behaved as inhibitors of rhodesain, with low micromolar Ki values. Their activity against the enzyme was found to be paralleled by an in vitro antitrypanosomal activity, with IC50 values in the mid-micromolar range. Notably, a preference for parasitic over human proteases, specifically cathepsins B and L, was observed.

ProteasesStereochemistryPeptidomimeticCathepsin LMolecular ConformationStereoisomerismCysteine Proteinase InhibitorsBiologyCrystallography X-RayBiochemistryCysteine Proteinase InhibitorsCathepsin BCathepsin LinhibitorsDrug DiscoveryHumansMoietyGeneral Pharmacology Toxicology and PharmaceuticstrypanosomarhodesainPharmacologychemistry.chemical_classificationOrganic ChemistryStereoisomerismIsoxazolesisoxazolinesCombinatorial chemistryIn vitroCysteine EndopeptidasesEnzymechemistrypeptidomimeticsbiology.proteinMolecular Medicineinhibitors; isoxazolines; peptidomimetics; rhodesain; trypanosomaProtein Binding
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