Search results for "Pepstatins"

showing 5 items of 5 documents

Negative staining across holes: application to fibril and tubular structures.

2007

The negative staining technique, when used with holey carbon support films, presents superior imaging conditions than is the case when samples are adsorbed to continuous carbon films. A demonstration of this negative staining approach is presented, using ammonium molybdate in combination with trehalose, applied to several fibrillar and tubular samples. Fibrils formed from the amyloid-beta peptide and the protease inhibitor pepstain A spread very well unsupported across holes and the different polymorphic fibril forms can be readily assessed. However, tubular forms of amyloid-beta have a tendency to be flattened, due to surface tension forces prior to and during specimen drying. Sub-fibril a…

AmyloidMaterials scienceGeneral Physics and Astronomychemistry.chemical_elementFibrilNegative Stainingchemistry.chemical_compoundFerrihydriteMicroscopy Electron TransmissionStructural BiologyIron-Binding ProteinsPepstatinsAnimalsHumansNanotechnologyGeneral Materials ScienceAmmonium molybdateMolybdenumAmyloid beta-PeptidesProteinsTrehaloseCell BiologyDNATrehaloseNegative stainCarbonStainingRatsCrystallographyCarbon filmchemistryBiophysicsCollagenPeptidesCarbonMicron (Oxford, England : 1993)
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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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Pepstatins: Aspartic proteinase inhibitors having potential therapeutic applications

1993

Cathepsin D (EC 3.4.23.5) is a lysomal aspartie proteinase that is involved, under normal phusiologycal conditions, ...

Pepstatin AProteinase inhibitorCathepsin DHIV InfectionsPharmacologyCathepsin Dchemistry.chemical_compoundMiceDrug DiscoveryPepstatinsAnimalsHumanscancerPharmacologychemistry.chemical_classificationbiologylysosomal proteinasesBacterial InfectionsNeoplasms ExperimentalMuscular Dystrophy AnimalCathepsinsRatsEnzymechemistryBiochemistryEnzyme inhibitorbiology.proteinMolecular MedicineProteinase inhibitorPepstatin
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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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Kinetics of in vivo inhibition of tissue cathepsin d by pepstatin A

1988

1. 1. We have investigated the kinetics of inhibition of cathepsin D in heart, liver and skeletal muscle of CD-1 mice following administration of 25, 50, 100 and 200 mg/kg i.p. of pepstatin A, a specific inhibitor of this protease. 2. 2. In the liver, a significant inhibition of cathepsin D occurred up to at least 15 days, whereas, in heart and skeletal muscle, this inhibition lasted for a much shorter period of time. 3. 3. These results show that the recovery of enzyme activity to normal values is dose-dependent and that, at the same dose level, marked differences occur in the recovery of enzyme activity in these organ tissues, the liver being the most sensitive one. © 1988.

Pepstatin Amedicine.medical_treatmentPeriod (gene)KineticsCathepsin DBiochemistryCathepsin DMicechemistry.chemical_compoundIn vivoPepstatinsmedicineAnimalsProteasebiologyMusclesMyocardiumSkeletal muscleEnzyme assayKineticsmedicine.anatomical_structureLiverchemistryBiochemistrybiology.proteinFemaleProteinase InhibitorsOligopeptidesPepstatin
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