Search results for "Pepstatin A"

showing 3 items of 3 documents

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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