leupeptins has been researched along with 2-bromohydroquinone* in 1 studies
1 other study(ies) available for leupeptins and 2-bromohydroquinone
Article | Year |
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Proteinases in renal cell death.
The role of proteinases in renal proximal tubule (RPT) cellular death was examined using specific inhibitors of proteinases. Rabbit RPT suspensions were incubated with antimycin A for 1 h or tetrafluoroethyl-L-cysteine (TFEC) for 4 h in the absence or presence of the specific cysteine proteinase inhibitor L-trans-epoxysuccinyl-leucylamido (4-guanidino)butane (E-64), the serine proteinase inhibitors N-p-tosyl-L-lysine chloromethyl ketone (TLCK) or 3,4-dichloroisocoumarin (DCS), the serine and cysteine proteinase inhibitors leupeptin or antipain, or the aspartic proteinase inhibitor pepstatin. E-64 and pepstatin decreased lactate dehydrogenase (LDH) release, a marker of cell death, from RPT exposed either to antimycin A or TFEC. TLCK, DCS, leupeptin, or antipain did not decrease antimycin A- or TFEC-induced cell death. Bromohydroquinone- or t-butylhydroperoxide-induced cell death was not decreased by any of the proteinase inhibitors. Loss of lysosomal membrane potential, indicated by neutral red release, occurred prior to the onset of antimycin A-induced cell death. Extensive inhibition of lysosomal cathepsins B and L by E-64 was correlated with cytoprotection. However, E-64 was only protective after some cell death had occurred. These results suggest that lysosomal cysteine and aspartic proteinases, but not serine proteinases, play a role in RPT cell death induced by antimycin A or TFEC. The observation that E-64 was only protective after some cell death had occurred suggests that lysosomal cathepsins are released from dying cells and subsequently attack the remaining viable cells. Topics: Animals; Anti-Bacterial Agents; Antimycin A; Antipain; Carboxypeptidases; Cathepsin A; Cathepsin B; Cell Death; Coumarins; Cysteine; Cysteine Proteinase Inhibitors; Dose-Response Relationship, Drug; Endopeptidases; Hydrocarbons, Fluorinated; Hydroquinones; Isocoumarins; Kidney Tubules, Proximal; L-Lactate Dehydrogenase; Leucine; Leupeptins; Lysosomes; Membrane Potentials; Pepstatins; Peroxides; Rabbits; Reactive Oxygen Species; Serine Proteinase Inhibitors; tert-Butylhydroperoxide; Tosyllysine Chloromethyl Ketone | 1996 |